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Literature summary for 3.4.24.14 extracted from

  • Bekhouche, M.; Colige, A.
    The procollagen N-proteinases ADAMTS2, 3 and 14 in pathophysiology (2015), Matrix Biol., 44-46C, 46-53.
    View publication on PubMed
Search for more literature for 3.4.24.14

Activating Compound

Activating Compound Comment Organism Structure
additional information proteolytic cleavage is required for enzyme activation, an autocatalytic cleavage occurring within the carboxy-terminal end, possibly in the PNP-domain, increases its activity Bos taurus
additional information proteolytic cleavage is required for enzyme activation, an autocatalytic cleavage occurring within the carboxy-terminal end, possibly in the PNP-domain, increases its activity Homo sapiens
additional information proteolytic cleavage is required for enzyme activation, an autocatalytic cleavage occurring within the carboxy-terminal end, possibly in the PNP-domain, increases its activity Mus musculus
additional information proteolytic cleavage is required for enzyme activation, an autocatalytic cleavage occurring within the carboxy-terminal end, possibly in the PNP-domain, increases its activity Rattus norvegicus
additional information proteolytic cleavage is required for enzyme activation, an autocatalytic cleavage occurring within the carboxy-terminal end, possibly in the PNP-domain, increases its activity Sus scrofa
additional information proteolytic cleavage is required for enzyme activation, an autocatalytic cleavage occurring within the carboxy-terminal end, possibly in the PNP-domain, increases its activity Ovis aries

Cloned(Commentary)

Cloned (Comment) Organism
gene ADAMTS14, alternative splicing is possible Bos taurus
gene ADAMTS14, alternative splicing is possible Homo sapiens
gene ADAMTS2, alternative splicing is possible Bos taurus
gene ADAMTS2, sequence comparisons Canis lupus familiaris
gene ADAMTS2, sequence comparisons, alternative splicing is possible Gallus gallus
gene ADAMTS2, sequence comparisons, alternative splicing is possible Homo sapiens
gene ADAMTS2, sequence comparisons, alternative splicing is possible Mus musculus
gene ADAMTS2, sequence comparisons, alternative splicing is possible Rattus norvegicus
gene ADAMTS2, sequence comparisons, alternative splicing is possible Sus scrofa
gene ADAMTS2, sequence comparisons, alternative splicing is possible Ovis aries
gene ADAMTS3 Bos taurus
gene ADAMTS3 Homo sapiens

Protein Variants

Protein Variants Comment Organism
additional information in vivo, the formation of tumors in nude mice by HEK cells is strongly reduced when they overexpress ADAMTS2, an observation that is correlated to a reduced intratumoral vascularization but that can also involve direct anti-tumor effects Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
papilin
-
 Bos taurus
papilin
-
 Canis lupus familiaris
papilin
-
 Gallus gallus
papilin
-
 Homo sapiens
papilin
-
 Mus musculus
papilin
-
 Ovis aries
papilin
-
 Rattus norvegicus
papilin
-
 Sus scrofa
TIMP3
-
 Bos taurus
TIMP3
-
 Canis lupus familiaris
TIMP3
-
 Gallus gallus
TIMP3
-
 Homo sapiens
TIMP3
-
 Mus musculus
TIMP3
-
 Ovis aries
TIMP3
-
 Rattus norvegicus
TIMP3
-
 Sus scrofa

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular collagen and extracellular matrix Gallus gallus
-
-
extracellular collagen and extracellular matrix Bos taurus
-
-
extracellular collagen and extracellular matrix Canis lupus familiaris
-
-
extracellular collagen and extracellular matrix Homo sapiens
-
-
extracellular collagen and extracellular matrix Mus musculus
-
-
extracellular collagen and extracellular matrix Rattus norvegicus
-
-
extracellular collagen and extracellular matrix Sus scrofa
-
-
extracellular collagen and extracellular matrix Ovis aries
-
-
additional information identification of nucleolin as a potential endothelial cell surface receptor for ADAMTS2 Homo sapiens
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ required Gallus gallus
Ca2+ required Bos taurus
Ca2+ required Canis lupus familiaris
Ca2+ required Homo sapiens
Ca2+ required Mus musculus
Ca2+ required Rattus norvegicus
Ca2+ required Sus scrofa
Ca2+ required Ovis aries
Zn2+ required Gallus gallus
Zn2+ required Bos taurus
Zn2+ required Canis lupus familiaris
Zn2+ required Homo sapiens
Zn2+ required Mus musculus
Zn2+ required Rattus norvegicus
Zn2+ required Sus scrofa
Zn2+ required Ovis aries

