Literature summary for 3.4.24.23 extracted from

Jang, B.; Yun, J.H.; Choi, S.; Park, J.; Shin, D.H.; Lee, S.T.; Lee, W.; Oh, E.S.
Tyrosine 51 residue of the syndecan-2 extracellular domain is involved in the interaction with and activation of pro-matrix metalloproteinase-7 (2019), Sci. Rep., 9, 10625 .

Search for more literature for 3.4.24.23

Cloned(Commentary)

Cloned (Comment)	Organism
recombinant expression of wild-type full-length, and deletion mutants, as well as isolated MMP-7 pro-domain as His-tagged proteins	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
additional information	generation of MMP-7 pro-domain mutants lacking the N-terminal linker of the pro-domain (DELTAN, residues 9-79), the C-terminal linker (DELTAC, residues 1-73), or both (DELTANC, residues 9-73), secondary structure homology modeling analysis. Mutant DELTANC retains the triple alpha-helical structure	Homo sapiens

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
cell surface	-	Homo sapiens	9986	-
extracellular	-	Homo sapiens	-	-

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Ca2+	required	Homo sapiens
Zn2+	a zinc metalloproteinase	Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
additional information	Homo sapiens	MMP-7 and syndecan-2 interaction analysis, mutational and NMR spectrometric analysis, overview. Interaction between the extracellular domain of syndecan-2 and the pro-domain of MMP-7	?	-	?

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
proteolytic modification	Tyr51 of the syndecan-2 extracellular domain mediates its interaction with and a and activating processing of pro-MMP-7 and regulates MMP-7-dependent syndecan-2 functions	Homo sapiens

Purification (Commentary)

Purification (Comment)	Organism
recombinant His-tagged wild-type full-length, His-tagged deletion mutants, and His-tagged MMP-7 pro-domain by nickel affinity chromatography	Homo sapiens

Source Tissue

Source Tissue	Comment	Organism	Textmining
colonic adenocarcinoma cell	overexpression of MMP-7	Homo sapiens	-
HT-29 cell	-	Homo sapiens	-
additional information	MMP-7 is overexpressed in a variety of epithelial cancers, such as stomach, liver, pancreatic, and colon cancer	Homo sapiens	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
(7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly-Leu-N-3(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-Ala-Arg-NH2 + H2O	-	Homo sapiens	(7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly + Leu-N-3(2,4-dinitrophenyl)-L-2,3-diaminopropionyl-Ala-Arg-NH2	-	?
additional information	MMP-7 and syndecan-2 interaction analysis, mutational and NMR spectrometric analysis, overview. Interaction between the extracellular domain of syndecan-2 and the pro-domain of MMP-7	Homo sapiens	?	-	?

Synonyms

Synonyms	Comment	Organism
Matrix metalloproteinase-7	-	Homo sapiens
MMP-7	-	Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
37	-	assay at	Homo sapiens

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.4	-	assay at	Homo sapiens

General Information

General Information	Comment	Organism
malfunction	MMP-7 pro-domain mutants lacking the N-terminal linker of the pro-domain (DELTAN, residues 9-79), the C-terminal linker (DELTAC, residues 1-73), or both (DELTANC, residues 9-73) interact with GST-tagged extracellular domain of syndecan-2 (S2E) in pulldown assays	Homo sapiens
metabolism	syndecans mediate the interaction between the ECM and the cell. Syndecan-2 regulates MMP-7 gene expression in colon cancer cells. The expression of a syndecan-2 mutant in which Tyr51 is changed to Ala diminishes the interaction between the syndecan-2 extracellular domain and the pro-domain of MMP-7. HT-29 colon adenocarcinoma cells expressing the interaction-defective mutant exhibit reductions in the cell-surface localization of MMP-7, the processing of pro-MMP-7 into active MMP-7, the MMP-7-mediated extracellular domain shedding of both syndecan-2 and E-cadherin, and syndecan-2-mediated anchorage-independent growth. Tyr51 of the syndecan-2 extracellular domain mediates its interaction with and a and activating processing of pro-MMP-7 and regulates MMP-7-dependent syndecan-2 functions. Syndecan-2 induces extracellular release of E-cadherin and supports the acquisition of a fibroblast-like morphology by regulation of MMP-7 in a colon cancer cell line	Homo sapiens
physiological function	the extracellular matrix (ECM) is the three-dimensional network that structurally and functionally integrates cells into tissues. Through its diversity in composition and physical nature, the ECM can perform many functions, such as providing support, separate tissues, and regulating intercellular communication. the matrix metalloproteinases (MMPs) perform important protease functions in extracellular matrix (ECM) degradation and remodeling. Matrix metalloproteinase-7 (MMP-7) plays a role in cancer progression. MMP-7 is overexpressed in a variety of epithelial cancers, such as stomach, liver, pancreatic, and colon cancer. Increased MMP-7 regulates cancer progression and invasion through regulating the proteolytic degradation of ECM molecules (e.g., elastin, type IV collagen, fibronectin, vitronectin, aggrecan, and proteoglycan), and non-ECM molecules (e.g., beta4 integrin, E-cadherin, FasL, proHB-EGF, and TNFalpha precursor). Syndecan-2 in association with MMP-7 regulates colon cancer activities. The N-terminal syndecan-2 extracellular domain directly interacts with the MMP-7 pro-domain, mutational analysis, overview	Homo sapiens

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Release 2023.1 (January 2023)