Any feedback?
Information on EC 3.4.21.117 - stratum corneum chymotryptic enzyme
for references in articles please use BRENDA:EC3.4.21.117Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
3.4.21.117 stratum corneum chymotryptic enzymeSpecify your search results
Word Map
- 3.4.21.117
- klk7
-
desquamation
- keratinocytes
-
cornified
- corneocyte
- netherton
-
corneodesmosomes
-
desmogleins
- corneodesmosin
-
spink5
- medicine
-
desmocollin
- vaspin
- diagnostics
- molecular biology
-
desquamatory
The enzyme appears in viruses and cellular organisms
Synonyms
kallikrein 7, stratum corneum chymotryptic enzyme, kallikrein-related peptidase 7, kallikrein-7, human stratum corneum chymotryptic enzyme, tissue kallikrein 7, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
hK7
human stratum corneum chymotryptic enzyme
kallikrein 7
kallikrein-related peptidase 7
KLK7
S01.300
-
-
-
-
SCCE
additional information
hK7
exhibits a chymotrypsin-like specificity preferring large hydrophobic or polar residues at the P1 position
kallikrein 7
-
-
-
-
kallikrein 7
-
-
kallikrein 7
-
the human kallikrein gene 7 is also known as the human stratum corneum chymotryptic enzyme
KLK7
-
-
additional information
-
KLK7 belongs to the kallikrein-related peptidase family
additional information
-
the enzyme belongs to the kallikrein subgroup of the serine protease enzyme family
additional information
-
the enzyme belongs to the multigene kallikrein serine protease family
additional information
the enzyme belongs to the human tissue kallikrein serine proteinase family
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cleavage of proteins with aromatic side chains in the P1 position
specific for amino acid residues with aromatic side chains in the P1 position
-
cleavage of proteins with aromatic side chains in the P1 position
enzyme exhibits a marked preference for cleavage downstream of Arg residues
-
cleavage of proteins with aromatic side chains in the P1 position
substrate binding pocket contains an Asn residue
cleavage of proteins with aromatic side chains in the P1 position
enzyme is a chymotrypsin-like serine protease
-
cleavage of proteins with aromatic side chains in the P1 position
enzyme is a chymotrypsin-like serine protease
cleavage of proteins with aromatic side chains in the P1 position
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
155215-90-0
-
9001-01-8
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Abz-AIKFFSA-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-AIKFF + SA-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-ALFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-ALF + SSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-FLFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-FLF + SSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-GFSPFRSSRI-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-GFSPF + RSSRI-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-GFSPFRSSRIGEIKEETT-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-GFSPF + RSSRIGEIKEETT-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-GLFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-GLF + SSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-HLFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-HLF + SSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-ILFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-ILF + SSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-KAFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-KAF + SSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-KFFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-KFF + SSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-KLFSSE-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-KLF + SSE-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-KLFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-KLF + SSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-KLTWLPL-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-KLTW + LPL-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-KLYSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-KLY + SSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-KPFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-KPF + SSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-KVFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-KVF + SSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-KYFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-KYF + SSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-LLFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-LLF + SSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-LMEKWTW-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-LMEKW + TW-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-MISLMKRP-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-MISLM + KRP-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-NLFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-NLF + SSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-PHVMRFP-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-PHVM + RFP-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-QLFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-QLF + SSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-RLFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-RLF + SSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-VARPYYL-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-VARPYY + L-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-VLFSSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-VLF + SSK-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-VQFYQGP-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-VQFY + QGP-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-VQMRGFA-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-VQM + RGF + A-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-YNPFVFT-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-YNPF + VF + T-Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Abz-YWSIQPF-Q-N-[2,4-dinitrophenyl]-ethylenediamine + H2O
Abz-Y + WSIQPF + Q-N-[2,4-dinitrophenyl]-ethylenediamine
-
-
-
?
Ac-ED(5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid)KPILFRLGK(4-(4-dimethylaminophenylazo)benzoic acid)E-NH2 + H2O
?
-
-
-
?
Ac-EFKPILWRLGC-(6-(9-oxo-9H-acridin-10-yl)-hexanoate)E-NH2 + H2O
?
-
-
-
?
acetyl-Phe-Val-Arg-4-nitroanilide + H2O
acetyl-Phe-Val-Arg + 4-nitroaniline
-
chromogenic substrate
-
-
?
benzoyl-Phe-Val-Arg-7-amido-4-methylcoumarin + H2O
benzoyl-Phe-Val-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-FR-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-FR + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-LR-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-LR + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
desmoglein 1 + H2O
?
-
kallikrein 7 cleaves both recombinant desmoglein 1 and desmoglein 2 in vitro
-
-
?
desmoglein 2 + H2O
?
-
kallikrein 7 cleaves both recombinant desmoglein 1 and desmoglein 2 in vitro. Ectopic expression of kallikrein 7 in BxPC-3 pancreatic cancer cells which express desoglein 2 but not desmoglein 1 or kallikrein 7 confirms the cleavage of desmoglein 2 in vivo
-
-
?
insulin beta chain + H2O
?
-
the most preferred P1 residue of KLK7 is Tyr, followed by Ala and Met, whereas Phe, Arg, and Lys are ranked quite low. Tyr is favored at S2 over the medium-sized hydrophobic residues Leu, Thr, Met, and Phe. In agreement with these findings, KLK7 cleaves the insulin B-chain after Asn-Gln-His-Leu, Glu-Ala-Leu-Tyr, Gly-Phe-Phe-Tyr, and Arg-Gly-Phe-Phe
-
-
?
L-Phe-7-amido-4-methylcoumarin + H2O
L-Phe + 7-amino-4-methylcoumarin
-
-
-
?
L-Tyr-7-amido-4-methylcoumarin + H2O
L-Tyr + 7-amino-4-methylcoumarin
-
-
-
?
LLVY-7-amido-4-methylcoumarin + H2O
LLVY + 7-amino-4-methylcoumarin
-
-
-
?
methoxy-succinyl-Ala-Ala-Pro-Met-4-nitroanilide + H2O
methoxy-succinyl-Ala-Ala-Pro-Met + 4-nitroaniline
methoxy-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
methoxy-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
methoxy-succinyl-Arg-Pro-Tyr-4-nitroanilide + H2O
methoxy-succinyl-Arg-Pro-Tyr + 4-nitroaniline
methoxy-succinyl-Arg-Pro-Tyr-7-amido-4-methylcoumarin + H2O
methoxy-succinyl-Arg-Pro-Tyr + 7-amino-4-methylcoumarin
-
-
-
?
methoxy-succinyl-Arg-Pro-Tyr-p-nitroanilide + H2O
methoxy-succinyl-Arg-Pro-Tyr + p-nitroaniline
-
-
-
?
N-carbobenzoxy-Gly-Pro-Arg-4-nitroanilide + H2O
N-carbobenzoxy-Gly-Pro-Arg + 4-nitroaniline
N-carbobenzoxy-Val-Gly-Arg-4-nitroanilide + H2O
N-carbobenzoxy-Val-Gly-Arg + 4-nitroaniline
o-aminobenzoyl-FRAPR-(2,4-dinitrophenyl)ethylenediamine + H2O
?
-
low activity
-
-
?
o-aminobenzoyl-FRLVR-(2,4-dinitrophenyl)ethylenediamine + H2O
o-aminobenzoyl-FR + LVR-(2,4-dinitrophenyl)ethylenediamine
-
low activity
-
?
o-aminobenzoyl-SVIRRVQ-(2,4-dinitrophenyl)ethylenediamine + H2O
?
-
-
-
-
?
o-aminobenzoyl-TSVIRRPQ-(2,4-dinitrophenyl)ethylenediamine + H2O
?
-
low activity
-
-
?
oxidized bovine insulin B chain + H2O
peptides + (Tyr)26
-
recombinant enzyme
product identification, cleavage sites are: Leu6-cysteic acid7, Tyr16-Leu17, Phe25-Tyr26, Tyr26-Tr27
?
Phe-7-amido-4-methylcoumarin + H2O
Phe + 7-amino-4-methylcoumarin
-
-
-
?
pro-matrix metalloproteinase-2 + H2O
?
-
KLK7 degrades, but does not activate, pro-matrix metalloproteinase-2
-
-
?
pro-matrix metalloproteinase-9 + H2O
matrix metalloproteinase-9
-
KLK7 degrades and activates pro-matrix metalloproteinase-9, cleavage occurs between Tyr443 and Gly444
the product is a truncated, active matrix metalloproteinase-9 lacking the C-terminal hemopexin domains which is not generated by other proteases
-
?
SANSNPAMAPRERKAGCKNFFWKTFTSC + H2O
SANSNPAMAPRERKAGCKNFF + WKTFTSC
-
-
-
?
Suc-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
Suc-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin
-
-
-
-
?
succinyl-AAPF-7-amido-4-methylcoumarin + H2O
succinyl-AAPF + 7-amino-4-methylcoumarin
-
-
-
?
succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
chromogenic substrate
-
-
?
succinyl-Ala-Ala-Pro-Phe-7-amido-4-methylcoumarin + H2O
succinyl-Ala-Ala-Pro-Phe + 7-amino-4-methylcoumarin
-
-
-
?
succinyl-Ala-Val-Pro-Phe 4-nitroanilide + H2O
succinyl-Ala-Val-Pro-Phe + 4-nitroaniline
-
-
-
?
succinyl-Leu-Leu-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-Leu-Leu-Tyr + 7-amino-4-methylcoumarin
-
-
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin
-
-
-
-
?
tert-butyloxycarbonyl-Leu-Gly-Arg-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-Leu-Gly-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
tert-butyloxycarbonyl-Phe-Ser-Arg-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-Phe-Ser-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Tyr-7-amido-4-methylcoumarin + H2O
Tyr + 7-amino-4-methylcoumarin
-
-
-
?
beta-amyloid peptide + H2O
?
-
degradation, the enzyme cleaves after both Phe residues within the core of Abeta42 in vitro, thereby inhibiting A? fibril formation and promoting the degradation of preformed fibrils
-
-
?
corneodesmosin + H2O
?
-
KLK7 degrades corneodesmosomes CDSN, DSC1, and DSG1
-
-
?
D-Ile-Pro-Arg-4-nitroanilide + H2O
D-Ile-Pro-Arg + 4-nitroaniline
-
chromogenic substrate
-
-
?
D-Ile-Pro-Arg-4-nitroanilide + H2O
D-Ile-Pro-Arg + 4-nitroaniline
-
low activity
-
-
?
D-Ile-Pro-Arg-4-nitroanilide + H2O
D-Ile-Pro-Arg + 4-nitroaniline
-
i.e. S2288
-
-
?
E-cadherin + H2O
?
-
kallikrein 7 degrades extracellular matrix proteins, and enhances pancreatic cancer cell invasion by shedding E-cadherin, overview
-
-
?
Fibronectin + H2O
?
-
kallikrein degrades components of the extracellular matrix
-
-
?
human pro-interleukin 1beta + H2O
human interleukin beta1 + ?
-
several claevage sites
product can be further degraded by the enzyme leading to its inactivation, product is in the active form
?
human pro-interleukin 1beta + H2O
human interleukin beta1 + ?
-
recombinant enzyme and substrate
product can be further degraded by the enzyme leading to its inactivation, product is in the active form
?
human pro-interleukin 1beta + H2O
human interleukin beta1 + ?
-
substrate is in the inactive form
product can be further degraded by the enzyme leading to its inactivation, product is in the active form
?
Mca-Arg-Pro-Lys-Pro-Val-Glu-Nva-Trp-Arg-Lys(Dnp)-NH2 + H2O
?
-
a fluorogenic peptide substrate
-
-
?
methoxy-succinyl-Ala-Ala-Pro-Met-4-nitroanilide + H2O
methoxy-succinyl-Ala-Ala-Pro-Met + 4-nitroaniline
-
chromogenic substrate
-
-
?
methoxy-succinyl-Ala-Ala-Pro-Met-4-nitroanilide + H2O
methoxy-succinyl-Ala-Ala-Pro-Met + 4-nitroaniline
-
low activity
-
-
?
methoxy-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
methoxy-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
chromogenic substrate
-
-
?
methoxy-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
methoxy-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
low activity
-
-
?
methoxy-succinyl-Arg-Pro-Tyr-4-nitroanilide + H2O
methoxy-succinyl-Arg-Pro-Tyr + 4-nitroaniline
-
-
-
?
methoxy-succinyl-Arg-Pro-Tyr-4-nitroanilide + H2O
methoxy-succinyl-Arg-Pro-Tyr + 4-nitroaniline
-
best substrate
-
-
?
methoxy-succinyl-Arg-Pro-Tyr-4-nitroanilide + H2O
methoxy-succinyl-Arg-Pro-Tyr + 4-nitroaniline
-
chromogenic substrate
-
-
?
methoxy-succinyl-Arg-Pro-Tyr-4-nitroanilide + H2O
methoxy-succinyl-Arg-Pro-Tyr + 4-nitroaniline
-
i.e. S2586
-
-
?
