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Fibronectin + H2O
?
release of the 33 kDa fibronectin fragment
-
-
?
fibulin-2 + H2O
?
-
-
-
?
fibulin-3 + H2O
?
-
-
-
?
lysyl oxidase + H2O
?
-
-
-
?
lysyl oxidase homologue 1 + H2O
?
-
-
-
?
pNcollagen
pCCollagen + oligopeptide
pNcollagen I + H2O
?
-
-
-
-
?
pNcollagen, carboxymethylated + H2O
?
-
pN collagen is collagen containing the N-terminal pro- peptide only
-
-
?
pro-collagen + H2O
collagen + collagen N-propeptide
procollagen I + H2O
pCCollagen I + oligopeptide
procollagen II + H2O
pCCollagen II + oligopeptide
procollagen III + H2O
pCCollagen III + oligopeptide
-
removes the N-terminal propeptide from the native procollagen III, ADAMTS2 purified from skin is unable to process type III procollagen despite its activity on type I procollagen
-
-
?
procollagen V + H2O
pCCollagen V + oligopeptide
-
processes the aminopropetide at the end of the variable domain, cleavage sequence is different from previously described sites for ADAMTS-2
-
-
?
propeptide of collagen alpha-1 chain + H2O
?
-
-
-
-
?
propeptide of collagen alpha-2 chain + H2O
?
-
-
-
-
?
prosaposin + H2O
?
-
-
-
?
thrombospondin-1 + H2O
?
-
-
-
?
type I aminoprocollagen + H2O
?
type I procollagen + H2O
?
type II procollagen + H2O
?
type III procollagen + H2O
?
type IV procollagen + H2O
?
type V procollagen + H2O
?
type XVIII procollagen + H2O
?
cleavage of collagen alpha-1(XVIII) chain
-
-
?
versican core protein + H2O
?
-
-
-
?
additional information
?
-
DKK3 + H2O
?
DKK3 is a highly glycosylated molecule. DKK3 is cleaved at positions 126M-/-V127, 128F-/-S129, and 130E-/-T131. Cleavage of DKK3 with potential implication in testis development
-
-
?
DKK3 + H2O
?
DKK3 is a highly glycosylated molecule. DKK3 is cleaved at positions 126M-/-V127. ADAMTS2 cleaves DKK3 upstream of the 2 conserved cysteine-rich domains known to be responsible for the inhibition of the Wnt pathway. Cleavage of DKK3 with potential implication in testis development
-
-
?
LTBP1 + H2O
?
cleavage of LTBP1 by ADAMTS3 at 315P-/-A316 and 775P-/-A776 positions
-
-
?
LTBP1 + H2O
?
LTBP1 cleavage by ADAMTS14 at the 36P-/-G37 position
-
-
?
pNcollagen
pCCollagen + oligopeptide
-
-
-
?
pNcollagen
pCCollagen + oligopeptide
-
-
-
?
pNcollagen
pCCollagen + oligopeptide
-
-
-
?
pNcollagen
pCCollagen + oligopeptide
-
-
-
?
pro-collagen + H2O
collagen + collagen N-propeptide
-
-
-
?
pro-collagen + H2O
collagen + collagen N-propeptide
E2R8G2
-
-
-
?
pro-collagen + H2O
collagen + collagen N-propeptide
-
-
-
-
?
pro-collagen + H2O
collagen + collagen N-propeptide
-
-
-
?
pro-collagen + H2O
collagen + collagen N-propeptide
-
-
-
?
pro-collagen + H2O
collagen + collagen N-propeptide
-
-
-
?
pro-collagen + H2O
collagen + collagen N-propeptide
-
-
-
?
pro-collagen + H2O
collagen + collagen N-propeptide
-
-
-
?
procollagen I + H2O
?
-
-
-
-
?
procollagen I + H2O
?
-
-
-
?
procollagen I + H2O
?
-
-
31037, 31041, 37034, 37035, 37036, 37037, 37039, 37040, 37041, 37042, 37043, 37044, 37046, 37050, 37051 -
-
?
procollagen I + H2O
?
-
-
-
?
procollagen I + H2O
?
-
-
-
?
procollagen I + H2O
?