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Bos taurus ADAMTS14 processes type I procollagen (alpha1 and alpha2 chains) and its strong sequence homology with ADAMTS2 suggests that the cleavage should occur at the same site ?
-
 ?
additional information Homo sapiens ADAMTS14 processes type I procollagen (alpha1 and alpha2 chains) and its strong sequence homology with ADAMTS2 suggests that the cleavage should occur at the same site ?
-
 ?
additional information Homo sapiens ADAMTS3 cleaves the aminopropeptide of type II collagen in swarm rat chondrosarcoma RCS-LTC cells stably transfected with human ADAMTS3 ?
-
 ?
additional information Bos taurus sequence homology of ADAMTS2 cleavage sites in alpha chain types I-III fibrillar collagens from different species, overview. The bovine enzyme ADAMTS2 cleaves at sites 158NFAP-/-QLSY165 in chain alpha1(I), and at 178NFAA-/-QMAG185 in chain alpha1(II), as well as at 76NFAA-/-QFDA83 in chains alpha2(I), respectively ?
-
 ?
additional information Gallus gallus sequence homology of ADAMTS2 cleavage sites in alpha chain types I-III fibrillar collagens from different species, overview. The chicken enzyme ADAMTS2 cleaves at sites 148NFAP-/-QMSY155 in chain alpha1(I), as well as at 74NFAA-/-QYDP81 in chains alpha2(I) ?
-
 ?
additional information Canis lupus familiaris sequence homology of ADAMTS2 cleavage sites in alpha chain types I-III fibrillar collagens from different species, overview. The dog enzyme ADAMTS2 cleaves at sites 154NFAP-/-QMSY161 in chain alpha1(I), and at 147FSP-/-QYDS154 in chain alpha1(III), as well as at 76NFAA-/-QYDG83 in chains alpha2(I) ?
-
 ?
additional information Homo sapiens sequence homology of ADAMTS2 cleavage sites in alpha chain types I-III fibrillar collagens from different species, overview. The human enzyme ADAMTS2 cleaves at sites 158NFAP-/-QLSY165 in chain alpha1(I), at 178NFAA-/-QMAG185 in chain alpha1(II), and at 150NYSP-/-QYDS157 in chain alpha1(III), as well as at 76NFAA-/-QYDG83 in chains alpha2(I), respectively ?
-
 ?
additional information Mus musculus sequence homology of ADAMTS2 cleavage sites in alpha chain types I-III fibrillar collagens from different species, overview. The murine enzyme ADAMTS2 cleaves at sites 148NFAS-/-QMSY155 in chain alpha1(I), at 178NFAA-/-QMAG185 in chain alpha1(II), and at 151NYSP-/-QFDS158 in chain alpha1(III), as well as at 81NFAA-/-QYSD89 in chains alpha2(I), respectively ?
-
 ?
additional information Rattus norvegicus sequence homology of ADAMTS2 cleavage sites in alpha chain types I-III fibrillar collagens from different species, overview. The rat enzyme ADAMTS2 cleaves at sites 148NFAS-/-QMSY155 in chain alpha1(I), at 110NFAA-/-QMAG117 in chain alpha1(II), and at 15NYSP-/-QFDS158 in chain alpha1(III), as well as at 81NFAA-/-QYSD89 in chains alpha2(I), respectively ?
-
 ?
pro-collagen + H2O Gallus gallus
-
 collagen + collagen N-propeptide
-
 ?
pro-collagen + H2O Bos taurus
-
 collagen + collagen N-propeptide
-
 ?
pro-collagen + H2O Canis lupus familiaris
-
 collagen + collagen N-propeptide
-
 ?
pro-collagen + H2O Homo sapiens
-
 collagen + collagen N-propeptide
-
 ?
pro-collagen + H2O Mus musculus
-
 collagen + collagen N-propeptide
-
 ?
pro-collagen + H2O Rattus norvegicus
-
 collagen + collagen N-propeptide
-
 ?
pro-collagen + H2O Sus scrofa
-
 collagen + collagen N-propeptide
-
 ?
pro-collagen + H2O Ovis aries
-
 collagen + collagen N-propeptide
-
 ?