N-carbobenzoxy-Gly-Pro-Arg-4-nitroanilide + H2O
N-carbobenzoxy-Gly-Pro-Arg + 4-nitroaniline
-
chromogenic substrate
-
-
?
N-carbobenzoxy-Gly-Pro-Arg-4-nitroanilide + H2O
N-carbobenzoxy-Gly-Pro-Arg + 4-nitroaniline
-
low activity
-
-
?
N-carbobenzoxy-Val-Gly-Arg-4-nitroanilide + H2O
N-carbobenzoxy-Val-Gly-Arg + 4-nitroaniline
-
chromogenic substrate
-
-
?
N-carbobenzoxy-Val-Gly-Arg-4-nitroanilide + H2O
N-carbobenzoxy-Val-Gly-Arg + 4-nitroaniline
-
low activity
-
-
?
polypeptide + H2O
peptides
-
mediates shedding and desquamation of skin cells
-
?
polypeptide + H2O
peptides
-
involved in desquamation in plantar stratum corneum
-
?
polypeptide + H2O
peptides
-
involved in desquamation in plantar stratum corneum
-
?
polypeptide + H2O
peptides
-
involved in desquamation in plantar stratum corneum
-
?
polypeptide + H2O
peptides
-
catalyzes the degradation of intercellular cohesive structures in the cornified layer of the skin in the continous sheeding of the cells from the skin surface
-
?
polypeptide + H2O
peptides
-
catalyzes the degradation of intercellular cohesive structures in the cornified layer of the skin in the continous sheeding of the cells from the skin surface
-
?
polypeptide + H2O
peptides
involved in pathological keratinization, psoriasis, and ovarian cancer
-
?
succinyl-Phe-Leu-Phe-4-nitroanilide + H2O
succinyl-Phe-Leu-Phe + 4-nitroaniline
-
chromogenic substrate
-
-
?
succinyl-Phe-Leu-Phe-4-nitroanilide + H2O
succinyl-Phe-Leu-Phe + 4-nitroaniline
-
low activity
-
-
?
succinyl-Val-Pro-Phe-4-nitroanilide + H2O
succinyl-Val-Pro-Phe + 4-nitroaniline
-
chromogenic substrate
-
-
?
succinyl-Val-Pro-Phe-4-nitroanilide + H2O
succinyl-Val-Pro-Phe + 4-nitroaniline
-
low activity
-
-
?
additional information
?
-
-
the enzyme causes canine atopic dermatitis
-
-
?
additional information
?
-
recombinant enzyme proform is activated by digestion with trypsin
-
-
?
additional information
?
-
-
recombinant enzyme proform is activated by digestion with trypsin
-
-
?
additional information
?
-
-
enzyme may contribute to tumor cell growth, tumor spread, and the metastatic potential of ovarian tumor cells
-
-
?
additional information
?
-
AACC insertion in the stratum corneum chymotryptic enzyme gene may result in a change to activity of stratum corneum chymotryptic enzyme within the skin barrier. Stratum corneum chymotryptic enzyme could have an important role in the development of atopic dermatitis
-
-
?
additional information
?
-
-
AACC insertion in the stratum corneum chymotryptic enzyme gene may result in a change to activity of stratum corneum chymotryptic enzyme within the skin barrier. Stratum corneum chymotryptic enzyme could have an important role in the development of atopic dermatitis
-
-
?
additional information
?
-
-
epidermal hyperproliferation and decreased skin barrier function in mice overexpressing stratum corneum chymotryptic enzyme
-
-
?
additional information
?
-
-
gene expression might be involved in lung tumorigenesis
-
-
?
additional information
?
-
-
increased expression of kallikrein 7 and decreased expression of its inhibitor antileukoprotease might play an important role in cervical adenocarcinoma development
-
-
?
additional information
?
-
kallikrein 7 is involved in desquamation
-
-
?
additional information
?
-
succinyl-Ala-Ala-Pro-Phe-tripeptidyl-p-nitroanilide is no substrate
-
-
?
additional information
?
-
the most favored P1 residue of hK7 is Tyr followed by Ala, Met, and Nle, whereas Phe is ranked rather low, and Trp seems to be totally excluded, at S2, the most preferred residue is again Tyr, well ahead of the medium-sized hydrophobic residues Leu, Nle, Thr, Met, and Phe, whereas Gly is almost not tolerated, at S3 and S4, nearly all residues are accepted with a slight preference for hydrophobic side chains
-
-
?
additional information
?
-
high enzyme activity shows a significantly better prognosis in breast cancer
-
-
?
additional information
?
-
-
high enzyme activity shows a significantly better prognosis in breast cancer
-
-
?
additional information
?
-
-
kallikrein 7 is involved in pathological keratinization, psoriasis and ovarian cancer
-
-
?
additional information
?
-
-
kallikrein 7 participates in normal desquamation by facilitating cell shedding at the skin surface, and it degrades components of the extracellular matrix, the aberrant expression and secretion of kallikrein 7 in human tumors may facilitate metastasis by directly degrading components of the extracellular matrix and may thus play an important role in tumorigenesis, overview, the enzyme is implicated in the degradation of intercellular cohesive structures in the stratum corneum preceding desquamation
-
-
?
additional information
?
-
the enzyme participates in skin desquamation but is also implicated in diverse skin diseases and is a potential biomarker of ovarian cancer
-
-
?
additional information
?
-
-
the enzyme participates in skin desquamation but is also implicated in diverse skin diseases and is a potential biomarker of ovarian cancer
-
-
?
additional information
?
-
active site structure and substrate specificity, overview, kallikrein 7 exhibits large positively charged surface patches, representing putative exosites for prime side substrate recognition, overview
-
-
?
additional information
?
-
-
active site structure and substrate specificity, overview, kallikrein 7 exhibits large positively charged surface patches, representing putative exosites for prime side substrate recognition, overview
-
-
?
additional information
?
-
-
similar to KLK5, KLK7 degrades proteins of corneodesmosomes, which are most likely physiological substrates of KLKs expressed in the stratum corneum of skin
-
-
?
additional information
?
-
the P3-P'3' sequence NLYRVR is identified as a preferred substrate for the enzyme, glutamate at position P3' is also well accepted, substrate specificity, overview. No activity with Abz-KVYFFFRENAI-Q-N-[2,4-dinitrophenyl]-ethylenediamine. Kininogenase activity of the enzyme using as substrate a synthetic peptide derived from human kininogen (Abz-MISLMKRPPGFSPFRSSRI-NH2) containing the amino acids F and M as two possible cleavage site
-
-
?
additional information
?
-
-
the P3-P'3' sequence NLYRVR is identified as a preferred substrate for the enzyme, glutamate at position P3' is also well accepted, substrate specificity, overview. No activity with Abz-KVYFFFRENAI-Q-N-[2,4-dinitrophenyl]-ethylenediamine. Kininogenase activity of the enzyme using as substrate a synthetic peptide derived from human kininogen (Abz-MISLMKRPPGFSPFRSSRI-NH2) containing the amino acids F and M as two possible cleavage site
-
-
?
additional information
?
-
recombinant KLK7 clearly shows Tyr over Phe preference at the P1 site. No activity is detected against substrates with Lys or Ala in P1 sites, and minimum activity (about 10% activity compared with trypsin-like KLKs) is observed against substrates with Arg in the P1 site
-
-
?
additional information
?
-
-
recombinant KLK7 clearly shows Tyr over Phe preference at the P1 site. No activity is detected against substrates with Lys or Ala in P1 sites, and minimum activity (about 10% activity compared with trypsin-like KLKs) is observed against substrates with Arg in the P1 site
-
-
?
additional information
?
-
KLK7 exerts chymotryptic-like cleavage preferences. KLK7 subsite preferences are also characterised in the P2-P2 region, demonstrating a preference for hydrophobic residues in the non-prime and hydrophilic residues in the prime subsites
-
-
?
additional information
?
-
-
KLK7 exerts chymotryptic-like cleavage preferences. KLK7 subsite preferences are also characterised in the P2-P2 region, demonstrating a preference for hydrophobic residues in the non-prime and hydrophilic residues in the prime subsites
-
-
?
additional information
?
-
-
enzyme exhibits a marked preference for cleavage downstream of Arg residues
-
-
?
additional information
?
-
-
the enzyme shows a unique extended chymotrypsin-like specificity and beta-amyloid peptide-degrading capacity
-
-
?
additional information
?
-
-
the enzyme's consensus motif is RX0(Y/F)-/-(Y/F)-/-(S/A/G/T) or RX0(Y/F)-/-(S/T/A) (0 = hydrophobic)
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
beta-amyloid peptide + H2O
?
-
degradation, the enzyme cleaves after both Phe residues within the core of Abeta42 in vitro, thereby inhibiting A? fibril formation and promoting the degradation of preformed fibrils
-
-
?
E-cadherin + H2O
?
-
kallikrein 7 degrades extracellular matrix proteins, and enhances pancreatic cancer cell invasion by shedding E-cadherin, overview
-
-
?
Fibronectin + H2O
?
-
kallikrein degrades components of the extracellular matrix
-
-
?
polypeptide + H2O
peptides
-
mediates shedding and desquamation of skin cells
-
?
polypeptide + H2O
peptides
-
involved in desquamation in plantar stratum corneum
-
?
polypeptide + H2O
peptides
-
involved in desquamation in plantar stratum corneum
-
?
polypeptide + H2O
peptides
-
involved in desquamation in plantar stratum corneum
-
?
polypeptide + H2O
peptides
-
catalyzes the degradation of intercellular cohesive structures in the cornified layer of the skin in the continous sheeding of the cells from the skin surface
-
?
polypeptide + H2O
peptides
-
catalyzes the degradation of intercellular cohesive structures in the cornified layer of the skin in the continous sheeding of the cells from the skin surface
-
?
polypeptide + H2O
peptides
involved in pathological keratinization, psoriasis, and ovarian cancer
-
?
additional information
?
-
-
the enzyme causes canine atopic dermatitis
-
-
?
additional information
?
-
-
enzyme may contribute to tumor cell growth, tumor spread, and the metastatic potential of ovarian tumor cells
-
-
?
additional information
?
-
AACC insertion in the stratum corneum chymotryptic enzyme gene may result in a change to activity of stratum corneum chymotryptic enzyme within the skin barrier. Stratum corneum chymotryptic enzyme could have an important role in the development of atopic dermatitis
-
-
?
additional information
?
-
-
AACC insertion in the stratum corneum chymotryptic enzyme gene may result in a change to activity of stratum corneum chymotryptic enzyme within the skin barrier. Stratum corneum chymotryptic enzyme could have an important role in the development of atopic dermatitis
-
-
?
additional information
?
-
-
epidermal hyperproliferation and decreased skin barrier function in mice overexpressing stratum corneum chymotryptic enzyme
-
-
?
additional information
?
-
-
gene expression might be involved in lung tumorigenesis
-
-
?
additional information
?
-
-
increased expression of kallikrein 7 and decreased expression of its inhibitor antileukoprotease might play an important role in cervical adenocarcinoma development
-
-
?
additional information
?
-
kallikrein 7 is involved in desquamation
-
-
?
additional information
?
-
high enzyme activity shows a significantly better prognosis in breast cancer
-
-
?
additional information
?
-
-
high enzyme activity shows a significantly better prognosis in breast cancer
-
-
?
additional information
?
-
-
kallikrein 7 is involved in pathological keratinization, psoriasis and ovarian cancer
-
-
?
additional information
?
-
-
kallikrein 7 participates in normal desquamation by facilitating cell shedding at the skin surface, and it degrades components of the extracellular matrix, the aberrant expression and secretion of kallikrein 7 in human tumors may facilitate metastasis by directly degrading components of the extracellular matrix and may thus play an important role in tumorigenesis, overview, the enzyme is implicated in the degradation of intercellular cohesive structures in the stratum corneum preceding desquamation
-
-
?
additional information
?
-
the enzyme participates in skin desquamation but is also implicated in diverse skin diseases and is a potential biomarker of ovarian cancer
-
-
?
additional information
?
-
-
the enzyme participates in skin desquamation but is also implicated in diverse skin diseases and is a potential biomarker of ovarian cancer
-
-
?
additional information
?
