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metabolism
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the N-propeptides of collagen are removed first, most probably in the Golgi or in the ERGIC (ER-Golgi intermediate compartment). In contrast, the C-propeptides are cleaved in a post-Golgi compartment
evolution
the enzyme belongs to the a disintegrin and metalloproteinase with thrombospondin type I domain proteases (ADAMTS) family, M12B ADAM branch
evolution
the enzyme belongs to the a disintegrin and metalloproteinase with thrombospondin type I domain proteases (ADAMTS) family, M12B ADAM branch
evolution
the enzyme belongs to the a disintegrin and metalloproteinase with thrombospondin type I domain proteases (ADAMTS) family, M12B ADAM branch
evolution
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the enzyme belongs to the disintegrin A and metalloproteinase with thrombospondin type I domain proteases (ADAMTS) family, M12B ADAM branch
evolution
the enzyme belongs to the disintegrin A and metalloproteinase with thrombospondin type I domain proteases (ADAMTS) family, M12B ADAM branch
evolution
the enzyme belongs to the disintegrin A and metalloproteinase with thrombospondin type I domain proteases (ADAMTS) family, M12B ADAM branch
evolution
the enzyme belongs to the disintegrin A and metalloproteinase with thrombospondin type I domain proteases (ADAMTS) family, M12B ADAM branch
evolution
the procollagen N-propeptidase belongs to the 'a disintegrin and metalloproteinase with thrombospondin type I domain' proteases (ADAMTS) family, M12B ADAM branch. Beside their specific enzymatic activity, the members are characterized by the presence of four thrombospondin type I domains (TSR1) and a C-terminal procollagen N-proteinase (PNP) domain comprising a protease-and-lacunin (PLAC) domain
evolution
the procollagen N-propeptidase belongs to the 'a disintegrin and metalloproteinase with thrombospondin type I domain' proteases (ADAMTS) family, M12B ADAM branch. Beside their specific enzymatic activity, the members are characterized by the presence of four thrombospondin type I domains (TSR1) and a C-terminal procollagen N-proteinase (PNP) domain comprising a protease-and-lacunin (PLAC) domain. ADAMTS14 is coexpressed with ADAMTS2
evolution
the procollagen N-propeptidase belongs to the 'a disintegrin and metalloproteinase with thrombospondin type I domain' proteases (ADAMTS) family, M12B ADAM branch. Beside their specific enzymatic activity, the members are characterized by the presence of four thrombospondin type I domains (TSR1) and a C-terminal procollagen N-proteinase (PNP) domain comprising a protease-and-lacunin (PLAC) domain. ADAMTS14 is coexpressed with ADAMTS2
malfunction
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mice with inactivation of both alleles of procollagen N-proteinase (ADAMTS-2) exhibit no difference between knockout mice and their wild type littermates
malfunction
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an anti-tumoral activity is also observed when using cells expressing recombinant deleted forms of ADAMTS-2, including catalytically inactive enzyme
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
malfunction
the absence of ADAMTS2 activity leads to the dermatosparactic type of Ehlers-Danlos syndrome, also previously known as EDS-type VIIC
malfunction
ADAMTS 3, one of the procollagen proteinases, is decreased in severe obstructive sleep apnea (OSA), overview. Lack of ADAMTS 3 proteinase may contribute to process of sleep apnea due to insufficient collagen syntheses
malfunction
in absence of ADAMTS2 activity (Ehlers-Danlos syndrome, dermatosparactic type) accumulation of processed alpha alpha1 and alpha2 chains, pNalpha1 and pNalpha2, is observed
malfunction
in Adamts2-KO mouse livers, collagen fibers are thinner and more irregular than in the control littermates, which correlated also with faster collagen degradation. Fragility of the skin occurs in Adamts2-KO mice
malfunction
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 might also involve direct anti-tumor effects. The absence of ADAMTS2 activity leads to a different type of disease, the dermatosparactic type of Ehlers-Danlos syndrome (EDS, also previously known as EDS-type VIIC). The main clinical manifestation of this rare genetic disease is the fragility of the skin, as in Adamts2-KO mice, but joint laxity is usually only moderate, which contrasts with the hypermobility in arthrochalasic EDS. The arthrochalasic type of EDS, caused by mutations affecting the aminoprocollagen cleavage site in alpha1 or alpha2 type I procollagen, is mainly characterized by joint hyperlaxity while skin collagen fibers are only moderately affected. EDS phenotypes, overview
malfunction
mice lacking ADAMTS2 display exacerbate cardiac hypertrophy on pressure overload-induced hypertrophic response, whereas mice with cardiac-specific overexpression of ADAMTS2 display alleviation of this detrimental phenotype. A murine model of aortic banding (AB)-induced cardiac hypertrophy, shows that mice after 4-week AB-treatment exhibit dramatically increased ADAMTS2 protein expression. Loss of ADAMTS2 (ADAMTS2-KO mice) aggravates pressure overload-induced hypertrophy
malfunction
overexpression of ADAMTS2 in cultured neonatal rat cardiomyocytes (NRCMs) results in markedly decreased cell sizes compared with those of cells in the control group
physiological function
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both long and short forms of the procollagen C-proteinase enhancers netrin-like (PCPE-1 NTR) domain show no inhibition, at micromolar concentrations, of several members of the metzincin superfamily, including matrix metalloproteinase-2, bone morphogenetic protein-1, and different ADAMTS-2, ADAMTS-4 or ADAMTS-5
physiological function
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ADAMTS-2 functions as anti-angiogenic and anti-tumoral molecule independently of its catalytic activity
physiological function
ADAMTS14, which is coexpressed with ADAMTS2 in different connective tissues, might be responsible for this partial alternative aminoprocollagen endopeptidase activity