Organism

Organism UniProt Comment Textmining
Bos taurus E1BC50 gene ADAMTS3; gene ADAMTS3
-
Bos taurus E1BFV4 gene ADAMTS14; gene ADAMTS14
-
Bos taurus P79331 gene ADAMTS2; gene ADAMTS2
-
Canis lupus familiaris E2R8G2 gene ADAMTS2; gene ADAMTS2
-
Gallus gallus
-
 gene ADAMTS2; gene ADAMTS2
-
Homo sapiens O15072 gene ADAMTS3; gene ADAMTS3
-
Homo sapiens O95450 gene ADAMTS2; gene ADAMTS2
-
Homo sapiens Q8WXS8 gene ADAMTS14; gene ADAMTS14
-
Mus musculus Q8C9W3 gene ADAMTS2; gene ADAMTS2
-
Ovis aries W5P0Z2 gene ADAMTS2; gene ADAMTS2
-
Rattus norvegicus D3ZTE7 gene ADAMTS2; gene ADAMTS2
-
Sus scrofa I3LAK9 gene ADAMTS2; gene ADAMTS2
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification ADAMTS2 is synthesized as an inactive proenzyme which is activated by mammalian subtilisins, such as furin, which cleave between the prodomain and the metalloproteinase domain Bos taurus
proteolytic modification ADAMTS2 is synthesized as an inactive proenzyme which is activated by mammalian subtilisins, such as furin, which cleave between the prodomain and the metalloproteinase domain Homo sapiens
proteolytic modification ADAMTS2 is synthesized as an inactive proenzyme which is activated by mammalian subtilisins, such as furin, which cleave between the prodomain and the metalloproteinase domain Mus musculus
proteolytic modification ADAMTS2 is synthesized as an inactive proenzyme which is activated by mammalian subtilisins, such as furin, which cleave between the prodomain and the metalloproteinase domain Rattus norvegicus
proteolytic modification ADAMTS2 is synthesized as an inactive proenzyme which is activated by mammalian subtilisins, such as furin, which cleave between the prodomain and the metalloproteinase domain Sus scrofa
proteolytic modification ADAMTS2 is synthesized as an inactive proenzyme which is activated by mammalian subtilisins, such as furin, which cleave between the prodomain and the metalloproteinase domain Ovis aries