-
recombinant KLK7 clearly shows Tyr over Phe preference at the P1 site. No activity is detected against substrates with Lys or Ala in P1 sites, and minimum activity (about 10% activity compared with trypsin-like KLKs) is observed against substrates with Arg in the P1 site
-
-
?
additional information
?
-
-
recombinant KLK7 clearly shows Tyr over Phe preference at the P1 site. No activity is detected against substrates with Lys or Ala in P1 sites, and minimum activity (about 10% activity compared with trypsin-like KLKs) is observed against substrates with Arg in the P1 site
-
-
?
additional information
?
-
-
the enzyme shows a unique extended chymotrypsin-like specificity and beta-amyloid peptide-degrading capacity
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Sodium citrate
inhibits the enzyme at up to 750 mM, but not at higher concentrations
Sodium sulfate
inhibits the enzyme at up to 1000 mM, but not at higher concentrations
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(4R)-4-benzyl-2-(2-methylphenyl)-3,4-dihydro-5H-pyrido[10,20:1,2]imidazo[4,5-d][1,3]diazepin-5-one
-
-
(4S)-4-(1-naphthyl)methyl-2-(2-methylphenyl)-3,4-dihydro-5H-pyrido[10,20:1,2] imidazo[4,5-d][1,3]diazepin-5-one
-
-
(4S)-4-(4-benzyloxy)benzyl-2-(3,4-dimethoxyphenyl)-3,4-dihydro-5H-pyrido [10,20:1,2]imidazo[4,5-d][1,3]diazepin-5-one
-
-
(4S)-4-(4-hydroxyphenyl)-2-(3,4-dimethoxyphenyl)-3,4-dihydro-5H-pyrido [10,20:1,2]imidazo[4,5-d][1,3]diazepin-5-one
-
-
(4S)-4-benzyl-2-(2,4-dimethylphenyl)-3,4-dihydro-5Hpyrido[10,20:1,2]imidazo [4,5-d][1,3]diazepin-5-one
-
cytotoxic effect
(4S)-4-benzyl-2-(2,5-dihydroxyphenyl)-3,4-dihydro-5Hpyrido[10,20:1,2]imidazo-[4,5-d][1,3]diazepin-5-one
-
-
(4S)-4-benzyl-2-(2,5-dimethoxyphenyl)-3,4-dihydro-5Hpyrido[10,20:1,2]imidazo [4,5-d][1,3]diazepin-5-one
-
cytotoxic effect
(4S)-4-benzyl-2-(2-hydroxyphenyl)-3,4-dihydro-5H-pyrido[10,20:1,2]imidazo-[4,5-d][1,3]diazepin-5-one
-
-
(4S)-4-benzyl-2-(2-methoxyphenyl)-3,4-dihydro-5H-pyrido[10,20:1,2]imidazo[4,5-d][1,3]diazepin-5-one
-
-
(4S)-4-benzyl-2-(2-methylphenyl)-3,4-dihydro-5H-pyrido[1',2':1,2]imidazo[4,5-d][1,3]diazepin-5-one
-
-
(4S)-4-benzyl-2-(2-methylpropyl)-3,4-dihydro-5H-pyrido[1',2':1,2]imidazo[4,5-d][1,3]diazepin-5-one
-
-
(4S)-4-benzyl-2-(3,4,5-trimethoxyphenyl)-3,4-dihydro-5Hpyrido[10,20:1,2] imidazo[4,5-d][1,3]diazepin-5-one
-
cytotoxic effect
(4S)-4-benzyl-2-(3,4-dimethoxyphenyl)-3,4-dihydro-5Hpyrido[10,20:1,2]imidazo [4,5-d][1,3]diazepin-5-one
-
mechanism of inhibition, modeling, overview. Cytotoxic effect
(4S)-4-benzyl-2-(3,4-dimethoxyphenyl)-4,5-dihydro-3H-pyrido [10,20:1,2]imidazo[4,5-d][1,3]diazepin-5-ol
-
-
(4S)-4-benzyl-2-(3-hydroxyphenyl)-3,4-dihydro-5H-pyrido[10,20:1,2]imidazo-[4,5-d][1,3]diazepin-5-one
-
-
(4S)-4-benzyl-2-(3-methoxyphenyl)-3,4-dihydro-5H-pyrido[10,20:1,2]imidazo[4,5-d][1,3]diazepin-5-one
-
-
(4S)-4-benzyl-2-(3-methylphenyl)-3,4-dihydro-5H-pyrido[1',2':1,2]imidazo[4,5-d][1,3]diazepin-5-one
-
-
(4S)-4-benzyl-2-(4-bromophenyl)-3,4-dihydro-5H-pyrido[1',2':1,2]imidazo[4,5-d][1,3]diazepin-5-one
-
-
(4S)-4-benzyl-2-(4-methoxyphenyl)-3,4-dihydro-5H-pyrido[1',2':1,2]imidazo[4,5-d][1,3]diazepin-5-one
-
-
(4S)-4-benzyl-2-(4-methylphenyl)-3,4-dihydro-5H-pyrido[1',2':1,2]imidazo[4,5-d][1,3]diazepin-5-one
-
-
(4S)-4-benzyl-2-(4-nitrophenyl)-3,4-dihydro-5H-pyrido[1',2':1,2]imidazo[4,5-d][1,3]diazepin-5-one
-
-
(4S)-4-benzyl-2-(pyridin-3-yl)-3,4-dihydro-5H-pyrido[1',2':1,2]imidazo[4,5-d][1,3]diazepin-5-one
-
-
(4S)-4-benzyl-2-phenyl-3,4-dihydro-5H-pyrido[1',2':1,2]imidazo[4,5-d][1,3]diazepin-5-one
-
-
(4S)-4-benzyl-3,4-dihydro-1H-pyrido[1',2':1,2]imidazo[4,5-d][1,3]diazepine-2,5-dione
-
-
(4S)-4-benzyloxymethyl-2-(2-methylphenyl)-3,4-dihydro-5H-pyrido[10,20:1,2] imidazo[4,5-d][1,3]diazepin-5-one
-
-
(4S)-4-benzyloxymethyl-2-(3,4-dimethoxyphenyl)-3,4-dihydro-5H-pyrido [10,20:1,2]imidazo[4,5-d][1,3]diazepin-5-one
-
-
(4S)-4-hydroxymethyl-2-(3,4-dimethoxyphenyl)-3,4-dihydro-5H-pyrido[10,20:1,2] imi-dazo[4,5-d][1,3]diazepin-5-one
-
-
(4S)-4-methyl-2-(2-methylphenyl)-3,4-dihydro-5H-pyrido[10,20:1,2]-imidazo[4,5-d][1,3]diazepin-5-one
-
-
(4S)-4-methyl-2-(3,4-dimethoxyphenyl)-3,4-dihydro-5Hpyrido[10,20:1,2] imidazo[4,5-d][1,3]diazepin-5-one
-
-
(S)-4-benzyl-2-(3,4-dimethoxyphenyl)-3-methyl-3H-pyrido[10,20:1,2]imidazo [4,5-d][1,3]diazepin-5(4H)-one
-
-
(S)-N-(1-(2-amino-imidazo[1,2-a]pyridin-3-yl)-1-oxo-3-phenylpropan-2-yl)-1H-pyrrole-2-carboxamide
-
-
(S)-N-(1-(2-amino-imidazo[1,2-a]pyridin-3-yl)-1-oxo-3-phenylpropan-2-yl)-2-methylbenzamide
-
-
(S)-N-(1-(2-amino-imidazo[1,2-a]pyridin-3-yl)-1-oxo-3-phenylpropan-2-yl)-2-phenylacetamide
-
-
(S)-N-(1-(2-amino-imidazo[1,2-a]pyridin-3-yl)-1-oxo-3-phenylpropan-2-yl)-3,4-dimethoxybenzamide
-
-
(S)-N-(1-(2-amino-imidazo[1,2-a]pyridin-3-yl)-1-oxo-3-phenylpropan-2-yl)-3-phenylpropanamide
-
-
(S)-N-(1-(2-amino-imidazo[1,2-a]pyridin-3-yl)-1-oxo-3-phenylpropan-2-yl)benzamide
-
-
(S)-N-(1-(2-amino-imidazo[1,2-a]pyridin-3-yl)-1-oxo-3-phenylpropan-2-yl)cinnamamide
-
-
(S)-N-(1-(2-amino-imidazo[1,2-a]pyridin-3-yl)-1-oxo-3-phenylpropan-2-yl)isonicotinamide
-
-
(S)-N-(1-(2-amino-imidazo[1,2-a]pyridin-3-yl)-1-oxo-3-phenylpropan-2-yl)picolinamide
-
-
1-(2-bromobenzene-1-sulfonyl)-5-methyl-3-(2-methyl-4,5-dihydro-1H-imidazol-4-yl)-1H-indole
1-(2-chlorobenzene-1-sulfonyl)-5-methyl-3-(2-methyl-4,5-dihydro-1H-imidazol-4-yl)-1H-indole
2-(2-fluoro-phenyl)-5,6,7,8-tertrahydro-benzol[4,5]thieno[2,3-d][1,3]oxazin-4-one
-
Cu2+
inhibition at low micromolar concentrations, structural basis for inhibition, overview; strong inhibitory effect
DMSO
catalytic activity of the protease decreases with increasing DMSO concentration
GKCLFSNPPICFPN
peptide inhibitor based on sunflower trypsin inhibitor-1, displays at least 1000fold selectivity over several proteases that are related by function (KLK5 and KLK14) or specificity (chymotrypsin)
LEKTI domain 6
i.e. lympho-epithelial Kazaltype-related inhibitor domain 6, specific inhibition, interaction and binding structure analysis, overview
-
LEKTI fragments
-
i.e. lympho-epithelial Kazaltype-related inhibitor fragments, furin-derived and secreted in cultured keratinocytes and in the epidermis, specifically inhibit KLK5, KLK7, and KLK14 and control desquamation through a pH-dependent interaction, overview
-
1-(2-bromobenzene-1-sulfonyl)-5-methyl-3-(2-methyl-4,5-dihydro-1H-imidazol-4-yl)-1H-indole
-
1-(2-bromobenzene-1-sulfonyl)-5-methyl-3-(2-methyl-4,5-dihydro-1H-imidazol-4-yl)-1H-indole
-
1-(2-chlorobenzene-1-sulfonyl)-5-methyl-3-(2-methyl-4,5-dihydro-1H-imidazol-4-yl)-1H-indole
-
1-(2-chlorobenzene-1-sulfonyl)-5-methyl-3-(2-methyl-4,5-dihydro-1H-imidazol-4-yl)-1H-indole
-
chymostatin
-
proteolysis of both the desmosomal proteins by kallikrein 7 is effectively inhibited in the presence of chymostatin
LEKTI
-
i.e. lympho-epithelial Kazaltype-related inhibitor, a 15-domain serine proteinase inhibitor
LEKTI
-
LEKTI is expressed in stratum corneum and in stratum granulosum and is a reversible inhibitor encoded by the SPINK5 (serine protease inhibitor Kazal type 5) gene. LEKTI is a weak inhibitor toward KLK 7 but a much stronger inhibitor toward KLK5
Zn2+
inhibition at low micromolar concentrations, noncompetitive inhibition type, structural basis for inhibition involving His99, overview; strong inhibitory effect
additional information
-
inhibition assay: 15 min preincubation of the enzyme with inhibitor at 21°C; no inhibition by Mg2+, E-64, 1,10-phenanthrolin, EDTA
-
additional information
-
phosphoramidon inhibits thermolysin and thus activation of pro-kallikrein 7
-
additional information
-
phosphoramidon inhibits thermolysin and thus activation of pro-kallikrein 7
-
additional information
-
usage of the pyridoimidazodiazepinone core as a potential scaffold to develop selective and competitive reversible inhibitors, analysis of structure-activity relationships, inhibition mechanisms, and selectivity as well as cytotoxicity against selected three human cancer cell lines, i.e. the HeLa cells, prostatic PC-3 cell line, and colorectal adenocarcinoma SW-620 cells, structure-based molecular docking, overview. No inhibition by 1b, 1f, 1g, 1h, 1i, 1j, 1l, 1m, 1q, 1r, 1s, 1t, 1u, 1v, 1w, 1x, 1z, 1aa, 1ab, 1ac, 1ad, 2a, 2b, 2c, 2d, 2f, 2h, and 2i
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
estrogen and glucocorticoids cause up-regulation of gene expression
-
additional information
estrogen and glucocorticoids cause up-regulation of gene expression
-
additional information
-
estrogen and glucocorticoids cause up-regulation of gene expression
-
additional information
-
KLK7 is activated by proteolytic cleavage through meprin alpha and beta, and through trypsin, overview. Cleavage by meprins enhances activation of LKL7 through trypsin
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Adenocarcinoma
Expression of human kallikrein 7 (hK7/SCCE) and its inhibitor antileukoprotease (ALP/SLPI) in uterine endocervical glands and in cervical adenocarcinomas.