-
-
-
?
procollagen I + H2O
pCCollagen I + oligopeptide
-
-
-
-
?
procollagen I + H2O
pCCollagen I + oligopeptide
-
-
partially processed procollagen containing only the C-propeptides
?
procollagen I + H2O
pCCollagen I + oligopeptide
-
-
partially processed procollagen containing only the C-propeptides
?
procollagen I + H2O
pCCollagen I + oligopeptide
-
-
partially processed procollagen containing only the C-propeptides
?
procollagen I + H2O
pCCollagen I + oligopeptide
-
-
partially processed procollagen containing only the C-propeptides
?
procollagen I + H2O
pCCollagen I + oligopeptide
-
-
partially processed procollagen containing only the C-propeptides
?
procollagen I + H2O
pCCollagen I + oligopeptide
-
partially processed procollagen containing only the C-propeptides
?
procollagen I + H2O
pCCollagen I + oligopeptide
-
not procollagen III
partially processed procollagen containing only the C-propeptides
?
procollagen I + H2O
pCCollagen I + oligopeptide
-
not procollagen III
partially processed procollagen containing only the C-propeptides
?
procollagen I + H2O
pCCollagen I + oligopeptide
-
not procollagen III
partially processed procollagen containing only the C-propeptides
?
procollagen I + H2O
pCCollagen I + oligopeptide
-
not procollagen III
partially processed procollagen containing only the C-propeptides
?
procollagen I + H2O
pCCollagen I + oligopeptide
-
substrate must be in native state
partially processed procollagen containing only the C-propeptides
?
procollagen I + H2O
pCCollagen I + oligopeptide
-
processing of either type I/II or type III procollagen
-
-
?
procollagen I + H2O
pCCollagen I + oligopeptide
-
removal of the N-terminal propeptide, cleavage of the substrate in native conformation but not after heat denaturation
-
-
?
procollagen I + H2O
pCCollagen I + oligopeptide
-
-
-
-
?
procollagen I + H2O
pCCollagen I + oligopeptide
-
-
partially processed procollagen containing only the C-propeptides
?
procollagen I + H2O
pCCollagen I + oligopeptide
-
-
partially processed procollagen containing only the C-propeptides
?
procollagen I + H2O
pCCollagen I + oligopeptide
-
-
partially processed procollagen containing only the C-propeptides
?
procollagen I + H2O
pCCollagen I + oligopeptide
-
-
partially processed procollagen containing only the C-propeptides
?
procollagen I + H2O
pCCollagen I + oligopeptide
-
-
partially processed procollagen containing only the C-propeptides
?
procollagen I + H2O
pCCollagen I + oligopeptide
-
-
partially processed procollagen containing only the C-propeptides
?
procollagen I + H2O
pCCollagen I + oligopeptide
-
not procollagen III
partially processed procollagen containing only the C-propeptides
?
procollagen I + H2O
pCCollagen I + oligopeptide
-
not procollagen III
partially processed procollagen containing only the C-propeptides
?
procollagen I + H2O
pCCollagen I + oligopeptide
-
not procollagen III
partially processed procollagen containing only the C-propeptides
?
procollagen I + H2O
pCCollagen I + oligopeptide
-
not procollagen III
partially processed procollagen containing only the C-propeptides
?
procollagen I + H2O
pCCollagen I + oligopeptide
-
not procollagen III
partially processed procollagen containing only the C-propeptides
?
procollagen I + H2O
pCCollagen I + oligopeptide
-
not procollagen III
partially processed procollagen containing only the C-propeptides
?
procollagen I + H2O
pCCollagen I + oligopeptide
-
cleavage of abnormal procollagen I
partially processed procollagen containing only the C-propeptides
?
procollagen I + H2O
pCCollagen I + oligopeptide
-
not procollagen IV
partially processed procollagen containing only the C-propeptides
?
procollagen I + H2O
pCCollagen I + oligopeptide
-
not procollagen IV
partially processed procollagen containing only the C-propeptides
?
procollagen I + H2O
pCCollagen I + oligopeptide
-
substrate must be in native state
partially processed procollagen containing only the C-propeptides
?
procollagen I + H2O
pCCollagen I + oligopeptide
-
substrate must be in native state
partially processed procollagen containing only the C-propeptides
?
procollagen I + H2O
pCCollagen I + oligopeptide
-
substrate must be in native state
partially processed procollagen containing only the C-propeptides
?
procollagen I + H2O
pCCollagen I + oligopeptide
-
substrate must be in native state
partially processed procollagen containing only the C-propeptides
?
procollagen I + H2O
pCCollagen I + oligopeptide
-
-
-
-
?
procollagen II + H2O
?