Source Tissue

Source Tissue Comment Organism Textmining
blood vessel
-
 Homo sapiens
-
cartilage
-
 Bos taurus
-
endothelial cell enzyme expression Homo sapiens
-
macrophage enzyme expression Homo sapiens
-
macrophage enzyme expression, overexpression by macrophages and peripheral blood monocytes stimulated by glucocorticoids Homo sapiens
-
monocyte overexpression by macrophages and peripheral blood monocytes stimulated by glucocorticoids Homo sapiens
-
additional information ADAMTS14 is usually co-expressed with ADAMTS2, although at a lower level, suggesting potential functional redundancy Bos taurus
-
additional information ADAMTS2 and ADAMTS3, but not ADAMTS14, are more abundant in the culprit plaques from patients presenting with acute myocardial infarction versus stable angina Homo sapiens
-
additional information ADAMTS3 is mainly expressed in cartilage, where it colocalizes with type II procollagen, and in the nervous system Bos taurus
-
nervous system
-
 Bos taurus
-
skin
-
 Gallus gallus
-
skin
-
 Bos taurus
-
skin
-
 Canis lupus familiaris
-
skin
-
 Homo sapiens
-
skin
-
 Mus musculus
-
skin
-
 Rattus norvegicus
-
skin
-
 Sus scrofa
-
skin
-
 Ovis aries
-
skin high expression of ADAMTS2 is detected in all type I collagen-rich tissues from fetal calf such as skin, bones, tendons and aorta, which supports its importance for type I collagen maturation Bos taurus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information ADAMTS14 processes type I procollagen (alpha1 and alpha2 chains) and its strong sequence homology with ADAMTS2 suggests that the cleavage should occur at the same site Bos taurus ?
-
 ?
additional information ADAMTS14 processes type I procollagen (alpha1 and alpha2 chains) and its strong sequence homology with ADAMTS2 suggests that the cleavage should occur at the same site Homo sapiens ?
-
 ?
additional information ADAMTS3 cleaves the aminopropeptide of type II collagen in swarm rat chondrosarcoma RCS-LTC cells stably transfected with human ADAMTS3 Homo sapiens ?
-
 ?
additional information sequence homology of ADAMTS2 cleavage sites in alpha chain types I-III fibrillar collagens from different species, overview. The bovine enzyme ADAMTS2 cleaves at sites 158NFAP-/-QLSY165 in chain alpha1(I), and at 178NFAA-/-QMAG185 in chain alpha1(II), as well as at 76NFAA-/-QFDA83 in chains alpha2(I), respectively Bos taurus ?
-
 ?
additional information sequence homology of ADAMTS2 cleavage sites in alpha chain types I-III fibrillar collagens from different species, overview. The chicken enzyme ADAMTS2 cleaves at sites 148NFAP-/-QMSY155 in chain alpha1(I), as well as at 74NFAA-/-QYDP81 in chains alpha2(I) Gallus gallus ?
-
 ?
additional information sequence homology of ADAMTS2 cleavage sites in alpha chain types I-III fibrillar collagens from different species, overview. The dog enzyme ADAMTS2 cleaves at sites 154NFAP-/-QMSY161 in chain alpha1(I), and at 147FSP-/-QYDS154 in chain alpha1(III), as well as at 76NFAA-/-QYDG83 in chains alpha2(I) Canis lupus familiaris ?
-
 ?
additional information sequence homology of ADAMTS2 cleavage sites in alpha chain types I-III fibrillar collagens from different species, overview. The human enzyme ADAMTS2 cleaves at sites 158NFAP-/-QLSY165 in chain alpha1(I), at 178NFAA-/-QMAG185 in chain alpha1(II), and at 150NYSP-/-QYDS157 in chain alpha1(III), as well as at 76NFAA-/-QYDG83 in chains alpha2(I), respectively Homo sapiens ?
-
 ?
additional information sequence homology of ADAMTS2 cleavage sites in alpha chain types I-III fibrillar collagens from different species, overview. The murine enzyme ADAMTS2 cleaves at sites 148NFAS-/-QMSY155 in chain alpha1(I), at 178NFAA-/-QMAG185 in chain alpha1(II), and at 151NYSP-/-QFDS158 in chain alpha1(III), as well as at 81NFAA-/-QYSD89 in chains alpha2(I), respectively Mus musculus ?
-
 ?
additional information sequence homology of ADAMTS2 cleavage sites in alpha chain types I-III fibrillar collagens from different species, overview. The rat enzyme ADAMTS2 cleaves at sites 148NFAS-/-QMSY155 in chain alpha1(I), at 110NFAA-/-QMAG117 in chain alpha1(II), and at 15NYSP-/-QFDS158 in chain alpha1(III), as well as at 81NFAA-/-QYSD89 in chains alpha2(I), respectively Rattus norvegicus ?
-
 ?
pro-collagen + H2O
-
 Gallus gallus collagen + collagen N-propeptide
-
 ?
pro-collagen + H2O
-
 Bos taurus collagen + collagen N-propeptide
-
 ?
pro-collagen + H2O
-
 Canis lupus familiaris collagen + collagen N-propeptide
-
 ?
pro-collagen + H2O
-
 Homo sapiens collagen + collagen N-propeptide
-
 ?
pro-collagen + H2O
-
 Mus musculus collagen + collagen N-propeptide
-
 ?
pro-collagen + H2O
-
 Rattus norvegicus collagen + collagen N-propeptide
-
 ?
pro-collagen + H2O
-
 Sus scrofa collagen + collagen N-propeptide
-
 ?
pro-collagen + H2O
-
 Ovis aries collagen + collagen N-propeptide
-
 ?

Synonyms

Synonyms Comment Organism
ADAMTS14
-
 Bos taurus
ADAMTS14
-
 Homo sapiens
ADAMTS2
-
 Gallus gallus
ADAMTS2
-
 Bos taurus
ADAMTS2
-
 Canis lupus familiaris
ADAMTS2
-
 Homo sapiens
ADAMTS2
-
 Mus musculus
ADAMTS2
-
 Rattus norvegicus
ADAMTS2
-
 Sus scrofa
ADAMTS2
-
 Ovis aries
ADAMTS3
-
 Bos taurus
ADAMTS3
-
 Homo sapiens
procollagen N-proteinase
-
 Gallus gallus
procollagen N-proteinase
-
 Bos taurus
procollagen N-proteinase
-
 Canis lupus familiaris
procollagen N-proteinase
-
 Homo sapiens
procollagen N-proteinase
-
 Mus musculus
procollagen N-proteinase
-
 Rattus norvegicus
procollagen N-proteinase
-
 Sus scrofa
procollagen N-proteinase
-
 Ovis aries