Adenocarcinoma
Expression of kallikrein-related peptidase 7 predicts poor prognosis in patients with unresectable pancreatic ductal adenocarcinoma.
Adenocarcinoma
Kallikrein 7 enhances pancreatic cancer cell invasion by shedding E-cadherin.
Adenocarcinoma
The extracellular matrix protein fibronectin is a substrate for kallikrein 7.
Alzheimer Disease
Altered kallikrein 7 and 10 concentrations in cerebrospinal fluid of patients with Alzheimer's disease and frontotemporal dementia.
Alzheimer Disease
Loss of kallikrein-related peptidase 7 exacerbates amyloid pathology in Alzheimer's disease model mice.
Breast Neoplasms
Evaluation of Kallikrein-related Peptidase 5 Expression and its Significance for Breast Cancer Patients: Association with Kallikrein-related Peptidase 7 Expression.
Breast Neoplasms
Expression analysis of the human kallikrein 7 (KLK7) in breast tumors: a new potential biomarker for prognosis of breast carcinoma.
Breast Neoplasms
Expression of the serine protease kallikrein 7 and its inhibitor antileukoprotease is decreased in prostate cancer.
Breast Neoplasms
Quantitative reverse transcription-PCR assay for detection of mRNA encoding full-length human tissue kallikrein 7: prognostic relevance of KLK7 mRNA expression in breast cancer.
Carcinogenesis
Analysis of human kallikrein 7 expression as a potential biomarker in cervical neoplasia.
Carcinogenesis
Kallikrein-related peptidase 7 (KLK7) is a proliferative factor that is aberrantly expressed in human colon cancer.
Carcinoma
Expression of the protease inhibitor antileukoprotease and the serine protease stratum corneum chymotryptic enzyme (SCCE) is coordinated in ovarian tumors.
Carcinoma
Human kallikrein 7 induces epithelial-mesenchymal transition-like changes in prostate carcinoma cells: a role in prostate cancer invasion and progression.
Carcinoma
Human tissue kallikrein 7, a novel biomarker for advanced ovarian carcinoma using a novel in situ quantitative method of protein expression.
Carcinoma
Kallikrein-related peptidase 7 promotes multicellular aggregation via the alpha(5)beta(1) integrin pathway and paclitaxel chemoresistance in serous epithelial ovarian carcinoma.
Carcinoma
The Co-Expression of Kallikrein 5 and Kallikrein 7 Associates with Poor Survival in Non-HPV Oral Squamous-Cell Carcinoma.
Carcinoma, Ovarian Epithelial
Kallikrein-related peptidase 7 promotes multicellular aggregation via the alpha(5)beta(1) integrin pathway and paclitaxel chemoresistance in serous epithelial ovarian carcinoma.
cathepsin l deficiency
Epidermal differentiation: the role of proteases and their inhibitors.
Colonic Neoplasms
Kallikrein-related peptidase 7 (KLK7) is a proliferative factor that is aberrantly expressed in human colon cancer.
Colorectal Neoplasms
Clinical significance of kallikrein-related peptidase 7 (KLK7) in colorectal cancer.
Dermatitis
Epidermal overexpression of stratum corneum chymotryptic enzyme in mice: a model for chronic itchy dermatitis.
Dermatitis, Atopic
Epidermal overexpression of stratum corneum chymotryptic enzyme in mice: a model for chronic itchy dermatitis.
Dermatitis, Atopic
Evaluation of kallikrein 7 as a disease-causing gene for canine atopic dermatitis using microsatellite-based association mapping.
Dermatitis, Atopic
Generation of a quenched phosphonate activity-based probe for labelling the active KLK7 protease.
Dermatitis, Atopic
Genetic association between an AACC insertion in the 3'UTR of the stratum corneum chymotryptic enzyme gene and atopic dermatitis.
Dermatitis, Atopic
TH2 cytokines increase kallikrein 7 expression and function in patients with atopic dermatitis.
Dermatitis, Atopic
The 3'-UTR AACCins5874 in the stratum corneum chymotryptic enzyme gene (SCCE/KLK7), associated with atopic dermatitis; causes an increased mRNA expression without altering its stability.
Eczema
Analysis of the individual and aggregate genetic contributions of previously identified serine peptidase inhibitor Kazal type 5 (SPINK5), kallikrein-related peptidase 7 (KLK7), and filaggrin (FLG) polymorphisms to eczema risk.
Eczema
Transcriptional gene silencing of kallikrein 5 and kallikrein 7 using siRNA prevents epithelial cell detachment induced by alkaline shock in an in vitro model of eczema.
Frontotemporal Dementia
Altered kallikrein 7 and 10 concentrations in cerebrospinal fluid of patients with Alzheimer's disease and frontotemporal dementia.
Ichthyosis
Expression of stratum corneum chymotryptic enzyme in ichthyoses and squamoproliferative processes.
Ichthyosis
Skin Barrier Function Is Not Impaired and Kallikrein 7 Gene Polymorphism Is Frequently Observed in Korean X-linked Ichthyosis Patients Diagnosed by Fluorescence in Situ Hybridization and Array Comparative Genomic Hybridization.
Melanoma
Aberrant expression of kallikrein-related peptidase 7 is correlated with human melanoma aggressiveness by stimulating cell migration and invasion.
Melanoma
Cell adhesion and communication proteins are differentially expressed in melanoma progression model.
Melanoma
Kallikrein-related peptidase 7 overexpression in melanoma cells modulates cell adhesion leading to a malignant phenotype.
Neoplasm Metastasis
Analysis of human kallikrein 7 expression as a potential biomarker in cervical neoplasia.
Neoplasms
3D-quantitative structure-activity relationship and docking studies of coumarin derivatives as tissue kallikrein 7 inhibitors.
Neoplasms
An unexpected switch in peptide binding mode: from simulation to substrate specificity.
Neoplasms
Analysis of human kallikrein 7 expression as a potential biomarker in cervical neoplasia.
Neoplasms
Definition of an immunogenic region within the ovarian tumor antigen stratum corneum chymotryptic enzyme.
Neoplasms
Discovery, Synthesis, Pharmacological Profiling, and Biological Characterization of Brintonamides A-E, Novel Dual Protease and GPCR Modulators from a Marine Cyanobacterium.
Neoplasms
Experiment research of cisplatin implants inhibiting transplantation tumor growth and regulating the expression of KLK7 and E-cad of tumor-bearing mice with gastric cancer.
Neoplasms
Expression of kallikrein 7 diminishes pancreatic cancer cell adhesion to vitronectin and enhances urokinase-type plasminogen activator receptor shedding.
Neoplasms
Expression of the protease inhibitor antileukoprotease and the serine protease stratum corneum chymotryptic enzyme (SCCE) is coordinated in ovarian tumors.
Neoplasms
Immunohistochemical localization and analysis of kallikrein-related peptidase 7 and 11 expression in paired cancer and benign foci in prostate cancer patients.
Neoplasms
Kallikrein-related peptidase 7 (KLK7) is a proliferative factor that is aberrantly expressed in human colon cancer.
Neoplasms
Parallel underexpression of kallikrein 5 and kallikrein 7 mRNA in breast malignancies.
Neoplasms
The serine protease stratum corneum chymotryptic enzyme (kallikrein 7) is highly overexpressed in squamous cervical cancer cells.
Neoplasms
The stratum corneum chymotryptic enzyme that mediates shedding and desquamation of skin cells is highly overexpressed in ovarian tumor cells.
Netherton Syndrome
Generation of a quenched phosphonate activity-based probe for labelling the active KLK7 protease.
Netherton Syndrome
SPINK5 knockdown in organotypic human skin culture as a model system for Netherton syndrome: effect of genetic inhibition of serine proteases kallikrein 5 and kallikrein 7.
Nevus
Cell adhesion and communication proteins are differentially expressed in melanoma progression model.
Obesity
Ablation of kallikrein 7 (KLK7) in adipose tissue ameliorates metabolic consequences of high fat diet-induced obesity by counteracting adipose tissue inflammation in vivo.
Ovarian Neoplasms
Clinical value of protein expression of kallikrein-related peptidase 7 (KLK7) in ovarian cancer.
Ovarian Neoplasms
Crystallization and preliminary crystallographic studies of human kallikrein 7, a serine protease of the multigene kallikrein family.
Ovarian Neoplasms
Expression of the protease inhibitor antileukoprotease and the serine protease stratum corneum chymotryptic enzyme (SCCE) is coordinated in ovarian tumors.
Ovarian Neoplasms
Human tissue kallikrein 7, a novel biomarker for advanced ovarian carcinoma using a novel in situ quantitative method of protein expression.
Ovarian Neoplasms
Integration of two in-depth quantitative proteomics approaches determines the kallikrein-related peptidase 7 (KLK7) degradome in ovarian cancer cell secretome.
Ovarian Neoplasms
Prognostic value of kallikrein-related peptidase 7 (KLK7) mRNA expression in advanced high-grade serous ovarian cancer.
Ovarian Neoplasms
Unfavorable prognostic value of human kallikrein 7 quantified by ELISA in ovarian cancer cytosols.
Pancreatic Neoplasms
Expression of kallikrein 7 diminishes pancreatic cancer cell adhesion to vitronectin and enhances urokinase-type plasminogen activator receptor shedding.
Pancreatic Neoplasms
Kallikrein 7 enhances pancreatic cancer cell invasion by shedding E-cadherin.
Pancreatic Neoplasms
Kallikrein-related peptidase 7 is a potential target for the treatment of pancreatic cancer.
Papillon-Lefevre Disease
Epidermal differentiation: the role of proteases and their inhibitors.
Prostatic Neoplasms
Expression of kallikrein-related peptidase 7 is decreased in prostate cancer.
Prostatic Neoplasms
Expression of the serine protease kallikrein 7 and its inhibitor antileukoprotease is decreased in prostate cancer.
Prostatic Neoplasms
Human kallikrein 7 induces epithelial-mesenchymal transition-like changes in prostate carcinoma cells: a role in prostate cancer invasion and progression.
Prostatic Neoplasms
Immunohistochemical localization and analysis of kallikrein-related peptidase 7 and 11 expression in paired cancer and benign foci in prostate cancer patients.
Pruritus
Epidermal overexpression of stratum corneum chymotryptic enzyme in mice: a model for chronic itchy dermatitis.
Psoriasis
Crystallization and preliminary crystallographic studies of human kallikrein 7, a serine protease of the multigene kallikrein family.
Psoriasis
Epidermal overexpression of stratum corneum chymotryptic enzyme in mice: a model for chronic itchy dermatitis.
Skin Diseases
A fluorescence lifetime-based assay for protease inhibitor profiling on human kallikrein 7.
Skin Diseases
A novel theranostic activity-based probe targeting kallikrein 7 for the diagnosis and treatment of skin diseases.
Skin Diseases
An unexpected switch in peptide binding mode: from simulation to substrate specificity.
Skin Diseases
Epidermal overexpression of stratum corneum chymotryptic enzyme in mice: a model for chronic itchy dermatitis.
Skin Diseases
Generation of a quenched phosphonate activity-based probe for labelling the active KLK7 protease.
Skin Diseases
Generation of recombinant antibodies against human tissue kallikrein 7 to treat skin diseases.
Skin Diseases
Pyrido-imidazodiazepinones as a new class of reversible inhibitors of human kallikrein 7.
Squamous Cell Carcinoma of Head and Neck
Immunohistochemical expression of kallikrein 7 in oral squamous cell carcinoma.
Stomach Neoplasms
Experiment research of cisplatin implants inhibiting transplantation tumor growth and regulating the expression of KLK7 and E-cad of tumor-bearing mice with gastric cancer.
Uterine Cervical Neoplasms
Serum human kallikrein 7 represents a new marker for cervical cancer.