-
-
-
-
?
procollagen II + H2O
?
-
-
-
?
procollagen II + H2O
?
-
-
31037, 31041, 37034, 37035, 37036, 37037, 37039, 37040, 37041, 37042, 37043, 37044, 37046, 37050, 37051 -
-
?
procollagen II + H2O
?
-
-
-
?
procollagen II + H2O
?
-
-
-
?
procollagen II + H2O
?
-
-
-
?
procollagen II + H2O
pCCollagen II + oligopeptide
-
-
-
-
?
procollagen II + H2O
pCCollagen II + oligopeptide
-
-
partially processed procollagen containing only the C-propeptides
?
procollagen II + H2O
pCCollagen II + oligopeptide
-
-
partially processed procollagen containing only the C-propeptides
?
procollagen II + H2O
pCCollagen II + oligopeptide
-
-
partially processed procollagen containing only the C-propeptides
?
procollagen II + H2O
pCCollagen II + oligopeptide
-
-
partially processed procollagen containing only the C-propeptides
?
procollagen II + H2O
pCCollagen II + oligopeptide
-
-
partially processed procollagen containing only the C-propeptides
?
procollagen II + H2O
pCCollagen II + oligopeptide
-
-
partially processed procollagen containing only the C-propeptides
?
procollagen II + H2O
pCCollagen II + oligopeptide
-
-
partially processed procollagen containing only the C-propeptides
?
procollagen II + H2O
pCCollagen II + oligopeptide
-
-
partially processed procollagen containing only the C-propeptides
?
procollagen II + H2O
pCCollagen II + oligopeptide
-
partially processed procollagen containing only the C-propeptides
?
procollagen II + H2O
pCCollagen II + oligopeptide
-
substrate must be in native state
partially processed procollagen containing only the C-propeptides
?
procollagen II + H2O
pCCollagen II + oligopeptide
-
removal of the N-terminal propeptide, cleavage of the substrate in native conformation but not after heat denaturation
-
-
?
procollagen II + H2O
pCCollagen II + oligopeptide
-
-
partially processed procollagen containing only the C-propeptides
?
procollagen II + H2O
pCCollagen II + oligopeptide
-
-
partially processed procollagen containing only the C-propeptides
?
procollagen II + H2O
pCCollagen II + oligopeptide
-
-
partially processed procollagen containing only the C-propeptides
?
procollagen II + H2O
pCCollagen II + oligopeptide
-
-
partially processed procollagen containing only the C-propeptides
?
procollagen II + H2O
pCCollagen II + oligopeptide
-
-
partially processed procollagen containing only the C-propeptides
?
procollagen II + H2O
pCCollagen II + oligopeptide
-
-
partially processed procollagen containing only the C-propeptides
?
procollagen II + H2O
pCCollagen II + oligopeptide
-
-
partially processed procollagen containing only the C-propeptides
?
procollagen II + H2O
pCCollagen II + oligopeptide
-
-
partially processed procollagen containing only the C-propeptides
?
procollagen II + H2O
pCCollagen II + oligopeptide
-
-
partially processed procollagen containing only the C-propeptides
?
procollagen II + H2O
pCCollagen II + oligopeptide
-
-
partially processed procollagen containing only the C-propeptides
?
procollagen II + H2O
pCCollagen II + oligopeptide
-
substrate must be in native state
partially processed procollagen containing only the C-propeptides
?
procollagen II + H2O
pCCollagen II + oligopeptide
-
substrate must be in native state
partially processed procollagen containing only the C-propeptides
?
procollagen II + H2O
pCCollagen II + oligopeptide
-
substrate must be in native state
partially processed procollagen containing only the C-propeptides
?
procollagen II + H2O
pCCollagen II + oligopeptide
-
substrate must be in native state
partially processed procollagen containing only the C-propeptides
?
procollagen II + H2O
pCCollagen II + oligopeptide
-
cleavage of abnormal procollagen II
partially processed procollagen containing only the C-propeptides
?
procollagen II + H2O
pCCollagen II + oligopeptide
-
-
-
-
?
procollagen III + H2O
?