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
additional information
-
 the enzyme requires a neutral to slightly basic pH for activity Gallus gallus
additional information
-
 the enzyme requires a neutral to slightly basic pH for activity Bos taurus
additional information
-
 the enzyme requires a neutral to slightly basic pH for activity Canis lupus familiaris
additional information
-
 the enzyme requires a neutral to slightly basic pH for activity Homo sapiens
additional information
-
 the enzyme requires a neutral to slightly basic pH for activity Mus musculus
additional information
-
 the enzyme requires a neutral to slightly basic pH for activity Rattus norvegicus
additional information
-
 the enzyme requires a neutral to slightly basic pH for activity Sus scrofa
additional information
-
 the enzyme requires a neutral to slightly basic pH for activity Ovis aries

Expression

Organism Comment Expression
Homo sapiens enzyme exxpression is upregulated by glucocorticoids up

General Information

General Information Comment Organism
evolution the enzyme belongs to the a disintegrin and metalloproteinase with thrombospondin type I domain proteases (ADAMTS) family, M12B ADAM branch Bos taurus
evolution the enzyme belongs to the a disintegrin and metalloproteinase with thrombospondin type I domain proteases (ADAMTS) family, M12B ADAM branch Homo sapiens
evolution the enzyme belongs to the a disintegrin and metalloproteinase with thrombospondin type I domain proteases (ADAMTS) family, M12B ADAM branch Mus musculus
evolution the enzyme belongs to the disintegrin A and metalloproteinase with thrombospondin type I domain proteases (ADAMTS) family, M12B ADAM branch Gallus gallus
evolution the enzyme belongs to the disintegrin A and metalloproteinase with thrombospondin type I domain proteases (ADAMTS) family, M12B ADAM branch Rattus norvegicus
evolution the enzyme belongs to the disintegrin A and metalloproteinase with thrombospondin type I domain proteases (ADAMTS) family, M12B ADAM branch Sus scrofa
evolution the enzyme belongs to the disintegrin A and metalloproteinase with thrombospondin type I domain proteases (ADAMTS) family, M12B ADAM branch Ovis aries
malfunction Adamts2-deficient mice phenotype, overview. The absence of ADAMTS2 activity leads to the dermatosparactic type of Ehlers-Danlos syndrome, also previously known as EDS-type VIIC Mus musculus
malfunction the absence of ADAMTS2 activity leads to the dermatosparactic type of Ehlers-Danlos syndrome, also previously known as EDS-type VIIC Homo sapiens
additional information the activity of proteinases can be controlled by mechanisms such as clearing by internalization into cells or co-localization with their substrates ADAMTS2, 3 and 14, although being secreted, are immobilized at the cell surface, or very close to it, at a location where procollagen processing is physiologically performed. The ancillary domains, especially the second TSR1, are required for efficient interactions with the cell layer compartment and with extracellular matrix components Gallus gallus
additional information the activity of proteinases can be controlled by mechanisms such as clearing by internalization into cells or co-localization with their substrates ADAMTS2, 3 and 14, although being secreted, are immobilized at the cell surface, or very close to it, at a location where procollagen processing is physiologically performed. The ancillary domains, especially the second TSR1, are required for efficient interactions with the cell layer compartment and with extracellular matrix components Bos taurus
additional information the activity of proteinases can be controlled by mechanisms such as clearing by internalization into cells or co-localization with their substrates ADAMTS2, 3 and 14, although being secreted, are immobilized at the cell surface, or very close to it, at a location where procollagen processing is physiologically performed. The ancillary domains, especially the second TSR1, are required for efficient interactions with the cell layer compartment and with extracellular matrix components Canis lupus familiaris
additional information the activity of proteinases can be controlled by mechanisms such as clearing by internalization into cells or co-localization with their substrates ADAMTS2, 3 and 14, although being secreted, are immobilized at the cell surface, or very close to it, at a location where procollagen processing is physiologically performed. The ancillary domains, especially the second TSR1, are required for efficient interactions with the cell layer compartment and with extracellular matrix components Homo sapiens
additional information the activity of proteinases can be controlled by mechanisms such as clearing by internalization into cells or co-localization with their substrates ADAMTS2, 3 and 14, although being secreted, are immobilized at the cell surface, or very close to it, at a location where procollagen processing is physiologically performed. The ancillary domains, especially the second TSR1, are required for efficient interactions with the cell layer compartment and with extracellular matrix components Mus musculus