Uterine Cervical Neoplasms
The serine protease stratum corneum chymotryptic enzyme (kallikrein 7) is highly overexpressed in squamous cervical cancer cells.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.002
Abz-GFSPFRSSRI-Q-N-[2,4-dinitrophenyl]-ethylenediamine
pH 7.5, 37°C
0.069
Abz-GFSPFRSSRIGEIKEETT-Q-N-[2,4-dinitrophenyl]-ethylenediamine
pH 7.5, 37°C
0.0059
Ac-ED(5-[(2-aminoethyl)amino]naphthalene-1-sulfonic acid)KPILFRLGK(4-(4-dimethylaminophenylazo)benzoic acid)E-NH2
kcat/KM: 170000/Msec
0.048
Ac-EFKPILWRLGC-(6-(9-oxo-9H-acridin-10-yl)-hexanoate)E-NH2
Vmax: 12 nM/sec
0.0443
L-Phe-7-amido-4-methylcoumarin
in 50 mM HEPES, pH 7.5, 150 mM NaCl, 0.005% Tween 20, at 25°C
0.0402
L-Tyr-7-amido-4-methylcoumarin
in 50 mM HEPES, pH 7.5, 150 mM NaCl, 0.005% Tween 20, at 25°C
0.304
methoxy-succinyl-Arg-Pro-Tyr-7-amido-4-methylcoumarin
wild-type, pH 8.0, temperature not specified in the publication
0.43
methoxy-succinyl-Arg-Pro-Tyr-7-amido-4-methylcoumarin
mutant S195A, pH 8.0, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1
Abz-GFSPFRSSRIGEIKEETT-Q-N-[2,4-dinitrophenyl]-ethylenediamine
pH 7.5, 37°C
0.000016
L-Phe-7-amido-4-methylcoumarin
in 50 mM HEPES, pH 7.5, 150 mM NaCl, 0.005% Tween 20, at 25°C
0.000033
L-Tyr-7-amido-4-methylcoumarin
in 50 mM HEPES, pH 7.5, 150 mM NaCl, 0.005% Tween 20, at 25°C
0.34
methoxy-succinyl-Arg-Pro-Tyr-7-amido-4-methylcoumarin
mutant S195A, pH 8.0, temperature not specified in the publication
24.5
methoxy-succinyl-Arg-Pro-Tyr-7-amido-4-methylcoumarin
wild-type, pH 8.0, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
14
Abz-GFSPFRSSRIGEIKEETT-Q-N-[2,4-dinitrophenyl]-ethylenediamine
pH 7.5, 37°C
0.79
methoxy-succinyl-Arg-Pro-Tyr-7-amido-4-methylcoumarin
mutant S195A, pH 8.0, temperature not specified in the publication
80.8
methoxy-succinyl-Arg-Pro-Tyr-7-amido-4-methylcoumarin
wild-type, pH 8.0, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
inhibition kinetics with LEKTi fragments, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0959
(4R)-4-benzyl-2-(2-methylphenyl)-3,4-dihydro-5H-pyrido[10,20:1,2]imidazo[4,5-d][1,3]diazepin-5-one
Homo sapiens
-
pH 8..0, 37°C
0.0839
(4S)-4-benzyl-2-(2,4-dimethylphenyl)-3,4-dihydro-5Hpyrido[10,20:1,2]imidazo [4,5-d][1,3]diazepin-5-one
Homo sapiens
-
pH 8..0, 37°C
0.0809
(4S)-4-benzyl-2-(2,5-dimethoxyphenyl)-3,4-dihydro-5Hpyrido[10,20:1,2]imidazo [4,5-d][1,3]diazepin-5-one
Homo sapiens
-
pH 8..0, 37°C
0.057
(4S)-4-benzyl-2-(2-methylphenyl)-3,4-dihydro-5H-pyrido[1',2':1,2]imidazo[4,5-d][1,3]diazepin-5-one
Homo sapiens
-
pH 8..0, 37°C
0.0557
(4S)-4-benzyl-2-(3,4,5-trimethoxyphenyl)-3,4-dihydro-5Hpyrido[10,20:1,2] imidazo[4,5-d][1,3]diazepin-5-one
Homo sapiens
-
pH 8..0, 37°C
0.0335
(4S)-4-benzyl-2-(3,4-dimethoxyphenyl)-3,4-dihydro-5Hpyrido[10,20:1,2]imidazo [4,5-d][1,3]diazepin-5-one
Homo sapiens
-
pH 8..0, 37°C
0.1248
(4S)-4-benzyl-2-(3-hydroxyphenyl)-3,4-dihydro-5H-pyrido[10,20:1,2]imidazo-[4,5-d][1,3]diazepin-5-one
Homo sapiens
-
pH 8..0, 37°C
0.072
(4S)-4-benzyl-2-(4-methoxyphenyl)-3,4-dihydro-5H-pyrido[1',2':1,2]imidazo[4,5-d][1,3]diazepin-5-one
Homo sapiens
-
pH 8..0, 37°C
0.068
(4S)-4-benzyl-2-(4-methylphenyl)-3,4-dihydro-5H-pyrido[1',2':1,2]imidazo[4,5-d][1,3]diazepin-5-one
Homo sapiens
-
pH 8..0, 37°C
0.1354
(S)-N-(1-(2-amino-imidazo[1,2-a]pyridin-3-yl)-1-oxo-3-phenylpropan-2-yl)-2-methylbenzamide
Homo sapiens
-
pH 8..0, 37°C
0.1492
(S)-N-(1-(2-amino-imidazo[1,2-a]pyridin-3-yl)-1-oxo-3-phenylpropan-2-yl)-2-phenylacetamide
Homo sapiens
-
pH 8..0, 37°C
0.00039 - 0.0004
1-(2-bromobenzene-1-sulfonyl)-5-methyl-3-(2-methyl-4,5-dihydro-1H-imidazol-4-yl)-1H-indole
0.0012 - 0.0015
1-(2-chlorobenzene-1-sulfonyl)-5-methyl-3-(2-methyl-4,5-dihydro-1H-imidazol-4-yl)-1H-indole
0.00007
2-(2-fluoro-phenyl)-5,6,7,8-tertrahydro-benzol[4,5]thieno[2,3-d][1,3]oxazin-4-one
Homo sapiens
-
0.00039
1-(2-bromobenzene-1-sulfonyl)-5-methyl-3-(2-methyl-4,5-dihydro-1H-imidazol-4-yl)-1H-indole
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.0004
1-(2-bromobenzene-1-sulfonyl)-5-methyl-3-(2-methyl-4,5-dihydro-1H-imidazol-4-yl)-1H-indole
Mus musculus
pH not specified in the publication, temperature not specified in the publication
0.0012
1-(2-chlorobenzene-1-sulfonyl)-5-methyl-3-(2-methyl-4,5-dihydro-1H-imidazol-4-yl)-1H-indole
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
quantitative ELISA analysis of enzyme activity in 260 samples of ovarian cancer cytosol, overview
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
additional information
-
enzyme shows optimal activity at neutral pH, and retains significant activity at acidic pH
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
37
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
brenda
-
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
breast cancer patients with KLK7 positive tumors have relatively shorter disease-free survival and overall survival than patients with KLK7 negative tumors
brenda
breast carcinoma cell line, enzyme is upregulated by estrogens and slightly by glucocorticoids
brenda
-
increased expression of kallikrein 7 and decreased expression of its inhibitor antileukoprotease might play an important role in cervical adenocarcinoma development
brenda
-
50% of the primary and 50% of the established cervical cancer cell lines express kallikrein 7
brenda
-
cervical intraepithelial neoplasia, cervicitis, squamous cervical carcinomas, and cervical adenocarcinomas
brenda
-
high expression of the enzyme
brenda
-
semi-quantitative RT-PCR determination and immunohistochemical analysis
brenda
-
the transcriptional changes 3 and 60 h after TNF treatment of normal, human papillomaviruses 16- and human papillomaviruses 18-immortalized keratinocytes is analyzed by microarray analysis. KLK7 shows a differential expression pattern associated with the differential response to TNF. KLK7 expression pattern is is equally expressed in TNF-treated or untreated human papillomaviruses 18-immortalized cells but it is not detected in normal primary keratinocytes or human papillomaviruses 16-immortalized cells
brenda
-
KLK7 shows strong expression in low grade in contrast to high grade clear cell renal cell carcinoma, RCC, overview. The expression of KLK7 can distinguish between oncocytoma and chromophobe RCC
brenda
-
KLK7 is strongly expressed in the tissue of patients with squamous cell carcinoma and differentiated tumors
brenda
additional information
enzyme expression analysis in 155 patients, overview
brenda
-
in contrast to the expression in ovarian cancer, high expression of KLK 7 is strongly associated with good prognosis in breast cancer patients
brenda
-
decrease in level of kallikrein 7 in patients with Alzheimer's disease and patients with frontotemporal dementia
brenda
the enzyme is strongly expressed in the upper layers of the epidermis
brenda
-
KLK7, KLK5, and cathelicidin colocalizes in keratinocytes lamellar granules stimulated with 1,25(OH)2VD3
brenda
-
KLK7 expression in the normal kidney shows granular cytoplasmic expression in tubules (stronger intensity in distal than proximal) and no expression in the mesangium
brenda
-
highest concentrations of KLK7 mRNA are found in the non-cancerous tissue of patients with (well or moderately) differentiated tumors and the lowest in those with poorly differentiated tumors
brenda
-
in the oral cavity, strong reactivity for KLK7 in human oral squamous cell carcinoma tissues, immunohistochemical analysis, overview
brenda
-
in the oral cavity, strong reactivity for KLK7 in orthotopic murine tumors, immunohistochemical analysis, overview
brenda
-
different carcinoma cell lines and types, overview
brenda
-
a short mRNA variant for KLK7 (alternative AUG, predicted protein N-terminally truncated and lacking catalytic histidine residue) expressed in normal ovary and in ovarian cancer
brenda
-
overexpression of the human tissue kallikrein genes KLK4, 5, 6, and 7 increases the malignant phenotype of ovarian cancer cells
brenda
-
short mRNA variant for KLK7 (alternative AUG, predicted protein N-terminally truncated and lacking catalytic histidine residue) expressed in normal ovary and in ovarian cancer
brenda
-
quantitative in situ protein expression analysis of 150 advanced-stage ovarian cancer samples of primary epithelial ovarian cancer patients, method development, overview
brenda
-
over-expressed in ovarian carcinoma tissues. Elevated KLK 7 mRNA expression in tumor tissue is associated with poorer prognosis for ovarian cancer patients
brenda
-
KLK7 is upregulated in epithelial ovarian carcinoma, expression of two different KLK7 transcripts, KLK7-253 and KLK7-181, simultaneously
brenda
-
KLK7 and KLK5 are expressed in pancreatic tissues by acinar cells. Motifs in the promoter of KLK7 and KLK 5 are identified for transcription factors which confer pancreatic expression
brenda
-
kallikrein 7 is overexpressed in pancreatic adenocarcinomas as well as other human cancers
brenda
-
PCR expression profile of serine proteases from both healthy and malignant pancreatic tissues
brenda
-
ALP is significantly decreased in prostate cancers compared with that in benign prostate epithelial cells. Immunohistochemical expression of kallikrein 7 is observed in prostate epithelial cells, whereas little or no staining is observed in prostate cancer. Western blot analysis reveals that hK7 and antileukoprotease are decreased in malignant prostate epithelium
brenda
-
significantly increased serum enzyme levels in cervical cancer patients compared to healthy individuals and patients with benign cervical disease
brenda
-
in a randomized controlled study on 20 volunteers, epidermal mRNA expression of genes essential for keratinocyte differentiation and desquamation after a 7-week treatment with two moisturizers is analyzed. Treatment with one test moisturizer (hydrocarbon cream) increased gene expression of involucrin, transglutaminase 1, kallikrein 5, and kallikrein 7, while the other moisturizer (complex cream) affects only expression of cyclin-dependent kinase inhibitor 1A
brenda
additional information
no expression in liver, pancreas, small intestine, bone marrow, ovary, skeletal muscle, spleen, colon, adrenal gland, prostate, heart, lung, and stomach
brenda
additional information
-
no expression in liver, pancreas, small intestine, bone marrow, ovary, skeletal muscle, spleen, colon, adrenal gland, prostate, heart, lung, and stomach
brenda
additional information
-
enzyme is specifically expressed in keratinizing squamous epithelia
brenda
additional information
-
no expression of kallikrein 7 by normal cervical keratinocytes
brenda
additional information
-
KLK7 tissue expression and distribution pattern, overview
brenda
additional information
-
mRNA levels of KLK7 in normal breast tissues, benign breast tissues, primary tumors, and lymph node metastases, by real-time RT-PCR and microarray, detailed overview
brenda
additional information
-
tissue expression analysis by quantitative RT PCR analysis
brenda
additional information
-
the enzyme is overexpressed in a variety of cancers, significantly increased serum enzyme levels with cervical cancer
brenda
additional information
-
tissue expression analysis by quantitative RT PCR analysis
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
physiological function
evolution
human kallikrein-related peptidase 7 is one member from a cluster of 15 serine peptidases of the chymotrypsin-like S1A family clan PA(S) sharing a high degree of identity and localized at human chromosome locus 19q13.4
evolution
-
human tissue kallikrein-7 is a chymotryptic serine protease member of tissue kallikrein family.