-
-
-
?
procollagen III + H2O
?
-
-
-
?
procollagen III + H2O
?
-
-
-
?
procollagen V + H2O
?
-
-
-
?
procollagen V + H2O
?
-
-
-
?
procollagen V + H2O
?
-
-
-
?
TGF-beta RIII + H2O
?
cleavage of TGF-beta RIII (beta-glycan) by ADAMTS3 between the endoglin-like and the zona pellucida domains at the 383P-/-384 site
-
-
?
TGF-beta RIII + H2O
?
in the presence of active ADAMTS14, the intact soluble TGF-beta RIII disappears, and a single cleavage product of 50 kDa is observed. No other cleavage product is seen
-
-
?
TGF-beta RIII + H2O
?
in the presence of active ADAMTS2, the intact soluble TGF-beta RIII disappears, and a single cleavage product of 50 kDa is observed. No other cleavage product is seen
-
-
?
type I aminoprocollagen + H2O
?
-
-
-
?
type I aminoprocollagen + H2O
?
-
-
-
?
type I aminoprocollagen + H2O
?
-
-
-
?
type I procollagen + H2O
?
-
-
-
?
type I procollagen + H2O
?
-
-
-
?
type I procollagen + H2O
?
alpha1 type I, cleavage sites in procollagen from different origins, overview
-
-
?
type I procollagen + H2O
?
alpha2 type I, cleavage sites in procollagen from different origins, overview
-
-
?
type I procollagen + H2O
?
cleavage of collagen alpha-1(I) chain and collagen alpha-2(I) chain
-
-
?
type I procollagen + H2O
?
-
-
-
-
?
type I procollagen + H2O
?
alpha1 type I, cleavage sites in procollagen from different origins, overview
-
-
?
type I procollagen + H2O
?
alpha2 type I, cleavage sites in procollagen from different origins, overview
-
-
?
type II procollagen + H2O
?
alpha1 type II, cleavage sites in procollagen from different origins, overview
-
-
?
type II procollagen + H2O
?
cleavage of collagen alpha-1(II) chain
-
-
?
type II procollagen + H2O
?
-
-
-
-
?
type II procollagen + H2O
?
alpha1 type II, cleavage sites in procollagen from different origins, overview
-
-
?
type III procollagen + H2O
?
alpha1 type III, cleavage sites in procollagen from different origins, overview
-
-
?
type III procollagen + H2O
?
cleavage of collagen alpha-1(III) chain
-
-
?
type III procollagen + H2O
?
cleavage of collagen alpha-1(III) chain, cleavage site: GFAP1218-/-1219YYGD
-
-
?
type III procollagen + H2O
?
alpha1 type III, cleavage sites in procollagen from different origins, overview
-
-
?
type IV procollagen + H2O
?
cleavage of collagen alpha-2(IV) chain
-
-
?
type IV procollagen + H2O
?
cleavage of collagen alpha-2(VI) chain and collagen alpha-2(VI) chain
-
-
?
type V procollagen + H2O
?
cleavage of collagen alpha-1(V) chain and alpha-2(V) chain
-
-
?
type V procollagen + H2O
?
cleavage of collagen alpha-2(V) chain
-
-
?
additional information
?
-
-
no cleavage of heat-denatured procollagen III
-
-
?
additional information
?
-
-
no cleavage of native procollagen III or collagen XIV, recombinant ADAMTS2 produced in 293 cells can process the N-propeptide of procollagen III in vitro
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
ADAMTS2 displays some affinity for type XIV collagen
-
-
?
additional information
?
-
E2R8G2
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
?
-
-
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
?
-
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
?
-
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
?
-
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
?
-
ADAMTS3 cleaves the aminopropeptide of type II collagen in swarm rat chondrosarcoma RCS-LTC cells stably transfected with human ADAMTS3
-
-
?
additional information
?
-
ADAMTS3 cleaves the aminopropeptide of type II collagen in swarm rat chondrosarcoma RCS-LTC cells stably transfected with human ADAMTS3
-
-
?
additional information
?