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
physiological function
ADAMTS3 promotes the release of a proteolytically cleaved active form of VEGF-C, a process that increases VEGF-R3 signaling
physiological function
ADAMTS3 promotes the release of a proteolytically cleaved active form of VEGF-C, a process that increases VEGF-R3 signaling
physiological function
E2R8G2
enzyme ADAMTS2 is crucial for fibrillar collagen organization, overview
physiological function
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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
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
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
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
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
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
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
physiological function
'a disintegrin and metalloproteinase with thrombospondin type-1 motifs' (ADAMTS) proteinases have important roles in degradation/repairing of extracellular matrix (ECM). They are thought to play a key role in pathogenesis of many diseases
physiological function
ADAMTS2 (a disintegrin and metalloproteinase with thrombospondin motifs 2) is recognized as a metalloproteinase that promotes the cleavage of amino propeptides of types I, II, III, and V procollagens. ADAMTS2 regulates the hypertrophic response through inhibiting the activation of the PI3K/AKT-dependent signaling pathway
physiological function
ADAMTS2 (a disintegrin and metalloproteinase with thrombospondin motifs 2) is recognized as a metalloproteinase that promotes the cleavage of amino propeptides of types I, II, III, and V procollagens. ADAMTS2 regulates the hypertrophic response through inhibiting the activation of the PI3K/AKT-dependent signaling pathway. ADAMTS2 decreases AKT phosphorylation on hypertrophic stress
physiological function
ADAMTS2 (a disintegrin and metalloproteinase with thrombospondin motifs 2) is recognized as a metalloproteinase that promotes the cleavage of amino propeptides of types I, II, III, and V procollagens. ADAMTS2 regulates the hypertrophic response through inhibiting the activation of the PI3K/AKT-dependent signaling pathway. ADAMTS2 modulates Ang II-induced cultured neonatal rat cardiomyocytes (NRCMs) hypertrophy in vitro
physiological function
ADAMTS2 and ADAMTS3, but not ADAMTS14, are more abundant in the culprit plaques from patients presenting with acute myocardial infarction (AMI) versus stable angina. Their expression overlap the area positive for CD31 or CD68 suggesting their expression by endothelial cells or macrophages. The Adamts14 gene is potentially implicated in knee osteoarthritis in woman
physiological function
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 by one of its C-terminal domains. The role of ADAMTS2 is crucial for collagen fibrils formation
physiological function
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 by one of its C-terminal domains. The role of ADAMTS2 is crucial for collagen fibrils formation. ADAMTS2 and ADAMTS3, but not ADAMTS14, are more abundant in the culprit plaques from patients presenting with acute myocardial infarction (AMI) versus stable angina. Their expression overlap the area positive for CD31 or CD68 suggesting their expression by endothelial cells or macrophages
physiological function
ADAMTS3 promotes the release of a proteolytically cleaved active form of VEGF-C, a process that increases VEGF-R3 signaling. ADAMTS2 and ADAMTS3, but not ADAMTS14, are more abundant in the culprit plaques from patients presenting with acute myocardial infarction (AMI) versus stable angina. Their expression overlap the area positive for CD31 or CD68 suggesting their expression by endothelial cells or macrophages
physiological function
type I collagen is a heterotrimer composed of 2 alpha1 chains and one alpha2 chain (which are the products of different genes) forming a typical triple helical domain. Besides the removal of the signal peptide, the maturation of type I procollagen into mature alpha chains involves cleavages of the aminopropeptide and the carboxypropeptide by aminoprocollagen peptidases (mainly ADAMTS2) and carboxyprocollagen peptidases (BMP1 and tolloids), respectively. In vivo in physiological conditions, only the fully processed alpha alpha1 and alpha2 chains are present in significant amounts. The excision of the aminopropeptide by ADAMTS2 converts the pro-chains into pC-chains, and the pN-chains into mature alpha chains
physiological function
type I collagen is a heterotrimer composed of 2 alpha1 chains and one alpha2 chain (which are the products of different genes) forming a typical triple helical domain. Besides the removal of the signal peptide, the maturation of type I procollagen into mature alpha chains involves cleavages of the aminopropeptide and the carboxypropeptide by aminoprocollagen peptidases (mainly ADAMTS2) and carboxyprocollagen peptidases (BMP1 and tolloids), respectively. In vivo in physiological conditions, only the fully processed alpha alpha1 and alpha2 chains are present in significant amounts. The excision of the aminopropeptide by ADAMTS2 converts the pro-chains into pC-chains, and the pN-chains into mature alpha chains
additional information
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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
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
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
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
additional information
E2R8G2
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
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
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
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
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
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
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
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