malfunction
-
kallikrein 7 may be causally involved in carcinogenesis, particularly in tumor metastasis and invasion
malfunction
-
KLK7 is upregulated in epithelial ovarian carcinoma with high levels correlated with poor prognosis. Mechanism for association of high KLK7 levels with chemoresistance and poor prognosis for serous EOC patients by promotion of peritoneal dissemination and reinvasion via increased MCA and alpha5beta1 integrin-dependent cell adhesion
physiological function
-
kallikrein 7 is a proteolytic enzyme important for epithelial cell shedding
physiological function
-
the serine proteases kallikrein 5 and kallikrein 7 control enzymatic processing of cathelicidin precursor in the skin and regulate the eventual function of the final forms of these peptides
physiological function
-
kallikrein 7 is a proteolytic enzyme important for epithelial cell shedding, the enzyme is involved in the degradation of several components of the extracellular matrix
physiological function
-
serine proteases of the tissue kallikrein-related peptidases family are implicated in tumorigenesis, kallikrein-related peptidase 7 is a proliferative factor that is aberrantly expressed in human colon cancer and involved in cell proliferation in vitro and in vivo
physiological function
-
the enzyme is involved in skin homeostasis and inflammation. Excess of enzyme activity is also associated with tumor metastasis processes, especially in ovarian carcinomas, prostatic and pancreatic cancers
physiological function
the enzyme plays roles in physiological and pathological skin desquamation processes that requires the presence of water in the stratum corneum, which is maintained by hygroscopic compounds collectively named as skin moisturizing factor
physiological function
-
the treatment of beta-amyloid oligomer preparations with the enzyme, but not the inactive proform, significantly reduces Abeta42-mediated toxicity to rat hippocampal neurons to the same extent as the known Abeta-degrading protease insulin-degrading enzyme
physiological function
inhibition of KLK7 alone is sufficient to block shedding, whereas KLK5 is also a major contributor
physiological function
KLK7 overexpression in melanoma cells mediates decrease of cell adhesion to extracellular matrix binding proteins, associated with downregulation of alpha5/beta1/alphav/beta3 integrin expression. Upregulation of MCAM/CD146 and increased spheroid formation is also detected
physiological function
KLK7-mediated cleavage of midkine results in an overall reduction in the pro-proliferative and pro-migratory effect of midkine. An inverse relation between KLK7 and midkine is also observed in human melanoma tissues
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). KLK7_HUMAN
253
0
27525
Swiss-Prot
Secretory Pathway (Reliability: 1)
KLK7_MOUSE
249
0
27257
Swiss-Prot
Secretory Pathway (Reliability: 1)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
?
x * 30000, gylcosylated form, x * 28000 and x * 20000, nonglycosylated froms, SDS-PAGE. X * 25000, calculated from sequence
additional information
tertiary and primary structure of kallikrein 7, overview
additional information
-
tertiary and primary structure of kallikrein 7, overview
additional information
three-dimensional structure and specific substrate site, involving conserved residues Ala190-Ser195, Val213-Cys220 and Pro225-Tyr228, molecular modeling, overview
additional information
-
three-dimensional structure and specific substrate site, involving conserved residues Ala190-Ser195, Val213-Cys220 and Pro225-Tyr228, molecular modeling, overview
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
proteolytic modification
proteolytic modification
recombinant enzyme proform is activated by digestion with trypsin
proteolytic modification
-
activation by thermolysin, inhibited by phosphoramidon
proteolytic modification
-
activation of recombinant pro-kallikrein 7 by thermolysin, inhibited by phosphoramidon
proteolytic modification
pro-kallikrein is activated by proteolytic clavage of the Xaa15-Ile16 bond
proteolytic modification
-
proKLK7 is processed and activated by meprin metalloproteases alpha and beta, which need to activated themselves by specifically by KLK4, KLK5, and KLK8, overview. Meprins cleave within the N-terminal region of proKLK7. This triggering leads to an accelerated activation of KLK7 (approximately 150%) in the presence of trypsin, overview
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
analysis of crystal structure of KLK7: owing to the conformational restrictions of the relatively narrow S1 pocket, the formation of a stabilizing hydrogen bond between the P1-Tyr-OH and the carboxamide of Asn189 has to be mediated by a water molecule. The S2 subsite is less separated from the S4 subsite than in KLK4-6 and less limited in size owing to a different position of the His99 imidazole side chain, which may also contribute to the capacity for the adaptation to P2 side chains of various size
-
kallikrein 7 bound to inhibitors succinyl-Ala-Ala-Pro-Phe-chloromethyl ketone and Ala-Ala-Phe-chloromethyl ketone, sitting-drop vapor diffusion method at 18°C, 0.001 ml protein solution, containing 7 mg/ml enzyme-inhibitor complex, is mixed with 0.001 ml reservoir solution containing 100 mM [bis(2-hydroxyethyl)amino]tris(hydroxymethyl)-methane-HCl, pH 6.0, 25% PEG 3350, and 2.5 M Li2SO4, equilibration against reservoir solution, X-ray diffraction structure determination and analysis at 1.0-2.5 A resolution
purified recombinant enzyme bound to specific inhibitor LEKTI domain 6, 8 mg/ml protein in sodium phosphate buffer, pH 7.5, with a reservoir solution containing 3.2 M ammonium sulfate in 0.1 M HEPES, pH 7.0, X-ray diffraction structure determination and anaylsis at 2.8 A resolution
purified recombinant His-tagged enzyme, sitting-drop vapour-diffusion method, 22°C, 0.0001 ml of 8 mg/ml protein in 50 mM sodium phosphate buffer, pH 7.5, mixed with 0.0001 ml of reservoir solution, X-ray diffraction structure determination and anaylsis at 2.8 A resolution
-
sitting drop vapour diffusion method, with 100 mM [bis(2-hydroxyethyl)amino]tris(hydroxymethyl)-methane-HCl, pH 6.0, 25% PEG 3350, and 2.5 M Li2SO4 or with 100 mM sodium cacodylate, pH 6.5, 200 mM magnesium acetate, and 30% (v/v) 2-methyl-2,4-pentanediol
two crystal structures of KLK7 are solved with either of two covalently bound chloromethyl ketone (CMK) inhibitors. Overall, the S1 pocket of KLK7 is larger and more hydrophobic than those of the tryptic KLK4, 5, and 6. The hydrophobicity of the S1 pocket is enhanced by the presence of Ala190 instead of Ser190, and at the bottom of the pocket, Asn189, a polar residue, replaces Asp189, a negatively charged residue. Consistent with specificity, Asn189 insteadof Asp189 would reduce the affinity of KLK7 for basic P1 side chains and allow binding of non-polar residues. The size and shape of the S1 pocket is well suited to accommodate residues with medium and large side chains, explaining the modified chymotryptic specificity. Tyr may be favored over Phe at P1 because of the potential of the carboxyamide group of Asn189 to hydrogen bond to a buried hydroxyl group
-
in complex with inhibitor 1-(2-chlorobenzene-1-sulfonyl)-5-methyl-3-(2-methyl-4,5-dihydro-1H-imidazol-4-yl)-1H-indole. 2-Chlorobenzene inserts into the S1 pocket, the methyl group on the imidazoline ring is located at the S2 site composed of side chains of His99, Asp102, His57, and Ser214
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H41F
H99A
additional information
H41F
site-directed mutagenesis, the mutant is inhibited by Zn2+ like the wild-type enzyme
H99A
site-directed mutagenesis, the mutant shows resistance against inhibition by Zn2+ in contrast to the wild-type enzyme
additional information
-
KLK7 is overexpressed in the pancreatic cancer cell line BxPC-3, and in vitro cell adhesion assays are performed to determine alterations in cell adhesion to collagen I, fibronectin, and vitronectin compared with vector-transfected cells. Changes in cell surface expression of alphavbeta3 integrin are examined by flow cytometry, and the release of soluble urokinase-type plasminogen activator receptor (uPAR) is monitored by Western blot analysis. The expression of KLK7 in BxPC-3 cells leads to reduced adhesion to vitronectin but not collagen I or fibronectin. Loss of cell adhesion to vitronectin is not caused by changes in the level of alphavbeta3 integrin cell surface expression. A significant increase in the amount of uPAR shed is observed in KLK7-expressing cells compared with vector-transfected control cells
additional information
-
the individual risk of eczema conferred by the SPINK5 polymorphism rs2303067 (Glu420Lys) and a previously described insertion in the 3'-untranslated region of KLK7 and potential epistatic effects between these variants and filaggrin mutations are analysed in patients with eczema and healthy counterparts. No association is seen with the SPINK5 or KLK7 variants. A weaker effect is observed for the SPINK5 variant with maternal transmission in the family-based study
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
nickel-nitrilotriacetic acid-Sepharose column chromatography and benzamidine-Sepharose column chromatography
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3)SS periplasm by nickel affinity chromatography
-
recombinant kallikrein 7 from HEK-293F cell culture supernatant by ultrafiltration and dialysis, anion exchange chromatography, and heparin affinity chromatography, followed by metal affinity on an iminodiacetic acid epoxy resin column, elution with L-histidine from the latter column, to homogeneity
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloning from keratinocyte library, DNA and RNA sequence determination and analysis, expression of the enzyme in its proform in murine C127 cells, enzyme activation by trypsin
DNA sequence determination and analysis, gene KLK7 mapps to chromosomal locus 19q13.3-13.4, human kallikrein gene family locus
enzyme overexpression in HT-29 cells resulting in increased cell proliferation
-
expression analysis by quantitative RT PCR analysis
expression in Pichia pastoris
gene KLK7, DNA and amino acid sequence determination and analysis, expression anaysis and microsatellite-based association mapping, allele sizes and distribution of KLK7, overview
-
gene KLK7, encoded on chromosome 19, expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)SS with secretion to the the bacterial periplasm
-
gene KLK7, expression in Escherichia coli with secretion to the the bacterial periplasm
gene KLK7, expression profiling in BxPC-3 cells from pancreatic adenocarcinomas
-
gene KLK7, genetic organization and structure of the kallikrein gene family, clustered on chromosome 19q13.3-q13.4
gene KLK7, overexpression in breast cancer cell lines aMCF-7, OVMZ-6, and MDA-231, quantitative expression analysis in wild-type native cells and in transfected cells, overview
gene KLK7, stable expression of pro-kallikrein 7 in HEK-293F cells, secretion of the recombinant protein to the cell culture supernatant, activation of the recombinant enzyme by thermolysin
-
stable overexpression of KLK7-253 in SKOV-3 cells, leading to formation of multicellular aggregates, MCAs, that promote cell survival and chemoresistance, with involvement of KLK7 and integrin-regulated cell adhesion. KLK7-253 cells form MCAs invade into mesothelial cell monolayers
-
the gene encoding the enzyme is localized at chromosome locus 19q13.4, recombinant expression in an insect cell line using the baculovirus transfection system
transgenic mice overexpressing human scce-gene. Epidermal hyperproliferation and decreased skin barrier function in mice overexpressing stratum corneum chymotryptic enzyme
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
increased extracellular calcium-induced KLK7 mRNA expression and protein release in epidermal keratinocyte. Increased protease activity and differential processing of cathelicidin accompanies increased KLK expression. 1,25(OH)2VD3 increases KLK expression independently of differentiation in keratinocytes
-
KLK7 expression is decreased in prostate cancer cells compared to normal benign prostate cells
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diagnostics
medicine
molecular biology
diagnostics
-
the enzyme is a biomarker for advanced ovarian carcinoma using a novel in situ quantitative method of protein expression, overview
diagnostics
-
the enzyme is a prognostic biomarker for ovarian cancer, but cannot be used independent from other markers, overview
diagnostics
-
human kallikrein 7 can potentially be used as a biomarker for the characterization of different stages of cervical disease
diagnostics
-
potential biomarkers for several carcinomas and other diseases, prognostic value of KLK7 mRNA expression in colorectal cancer tissue giving, upregulation of KLK7 expression gives a poor prognosis, overview
medicine
-
because the enzyme appears only in abundance in tumor tissue and contains a secretion signal sequence, suggesting that the enzyme is secreted, it may prove to be a useful diagnostic/prognostic tool for the detection of metastatic or recurrent disease or as a novel molecular target for cervical cancer therapy
medicine
-
breast cancer patients with KLK7 positive tumors have relatively shorter disease-free survival and overall survival than patients with KLK7 negative tumors. KLK7 gene expression may be used as a marker of unfavorable prognosis for breast cancer patients
medicine
expression of full-length KLK7 mRNA may represent a new prognostic marker in breast cancer disease
medicine
-
kallikrein 7 may be useful in clinics as biomarkers for the detection and monitoring of non-small cell lung cancer
medicine
-
ectopic expression of KLK7 in pancreatic cancer cells leads to a reduction in cell adhesion to vitronectin that may result from the cleavage of uPAR from the cell surface. KLK 7 expression, plays an important role in the dissemination of tumor cells through the production of soluble uPAR in pancreatic cancer
medicine
study on KLK7 expression in prostate cancer. A total of 64 of 92 (69.57%) benign cases show positive staining for KLK7 and 23 of 116 (19.83%)malignant cases show positive staining. The expression level of kallikrein-related peptidase 7 mRNA is significantly decreased in prostate cancer tissues compared with that in benign prostate hyperplasia tissues and normal prostate tissue. The protein expression levels of KLK7 is lower in prostate cancer than in benign prostate hyperplasia tissues and normal prostate tissue. Kallikrein-related peptidase 7 and KLK7 expression are downregulated in prostate cancer and lower expression of kallikrein-related peptidase 7 closely correlates with higher Gleason score and higher prostate-specific antigen level
molecular biology
an activity assay for human kallikrein 7 is developed using a blue-fluorescent acridone dye, featuring a remarkably long lifetime that can be quenched by either of the 2 natural amino acids, tyrosine and tryptophan. Incorporating this probe and 1 of the quenching amino acids on either side of the scissile bond of the substrate peptide makes it possible to monitor the enzymatic activity by quantifying the increase in the fluorescence lifetime signal. A systematic investigation of substrate structures leads to a homogenous, microplate-based, compound profiling assay that yields inhibitory constants down into the single-digit nanomolar range
molecular biology
-
kallikrein 7 and antileukoprotease are down-regulated in prostate cancers
molecular biology
-
kallikrein 7 may play a critical role in the invasion of cancer cells in which it is aberrantly expressed by degrading important cell adhesive molecules like desmogleins and E-cadherin
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Boeckmann, B.; Bairoch, A.; Apweiler, R.; Blatter, M.C.; Estreicher, A.; Gasteiger, E.; Martin M.J.; Michoud, K.; O'Donovan, C.; Phan, I.; Pilbout, S.; Schneider, M.