-
ADAMTS3 cleaves the aminopropeptide of type II collagen in swarm rat chondrosarcoma RCS-LTC cells stably transfected with human ADAMTS3
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
preferential substrate specificity of ADAMTS2, 3, and 14 regarding the different fibrillar procollagens is dictated first by their tissue distribution
-
-
?
additional information
?
-
preferential substrate specificity of ADAMTS2, 3, and 14 regarding the different fibrillar procollagens is dictated first by their tissue distribution
-
-
?
additional information
?
-
preferential substrate specificity of ADAMTS2, 3, and 14 regarding the different fibrillar procollagens is dictated first by their tissue distribution
-
-
?
additional information
?
-
ADAMTS2 displays some affinity for type XIV collagen
-
-
?
additional information
?
-
-
ADAMTS2 displays some affinity for type XIV collagen
-
-
?
additional information
?
-
analysis of substrate specificity and cleavage site specificity, comparison of ADAMTS2, 3, and 14 isozymes, overview
-
-
?
additional information
?
-
analysis of substrate specificity and cleavage site specificity, comparison of ADAMTS2, 3, and 14 isozymes, overview
-
-
?
additional information
?
-
analysis of substrate specificity and cleavage site specificity, comparison of ADAMTS2, 3, and 14 isozymes, overview
-
-
?
additional information
?
-
-
analysis of substrate specificity and cleavage site specificity, comparison of ADAMTS2, 3, and 14 isozymes, overview
-
-
?
additional information
?
-
analysis of substrate specificity and cleavage site specificity, comparison of ADAMTS2, 3, and 14 isozymes, overview. No activity with LTBP1
-
-
?
additional information
?
-
analysis of substrate specificity and cleavage site specificity, comparison of ADAMTS2, 3, and 14 isozymes, overview. No activity with LTBP1
-
-
?
additional information
?
-
analysis of substrate specificity and cleavage site specificity, comparison of ADAMTS2, 3, and 14 isozymes, overview. No activity with LTBP1
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additional information
?
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analysis of substrate specificity and cleavage site specificity, comparison of ADAMTS2, 3, and 14 isozymes, overview. No activity with LTBP1
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additional information
?
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sequence homology of ADAMTS14 cleavage sites in type I-III fibrillar collagens from different species, overview. 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
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?
additional information
?
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sequence homology of ADAMTS14 cleavage sites in type I-III fibrillar collagens from different species, overview. 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
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?
additional information
?
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sequence homology of ADAMTS14 cleavage sites in type I-III fibrillar collagens from different species, overview. 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
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?
additional information
?
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sequence homology of ADAMTS2 cleavage sites in type I-III fibrillar collagens from different species, overview
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?
additional information
?
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sequence homology of ADAMTS2 cleavage sites in type I-III fibrillar collagens from different species, overview
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additional information
?
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sequence homology of ADAMTS2 cleavage sites in type I-III fibrillar collagens from different species, overview
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additional information
?
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sequence homology of ADAMTS3 cleavage sites in type I-III fibrillar collagens from different species, overview
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additional information
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sequence homology of ADAMTS3 cleavage sites in type I-III fibrillar collagens from different species, overview
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additional information
?
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sequence homology of ADAMTS3 cleavage sites in type I-III fibrillar collagens from different species, overview
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additional information
?
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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
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?
additional information
?
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preferential substrate specificity of ADAMTS2, 3, and 14 regarding the different fibrillar procollagens is dictated first by their tissue distribution
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?
additional information
?
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sequence homology of ADAMTS2 cleavage sites in type I-III fibrillar collagens from different species, overview
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?
additional information
?
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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
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pro-collagen + H2O
collagen + collagen N-propeptide
procollagen I + H2O
pCCollagen I + oligopeptide
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type I aminoprocollagen + H2O
?
type I procollagen + H2O
?
type II procollagen + H2O
?