additional information the activity of proteinases can be controlled by mechanisms such as clearing by internalization into cells or co-localization with their substrates ADAMTS2, 3 and 14, although being secreted, are immobilized at the cell surface, or very close to it, at a location where procollagen processing is physiologically performed. The ancillary domains, especially the second TSR1, are required for efficient interactions with the cell layer compartment and with extracellular matrix components Rattus norvegicus
additional information the activity of proteinases can be controlled by mechanisms such as clearing by internalization into cells or co-localization with their substrates ADAMTS2, 3 and 14, although being secreted, are immobilized at the cell surface, or very close to it, at a location where procollagen processing is physiologically performed. The ancillary domains, especially the second TSR1, are required for efficient interactions with the cell layer compartment and with extracellular matrix components Sus scrofa
additional information the activity of proteinases can be controlled by mechanisms such as clearing by internalization into cells or co-localization with their substrates ADAMTS2, 3 and 14, although being secreted, are immobilized at the cell surface, or very close to it, at a location where procollagen processing is physiologically performed. The ancillary domains, especially the second TSR1, are required for efficient interactions with the cell layer compartment and with extracellular matrix components Ovis aries
physiological function ADAMTS14, which is coexpressed with ADAMTS2 in different connective tissues, might be responsible for this partial alternative aminoprocollagen endopeptidase activity Bos taurus
physiological function ADAMTS14, which is coexpressed with ADAMTS2 in different connective tissues, might be responsible for this partial alternative aminoprocollagen endopeptidase activity. Adamts14 gene is potentially implicated in knee osteoarthritis in women. The Adamts14 gene seem to be linked to the predisposition to multiple sclerosis Homo sapiens
physiological function ADAMTS3 promotes the release of a proteolytically cleaved active form of VEGF-C, a process that increases VEGF-R3 signaling Bos taurus
physiological function ADAMTS3 promotes the release of a proteolytically cleaved active form of VEGF-C, a process that increases VEGF-R3 signaling Homo sapiens
physiological function enzyme ADAMTS2 is crucial for fibrillar collagen organization, overview Canis lupus familiaris
physiological function enzyme ADAMTS2 is crucial for fibrillar collagen organization, overview. ADAMTS2 induces the apoptosis of endothelial cells by a mechanism independent of its catalytic activity but potentially related to interactions with a cell surface receptor Gallus gallus
physiological function enzyme ADAMTS2 is crucial for fibrillar collagen organization, overview. ADAMTS2 induces the apoptosis of endothelial cells by a mechanism independent of its catalytic activity but potentially related to interactions with a cell surface receptor. ADAMTS2 shows potent anti-angiogenic activity Bos taurus
physiological function enzyme ADAMTS2 is crucial for fibrillar collagen organization, overview. ADAMTS2 induces the apoptosis of endothelial cells by a mechanism independent of its catalytic activity but potentially related to interactions with a cell surface receptor. ADAMTS2 shows potent anti-angiogenic activity Mus musculus
physiological function enzyme ADAMTS2 is crucial for fibrillar collagen organization, overview. ADAMTS2 induces the apoptosis of endothelial cells by a mechanism independent of its catalytic activity but potentially related to interactions with a cell surface receptor. ADAMTS2 shows potent anti-angiogenic activity Rattus norvegicus
physiological function enzyme ADAMTS2 is crucial for fibrillar collagen organization, overview. ADAMTS2 induces the apoptosis of endothelial cells by a mechanism independent of its catalytic activity but potentially related to interactions with a cell surface receptor. ADAMTS2 shows potent anti-angiogenic activity Sus scrofa
physiological function enzyme ADAMTS2 is crucial for fibrillar collagen organization, overview. ADAMTS2 induces the apoptosis of endothelial cells by a mechanism independent of its catalytic activity but potentially related to interactions with a cell surface receptor. ADAMTS2 shows potent anti-angiogenic activity Ovis aries
physiological function enzyme ADAMTS2 is crucial for fibrillar collagen organization, overview. ADAMTS2 induces the apoptosis of endothelial cells by a mechanism independent of its catalytic activity but potentially related to interactions with a cell surface receptor. ADAMTS2 shows potent anti-angiogenic activity. In vivo, the formation of tumors in nude mice by HEK cells is strongly reduced when they overexpress ADAMTS2, an observation that is correlated to a reduced intratumoral vascularization but that can also involve direct anti-tumor effects Homo sapiens