The SWISS-PROT protein knowledgebase and its supplement TrEMBL
Nucleic Acids Res.
31
365-370
2003
Homo sapiens (P49862)
brenda
El Moujahed, A.; Gutman, N.; Brillard, M.; Gauthier, F.
Substrate specificity of two kallikrein family gene products isolated from the rat submandibular gland
FEBS Lett.
265
137-140
1990
Rattus norvegicus
brenda
Yousef, G.M.; Diamandis, E.P.
The new human tissue kallikrein gene family: structure, function, and association to disease
Endocr. Rev.
22
184-204
2001
Homo sapiens (P49862)
brenda
Lundstrom, A.; Egelrud, T.
Stratum corneum chymotryptic enzyme: a proteinase which may be generally present in the stratum corneum and with a possible involvement in desquamation
Acta Derm. Venereol.
71
471-474
1991
Homo sapiens
brenda
Egelrud, T.
Purification and preliminary characterization of stratum corneum chymotryptic enzyme: a proteinase that may be involved in desquamation
J. Invest. Dermatol.
101
200-204
1993
Homo sapiens
brenda
Hansson, L.; Stromqvist, M.; Backman, A.; Wallbrandt, P.; Carlstein, A.; Egelrud, T.
Cloning, expression, and characterization of stratum corneum chymotryptic enzyme. A skin-specific human serine proteinase
J. Biol. Chem.
269
19420-19426
1994
Homo sapiens (P49862), Homo sapiens
brenda
Skytt, A.; Stromqvist, M.; Egelrud, T.
Primary substrate specificity of recombinant human stratum corneum chymotryptic enzyme
Biochem. Biophys. Res. Commun.
211
586-589
1995
Homo sapiens
brenda
Franzke, C.W.; Baici, A.; Bartels, J.; Christophers, E.; Wiedow, O.
Antileukoprotease inhibits stratum corneum chymotryptic enzyme. Evidence for a regulative function in desquamation
J. Biol. Chem.
271
21886-21890
1996
Homo sapiens
brenda
Tanimoto, H.; Underwood, L.J.; Shigemasa, K.; Yan Yan, M.S.; Clarke, J.; Parmley, T.H.; O'Brien, T.J.
The stratum corneum chymotryptic enzyme that mediates shedding and desquamation of skin cells is highly overexpressed in ovarian tumor cells
Cancer
86
2074-2082
1999
Homo sapiens
brenda
Nylander-Lundqvist, E.; Egelrud, T.
Formation of active IL-1 beta from pro-IL-1 beta catalyzed by stratum corneum chymotryptic enzyme in vitro
Acta Derm. Venereol.
77
203-206
1997
Homo sapiens
brenda
Yousef, G.M.; Scorilas, A.; Magklara, A.; Soosaipillai, A.; Diamandis, E.P.
The KLK7 (PRSS6) gene, encoding for the stratum corneum chymotryptic enzyme is a new member of the human kallikrein gene family - genomic characterization, mapping, tissue expression and hormonal regulation
Gene
254
119-128
2000
Homo sapiens (P49862), Homo sapiens
brenda
Ny, A.; Egelrud, T.
Epidermal hyperproliferation and decreased skin barrier function in mice overexpressing stratum corneum chymotryptic enzyme
Acta Derm. Venereol.
84
18-22
2004
Homo sapiens
brenda
Planque, C.; de Monte, M.; Guyetant, S.; Rollin, J.; Desmazes, C.; Panel, V.; Lemarie, E.; Courty, Y.
KLK5 and KLK7, two members of the human tissue kallikrein family, are differentially expressed in lung cancer
Biochem. Biophys. Res. Commun.
329
1260-1266
2005
Homo sapiens
brenda
Tan, O.L.; Whitbread, A.K.; Clements, J.A.; Dong, Y.
Kallikrein-related peptidase (KLK) family mRNA variants and protein isoforms in hormone-related cancers: do they have a function?
Biol. Chem.
387
697-705
2006
Homo sapiens
brenda
Prezas, P.; Arlt, M.J.; Viktorov, P.; Soosaipillai, A.; Holzscheiter, L.; Schmitt, M.; Talieri, M.; Diamandis, E.P.; Krueger, A.; Magdolen, V.
Overexpression of the human tissue kallikrein genes KLK4, 5, 6, and 7 increases the malignant phenotype of ovarian cancer cells
Biol. Chem.
387
807-811
2006
Homo sapiens
brenda
Diamandis, E.P.; Scorilas, A.; Kishi, T.; Blennow, K.; Luo, L.Y.; Soosaipillai, A.; Rademaker, A.W.; Sjogren, M.
Altered kallikrein 7 and 10 concentrations in cerebrospinal fluid of patients with Alzheimers disease and frontotemporal dementia
Clin. Biochem.
37
230-237
2004
Homo sapiens
brenda
Kishi, T.; Soosaipillai, A.; Grass, L.; Little, S.P.; Johnstone, E.M.; Diamandis, E.P.
Development of an immunofluorometric assay and quantification of human kallikrein 7 in tissue extracts and biological fluids
Clin. Chem.
50
709-716
2004
Homo sapiens (P49862), Homo sapiens
brenda
Baretton, G.; Luther, T.; Tjan-Heijnen, V.C.; Talieri, M.; Schmitt, M.; Sweep, F.C.; Span, P.N.; Magdolen, V.
Quantitative reverse transcription-PCR assay for detection of mRNA encoding full-length human tissue kallikrein 7: prognostic relevance of KLK7 mRNA expression in breast cancer
Clin. Chem.
52
1070-1079
2006
Homo sapiens (P49862), Homo sapiens
brenda
Santin, A.D.; Cane, S.; Bellone, S.; Bignotti, E.; Palmieri, M.; De Las Casas, L.E.; Roman, J.J.; Anfossi, S.; OBrien, T.; Pecorelli, S.
The serine protease stratum corneum chymotryptic enzyme (kallikrein 7) is highly overexpressed in squamous cervical cancer cells
Gynecol. Oncol.
94
283-288
2004
Homo sapiens
brenda
Caubet, C.; Jonca, N.; Brattsand, M.; Guerrin, M.; Bernard, D.; Schmidt, R.; Egelrud, T.; Simon, M.; Serre, G.
Degradation of corneodesmosome proteins by two serine proteases of the kallikrein family, SCTE/KLK5/hK5 and SCCE/KLK7/hK7
J. Invest. Dermatol.
122
1235-1244
2004
Homo sapiens (P49862)
brenda
Vasilopoulos, Y.; Cork, M.J.; Murphy, R.; Williams, H.C.; Robinson, D.A.; Duff, G.W.; Ward, S.J.; Tazi-Ahnini, R.
Genetic association between an AACC insertion in the 3UTR of the stratum corneum chymotryptic enzyme gene and atopic dermatitis
J. Invest. Dermatol.
123
62-66
2004
Homo sapiens (P49862), Homo sapiens
brenda
Tian, X.; Shigemasa, K.; Hirata, E.; Gu, L.; Uebaba, Y.; Nagai, N.; OBrien, T.J.; Ohama, K.
Expression of human kallikrein 7 (hK7/SCCE) and its inhibitor antileukoprotease (ALP/SLPI) in uterine endocervical glands and in cervical adenocarcinomas
Oncol. Rep.
12
1001-1006
2004
Homo sapiens
brenda
Talieri, M.; Diamandis, E.P.; Gourgiotis, D.; Mathioudaki, K.; Scorilas, A.
Expression analysis of the human kallikrein 7 (KLK7) in breast tumors: A new potential biomarker for prognosis of breast carcinoma
Thromb. Haemost.
91
180-186
2004
Homo sapiens
brenda
Psyrri, A.; Kountourakis, P.; Scorilas, A.; Markakis, S.; Camp, R.; Kowalski, D.; Diamandis, E.P.; Dimopoulos, M.A.
Human tissue kallikrein 7, a novel biomarker for advanced ovarian carcinoma using a novel in situ quantitative method of protein expression
Ann. Oncol.
19
1271-1277
2008
Homo sapiens
brenda
Prezas, P.; Scorilas, A.; Yfanti, C.; Viktorov, P.; Agnanti, N.; Diamandis, E.; Talieri, M.
The role of human tissue kallikreins 7 and 8 in intracranial malignancies
Biol. Chem.
387
1607-1612
2006
Homo sapiens
brenda
Singh, J.; Naran, A.; Misso, N.L.; Rigby, P.J.; Thompson, P.J.; Bhoola, K.D.
Expression of kallikrein-related peptidases (KRP/hK5, 7, 6, 8) in subtypes of human lung carcinoma
Int. Immunopharmacol.
8
300-306
2008
Homo sapiens
brenda
Debela, M.; Magdolen, V.; Schechter, N.; Valachova, M.; Lottspeich, F.; Craik, C.S.; Choe, Y.; Bode, W.; Goettig, P.
Specificity profiling of seven human tissue kallikreins reveals individual subsite preferences
J. Biol. Chem.
281
25678-25688
2006
Homo sapiens (P49862)
brenda
Deraison, C.; Bonnart, C.; Lopez, F.; Besson, C.; Robinson, R.; Jayakumar, A.; Wagberg, F.; Brattsand, M.; Hachem, J.P.; Leonardsson, G.; Hovnanian, A.
LEKTI fragments specifically inhibit KLK5, KLK7, and KLK14 and control desquamation through a pH-dependent interaction
Mol. Biol. Cell
18
3607-3619
2007
Homo sapiens
brenda
Debela, M.; Hess, P.; Magdolen, V.; Schechter, N.M.; Steiner, T.; Huber, R.; Bode, W.; Goettig, P.
Chymotryptic specificity determinants in the 1.0 A structure of the zinc-inhibited human tissue kallikrein 7
Proc. Natl. Acad. Sci. USA
104
16086-16091
2007
Homo sapiens (P49862), Homo sapiens
brenda
Fernandez, I.S.; Staendker, L.; Forssmann, W.G.; Gimenez-Gallego, G.; Romero, A.
Crystallization and preliminary crystallographic studies of human kallikrein 7, a serine protease of the multigene kallikrein family
Acta Crystallogr. Sect. F
F63
669-672
2007
Homo sapiens
brenda
Stenshamn, K.; Bongcam-Rudloff, E.; Hillbertz, N.S.; Nodtvedt, A.; Bergvall, K.; Hedhammar, A.; Andersson, G.
Evaluation of kallikrein 7 as a disease-causing gene for canine atopic dermatitis using microsatellite-based association mapping
Anim. Genet.