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?
additional information
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pro-collagen + H2O
collagen + collagen N-propeptide
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?
pro-collagen + H2O
collagen + collagen N-propeptide
E2R8G2
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-
-
?
pro-collagen + H2O
collagen + collagen N-propeptide
-
-
-
-
?
pro-collagen + H2O
collagen + collagen N-propeptide
-
-
-
?
pro-collagen + H2O
collagen + collagen N-propeptide
-
-
-
?
pro-collagen + H2O
collagen + collagen N-propeptide
-
-
-
?
pro-collagen + H2O
collagen + collagen N-propeptide
-
-
-
?
pro-collagen + H2O
collagen + collagen N-propeptide
-
-
-
?
procollagen I + H2O
?
-
-
-
-
?
procollagen I + H2O
?
-
-
-
?
procollagen I + H2O
?
-
-
31037, 31041, 37034, 37035, 37036, 37037, 37039, 37040, 37041, 37042, 37043, 37044, 37046, 37050, 37051 -
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procollagen I + H2O
?
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-
-
?
procollagen I + H2O
?
-
-
-
?
procollagen I + H2O
?
-
-
-
?
procollagen II + H2O
?
-
-
-
-
?
procollagen II + H2O
?
-
-
-
?
procollagen II + H2O
?
-
-
31037, 31041, 37034, 37035, 37036, 37037, 37039, 37040, 37041, 37042, 37043, 37044, 37046, 37050, 37051 -
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?
procollagen II + H2O
?
-
-
-
?
procollagen II + H2O
?
-
-
-
?
procollagen II + H2O
?
-
-
-
?
procollagen III + H2O
?
-
-
-
?
procollagen III + H2O
?
-
-
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?
procollagen III + H2O
?
-
-
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?
procollagen V + H2O
?
-
-
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?
procollagen V + H2O
?
-
-
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?
procollagen V + H2O
?
-
-
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?
type I aminoprocollagen + H2O
?
-
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-
?
type I aminoprocollagen + H2O
?
-
-
-
?
type I procollagen + H2O
?
-
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?
type I procollagen + H2O
?
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-
?
type I procollagen + H2O
?
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-
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?
additional information
?
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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
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?
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
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?
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
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?
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
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?
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
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?
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
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?
additional information
?
-
E2R8G2
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)
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?
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)
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?
additional information
?
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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
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?
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
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?
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
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?
additional information
?
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ADAMTS3 cleaves the aminopropeptide of type II collagen in swarm rat chondrosarcoma RCS-LTC cells stably transfected with human ADAMTS3
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?
additional information
?
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ADAMTS3 cleaves the aminopropeptide of type II collagen in swarm rat chondrosarcoma RCS-LTC cells stably transfected with human ADAMTS3
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?
additional information
?
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ADAMTS3 cleaves the aminopropeptide of type II collagen in swarm rat chondrosarcoma RCS-LTC cells stably transfected with human ADAMTS3
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?
additional information
?
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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
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?
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
-
-
?
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
-
-
?
additional information
?
-
preferential substrate specificity of ADAMTS2, 3, and 14 regarding the different fibrillar procollagens is dictated first by their tissue distribution
-
-
?
additional information
?
-
preferential substrate specificity of ADAMTS2, 3, and 14 regarding the different fibrillar procollagens is dictated first by their tissue distribution
-
-
?
additional information
?
-
preferential substrate specificity of ADAMTS2, 3, and 14 regarding the different fibrillar procollagens is dictated first by their tissue distribution
-
-
?
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
-
-
?
additional information
?
-
preferential substrate specificity of ADAMTS2, 3, and 14 regarding the different fibrillar procollagens is dictated first by their tissue distribution
-
-
?
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
-
-
?
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Alzheimer Disease
A disintegrin and metalloproteinase with thrombospondin motifs 2 cleaves and inactivates Reelin in the postnatal cerebral cortex and hippocampus, but not in the cerebellum.
Angina, Stable
Expression of ADAMTS-2, -3, -13, and -14 in culprit coronary lesions in patients with acute myocardial infarction or stable angina.
Brain Diseases
A disintegrin and metalloproteinase with thrombospondin motifs 2 cleaves and inactivates Reelin in the postnatal cerebral cortex and hippocampus, but not in the cerebellum.
Carcinogenesis
ADAMTS14 Gene Polymorphism and Environmental Risk in the Development of Oral Cancer.
Carcinogenesis
Decreased Cytoplasmic Expression of ADAMTS14 Is Correlated with Reduced Survival Rates in Oral Squamous Cell Carcinoma Patients.