37
601-603
2006
Canis lupus familiaris
brenda
Ramani, V.C.; Haun, R.S.
The extracellular matrix protein fibronectin is a substrate for kallikrein 7
Biochem. Biophys. Res. Commun.
369
1169-1173
2008
Homo sapiens
brenda
Johnson, S.K.; Ramani, V.C.; Hennings, L.; Haun, R.S.
Kallikrein 7 enhances pancreatic cancer cell invasion by shedding E-cadherin
Cancer
109
1811-1820
2007
Homo sapiens
brenda
Shan, S.J.; Scorilas, A.; Katsaros, D.; Rigault de la Longrais, I.; Massobrio, M.; Diamandis, E.P.
Unfavorable prognostic value of human kallikrein 7 quantified by ELISA in ovarian cancer cytosols
Clin. Chem.
52
1879-1886
2006
Homo sapiens
brenda
Fernandez, I.S.; Staendker, L.; Maegert, H.J.; Forssmann, W.G.; Gimenez-Gallego, G.; Romero, A.
Crystal structure of human epidermal kallikrein 7 (hK7) synthesized directly in its native state in E. coli: insights into the atomic basis of its inhibition by LEKTI domain 6 (LD6)
J. Mol. Biol.
377
1488-1497
2008
Homo sapiens (P49862), Homo sapiens
brenda
Debela, M.; Beaufort, N.; Magdolen, V.; Schechter, N.M.; Craik, C.S.; Schmitt, M.; Bode, W.; Goettig, P.
Structures and specificity of the human kallikrein-related peptidases KLK 4, 5, 6, and 7
Biol. Chem.
389
623-632
2008
Homo sapiens
brenda
Pettus, J.R.; Johnson, J.J.; Shi, Z.; Davis, J.W.; Koblinski, J.; Ghosh, S.; Liu, Y.; Ravosa, M.J.; Frazier, S.; Stack, M.S.
Multiple kallikrein (KLK 5, 7, 8, and 10) expression in squamous cell carcinoma of the oral cavity
Histol. Histopathol.
24
197-207
2009
Homo sapiens, Mus musculus
brenda
Buraczewska, I.; Berne, B.; Lindberg, M.; Loden, M.; Toermae, H.
Long-term treatment with moisturizers affects the mRNA levels of genes involved in keratinocyte differentiation and desquamation
Arch. Dermatol. Res.
301
175-181
2009
Homo sapiens
brenda
Xuan, Q.; Yang, X.; Mo, L.; Huang, F.; Pang, Y.; Qin, M.; Chen, Z.; He, M.; Wang, Q.; Mo, Z.N.
Expression of the serine protease kallikrein 7 and its inhibitor antileukoprotease is decreased in prostate cancer
Arch. Pathol. Lab. Med.
132
1796-1801
2008
Homo sapiens
brenda
Eissa, A.; Diamandis, E.P.
Human tissue kallikreins as promiscuous modulators of homeostatic skin barrier functions
Biol. Chem.
389
669-680
2008
Homo sapiens
brenda
Dong, Y.; Matigian, N.; Harvey, T.J.; Samaratunga, H.; Hooper, J.D.; Clements, J.A.
Tissue-specific promoter utilisation of the kallikrein-related peptidase genes, KLK5 and KLK7, and cellular localisation of the encoded proteins suggest roles in exocrine pancreatic function
Biol. Chem.
389
99-109
2008
Homo sapiens
brenda
Ramani, V.C.; Hennings, L.; Haun, R.S.
Desmoglein 2 is a substrate of kallikrein 7 in pancreatic cancer
BMC Cancer
8
373
2008
Homo sapiens
brenda
Termini, L.; Boccardo, E.; Esteves, G.H.; Hirata, R.; Martins, W.K.; Colo, A.E.; Neves, E.J.; Villa, L.L.; Reis, L.F.
Characterization of global transcription profile of normal and HPV-immortalized keratinocytes and their response to TNF treatment
BMC Med. Genomics
1
29
2008
Homo sapiens
brenda
Weidinger, S.; Baurecht, H.; Wagenpfeil, S.; Henderson, J.; Novak, N.; Sandilands, A.; Chen, H.; Rodriguez, E.; ORegan, G.M.; Watson, R.; Liao, H.; Zhao, Y.; Barker, J.N.; Allen, M.; Reynolds, N.; Meggitt, S.; Northstone, K.; Smith, G.D.; Strobl, C.; Stahl, C.; Kneib, T.; Klopp, N.; Bieber, T.; Behren, B.e.h.r.e.n.d.
Analysis of the individual and aggregate genetic contributions of previously identified serine peptidase inhibitor Kazal type 5 (SPINK5), kallikrein-related peptidase 7 (KLK7), and filaggrin (FLG) polymorphisms to eczema risk
J. Allergy Clin. Immunol.
122
560-568
2008
Homo sapiens
brenda
Doering, K.; Meder, G.; Hinnenberger, M.; Woelcke, J.; Mayr, L.M.; Hassiepen, U.
A fluorescence lifetime-based assay for protease inhibitor profiling on human kallikrein 7
J. Biomol. Screen.
14
1-9
2009
Homo sapiens (P49862), Homo sapiens
brenda
Ramani, V.C.; Haun, R.S.
Expression of kallikrein 7 diminishes pancreatic cancer cell adhesion to vitronectin and enhances urokinase-type plasminogen activator receptor shedding
Pancreas
37
399-404
2008
Homo sapiens
brenda
Gabril, M.; White, N.M.; Moussa, M.; Chow, T.F.; Metias, S.M.; Fatoohi, E.; Yousef, G.M.
Immunohistochemical analysis of kallikrein-related peptidases in the normal kidney and renal tumors: potential clinical implications
Biol. Chem.
391
403-409
2010
Homo sapiens
brenda
Ohler, A.; Debela, M.; Wagner, S.; Magdolen, V.; Becker-Pauly, C.
Analyzing the protease web in skin: meprin metalloproteases are activated specifically by KLK4, 5 and 8 vice versa leading to processing of proKLK7 thereby triggering its activation
Biol. Chem.
391
455-460
2010
Homo sapiens
brenda
Dong, Y.; Tan, O.L.; Loessner, D.; Stephens, C.; Walpole, C.; Boyle, G.M.; Parsons, P.G.; Clements, J.A.
Kallikrein-related peptidase 7 promotes multicellular aggregation via the alpha(5)beta(1) integrin pathway and paclitaxel chemoresistance in serous epithelial ovarian carcinoma
Cancer Res.
70
2624-2633
2010
Homo sapiens
brenda
Li, X.; Liu, J.; Wang, Y.; Zhang, L.; Ning, L.; Feng, Y.
Parallel underexpression of kallikrein 5 and kallikrein 7 mRNA in breast malignancies
Cancer Sci.
100
601-607
2009
Homo sapiens
brenda
Termini, L.; Maciag, P.C.; Soares, F.A.; Nonogaki, S.; Pereira, S.M.; Alves, V.A.; Longatto-Filho, A.; Villa, L.L.
Analysis of human kallikrein 7 expression as a potential biomarker in cervical neoplasia
Int. J. Cancer
127
485-490
2010
Homo sapiens
brenda
Morizane, S.; Yamasaki, K.; Kabigting, F.D.; Gallo, R.L.
Kallikrein expression and cathelicidin processing are independently controlled in keratinocytes by calcium, vitamin D3, and retinoic acid
J. Invest. Dermatol.
130
1297-1306
2010
Homo sapiens
brenda
Talieri, M.; Mathioudaki, K.; Prezas, P.; Alexopoulou, D.K.; Diamandis, E.P.; Xynopoulos, D.; Ardavanis, A.; Arnogiannaki, N.; Scorilas, A.
Clinical significance of kallikrein-related peptidase 7 (KLK7) in colorectal cancer
Thromb. Haemost.
101
741-747
2009
Homo sapiens
brenda
Ramani, V.C.; Kaushal, G.P.; Haun, R.S.
Proteolytic action of kallikrein-related peptidase 7 produces unique active matrix metalloproteinase-9 lacking the C-terminal hemopexin domains
Biochim. Biophys. Acta
1813
1525-1531
2011
Homo sapiens
brenda
Jamaspishvili, T.; Scorilas, A.; Kral, M.; Khomeriki, I.; Kurfurstova, D.; Kolar, Z.; Bouchal, J.
Immunohistochemical localization and analysis of kallikrein-related peptidase 7 and 11 expression in paired cancer and benign foci in prostate cancer patients
Neoplasma
58
298-303
2011
Homo sapiens
brenda
Oliveira, J.R.; Bertolin, T.C.; Andrade, D.; Oliveira, L.C.; Kondo, M.Y.; Santos, J.A.; Blaber, M.; Juliano, L.; Severino, B.; Caliendo, G.; Santagada, V.; Juliano, M.A.
Specificity studies on Kallikrein-related peptidase 7 (KLK7) and effects of osmolytes and glycosaminoglycans on its peptidase activity
Biochim. Biophys. Acta
1854
73-83
2015
Homo sapiens (P49862), Homo sapiens
brenda
Walker, F.; Nicole, P.; Jallane, A.; Soosaipillai, A.; Mosbach, V.; Oikonomopoulou, K.; Diamandis, E.P.; Magdolen, V.; Darmoul, D.
Kallikrein-related peptidase 7 (KLK7) is a proliferative factor that is aberrantly expressed in human colon cancer
Biol. Chem.
395
1075-1086
2014
Homo sapiens
brenda
Shropshire, T.D.; Reifert, J.; Rajagopalan, S.; Baker, D.; Feinstein, S.C.; Daugherty, P.S.
Amyloid ? peptide cleavage by kallikrein 7 attenuates fibril growth and rescues neurons from Abeta-mediated toxicity in vitro
Biol. Chem.
395
109-118
2014
Rattus norvegicus
brenda
Arama, D.; Soualmia, F.; Lisowski, V.; Longevial, J.; Bosc, E.; Maillard, L.; Martinez, J.; Masurier, N.; El Amri, C.
Pyrido-imidazodiazepinones as a new class of reversible inhibitors of human kallikrein 7
Eur. J. Med. Chem.
93
203-213
2015
Homo sapiens
-
brenda
Li, W.; Zhao, Y.; Ren, L.; Wu, X.
Serum human kallikrein 7 represents a new marker for cervical cancer
Med. Oncol.
31
208
2014
Homo sapiens
brenda
Zhang, C.; Zhu, Y.; Rui, W.; Dai, J.; Shen, Z.
Expression of kallikrein-related peptidase 7 is decreased in prostate cancer
Asian J. Androl.
17
106-110
2015
Homo sapiens (P49862), Homo sapiens
brenda
Haddada, M.; Draoui, H.; Deschamps, L.; Walker, F.; Delaunay, T.; Brattsand, M.; Magdolen, V.; Darmoul, D.
Kallikrein-related peptidase 7 overexpression in melanoma cells modulates cell adhesion leading to a malignant phenotype
Biol. Chem.
399
1099-1105
2018
Homo sapiens (P49862), Homo sapiens
brenda
Murafuji, H.; Muto, T.; Goto, M.; Imajo, S.; Sugawara, H.; Oyama, Y.; Minamitsuji, Y.; Miyazaki, S.; Murai, K.; Fujioka, H.
Discovery and structure-activity relationship of imidazolinylindole derivatives as kallikrein 7 inhibitors
Bioorg. Med. Chem. Lett.
29
334-338
2019
Homo sapiens (P49862), Homo sapiens, Mus musculus (Q91VE3), Mus musculus
brenda
Yu, Y.; Prassas, I.; Dimitromanolakis, A.; Diamandis, E.P.
Novel biological substrates of human kallikrein 7 identified through degradomics
J. Biol. Chem.
290
17762-17775
2015
Homo sapiens (P49862), Homo sapiens
brenda
de Veer, S.J.; Furio, L.; Swedberg, J.E.; Munro, C.A.; Brattsand, M.; Clements, J.A.; Hovnanian, A.; Harris, J.M.
Selective substrates and inhibitors for kallikrein-related peptidase 7 (KLK7) shed light on KLK proteolytic activity in the stratum corneum
J. Invest. Dermatol.
137
430-439
2017
Homo sapiens (P49862)
brenda
Silva, L.M.; Stoll, T.; Kryza, T.; Stephens, C.R.; Hastie, M.L.; Irving-Rodgers, H.F.; Dong, Y.; Gorman, J.J.; Clements, J.A.
Mass spectrometry-based determination of kallikrein-related peptidase 7 (KLK7) cleavage preferences and subsite dependency
Sci. Rep.
7
6789
2017
Homo sapiens (P49862), Homo sapiens
brenda
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 3.4.21.117)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