Carcinogenesis
Effects of ADAMTS14 genetic polymorphism and cigarette smoking on the clinicopathologic development of hepatocellular carcinoma.
Carcinoma
Decreased Cytoplasmic Expression of ADAMTS14 Is Correlated with Reduced Survival Rates in Oral Squamous Cell Carcinoma Patients.
Carcinoma
Overexpression of ADAMTS-2 in tumor cells and stroma is predictive of poor clinical prognosis in gastric cancer.
Carcinoma, Hepatocellular
Effects of ADAMTS14 genetic polymorphism and cigarette smoking on the clinicopathologic development of hepatocellular carcinoma.
Carcinoma, Hepatocellular
The competing endogenous circular RNA ADAMTS14 suppressed hepatocellular carcinoma progression through regulating microRNA-572/regulator of calcineurin 1.
Cardiomegaly
Critical Role of ADAMTS2 (A Disintegrin and Metalloproteinase With Thrombospondin Motifs 2) in Cardiac Hypertrophy Induced by Pressure Overload.
Cardiomegaly
Systems Genetics Approach Identifies Gene Pathways and Adamts2 as Drivers of Isoproterenol-Induced Cardiac Hypertrophy and Cardiomyopathy in Mice.
Cardiomyopathies
Systems Genetics Approach Identifies Gene Pathways and Adamts2 as Drivers of Isoproterenol-Induced Cardiac Hypertrophy and Cardiomyopathy in Mice.
Colonic Neoplasms
[Identification of protein markers for serum diagnosis of cancer based on microRNA expression profiling].
Congenital Abnormalities
ADAMTS proteins in human disorders.
Corneal Dystrophies, Hereditary
Cross-ancestry genome-wide association analysis of corneal thickness strengthens link between complex and Mendelian eye diseases.
Craniofacial Fibrous Dysplasia
Gene expression profiling of craniofacial fibrous dysplasia reveals ADAMTS2 overexpression as a potential marker.
Dermatitis, Atopic
Spontaneous atopic dermatitis due to immune dysregulation in mice lacking Adamts2 and 14.
Ehlers-Danlos Syndrome
A homozygous ADAMTS2 nonsense mutation in a Doberman Pinscher dog with Ehlers Danlos syndrome and extreme skin fragility.
Ehlers-Danlos Syndrome
Abnormal dentin structure in two novel gene mutations [COL1A1, Arg134Cys] and [ADAMTS2, Trp795-to-ter] causing rare type I collagen disorders.
Ehlers-Danlos Syndrome
ADAMTS: a novel family of extracellular matrix proteases.
Ehlers-Danlos Syndrome
Cloning and characterization of ADAMTS-14, a novel ADAMTS displaying high homology with ADAMTS-2 and ADAMTS-3.
Ehlers-Danlos Syndrome
Connective tissue disorders in domestic animals.
Ehlers-Danlos Syndrome
Expanding the clinical and mutational spectrum of the Ehlers-Danlos syndrome, dermatosparaxis type.
Ehlers-Danlos Syndrome
Human Ehlers-Danlos syndrome type VII C and bovine dermatosparaxis are caused by mutations in the procollagen I N-proteinase gene.
Ehlers-Danlos Syndrome
In vivo and in vitro noncovalent association of excised alpha 1 (I) amino-terminal propeptides with mutant pN alpha 2(I) collagen chains in native mutant collagen in a case of Ehlers-Danlos syndrome, type VII.
Ehlers-Danlos Syndrome
Novel types of mutation responsible for the dermatosparactic type of Ehlers-Danlos syndrome (Type VIIC) and common polymorphisms in the ADAMTS2 gene.
Ehlers-Danlos Syndrome
Polymorphic variation within the ADAMTS2, ADAMTS14, ADAMTS5, ADAM12 and TIMP2 genes and the risk of Achilles tendon pathology: A genetic association study.
Ehlers-Danlos Syndrome
Regulation of procollagen amino-propeptide processing during mouse embryogenesis by specialization of homologous ADAMTS proteases: insights on collagen biosynthesis and dermatosparaxis.
Ehlers-Danlos Syndrome
The natural history, including orofacial features of three patients with Ehlers-Danlos syndrome, dermatosparaxis type (EDS type VIIC).
Ehlers-Danlos Syndrome
Transforming growth factor-beta induces secretion of activated ADAMTS-2. A procollagen III N-proteinase.
Exostoses
Evidence of genetic underexpression in chorionic villi samples of euploid fetuses with increased nuchal translucency at 10-11 weeks' gestation.
Genetic Diseases, Inborn
The ADAMTS(L) family and human genetic disorders.
Heart Defects, Congenital
A case report of familial 4q13.3 microdeletion in three individuals with syndromic intellectual disability.
Infertility, Male
Transgenic mice with inactive alleles for procollagen N-proteinase (ADAMTS-2) develop fragile skin and male sterility.
Intellectual Disability
A case report of familial 4q13.3 microdeletion in three individuals with syndromic intellectual disability.
Leukemia
ADAMTS2 gene dysregulation in T/myeloid mixed phenotype acute leukemia.
Liver Cirrhosis
ADAM metallopeptidase with thrombospondin type 1 motif 2 inactivation reduces the extent and stability of carbon tetrachloride-induced hepatic fibrosis in mice.
Lymphatic Metastasis
Decreased Cytoplasmic Expression of ADAMTS14 Is Correlated with Reduced Survival Rates in Oral Squamous Cell Carcinoma Patients.
Lymphedema
Efficient activation of the lymphangiogenic growth factor VEGF-C requires the C-terminal domain of VEGF-C and the N-terminal domain of CCBE1.
Mesothelioma
Genetic variants associated with increased risk of malignant pleural mesothelioma: a genome-wide association study.
Mouth Neoplasms
ADAMTS14 Gene Polymorphism and Environmental Risk in the Development of Oral Cancer.
Multiple Sclerosis
Genetic association between polymorphisms in the ADAMTS14 gene and multiple sclerosis.
Myocardial Infarction
Expression of ADAMTS-2, -3, -13, and -14 in culprit coronary lesions in patients with acute myocardial infarction or stable angina.
Myopia
Cross-ancestry genome-wide association analysis of corneal thickness strengthens link between complex and Mendelian eye diseases.
Myopia
Novel Myopia Genes and Pathways Identified From Syndromic Forms of Myopia.
Neoplasm Metastasis
Combination of laser microdissection, 2D-DIGE and MALDI-TOF MS to identify protein biomarkers to predict colorectal cancer spread.
Neoplasm Metastasis
Decreased Cytoplasmic Expression of ADAMTS14 Is Correlated with Reduced Survival Rates in Oral Squamous Cell Carcinoma Patients.
Neoplasm Metastasis
Effect of insulin on the mRNA expression of procollagen N-proteinases in chondrosarcoma OUMS-27 cells.
Neoplasms
ADAMTS-2 functions as anti-angiogenic and anti-tumoral molecule independently of its catalytic activity.
Neoplasms
ADAMTS14 Gene Polymorphism and Environmental Risk in the Development of Oral Cancer.
Neoplasms
Combination of laser microdissection, 2D-DIGE and MALDI-TOF MS to identify protein biomarkers to predict colorectal cancer spread.
Neoplasms
Decreased Cytoplasmic Expression of ADAMTS14 Is Correlated with Reduced Survival Rates in Oral Squamous Cell Carcinoma Patients.
Neoplasms
Effect of insulin on the mRNA expression of procollagen N-proteinases in chondrosarcoma OUMS-27 cells.
Neoplasms
Increased mRNA expression of ADAMs in renal cell carcinoma and their association with clinical outcome.
Neoplasms
Increasing the number of thyroid lesions classes in microarray analysis improves the relevance of diagnostic markers.
Neoplasms
Overall survival in EGFR mutated non-small-cell lung cancer patients treated with afatinib after EGFR TKI and resistant mechanisms upon disease progression.
Neoplasms
Overexpression of ADAMTS-2 in tumor cells and stroma is predictive of poor clinical prognosis in gastric cancer.
Neoplasms
The membrane proteases adams and hepsin are differentially expressed in renal cell carcinoma. Are they potential tumor markers?
Obstetric Labor, Premature
Comparative analysis of gene expression in maternal peripheral blood and monocytes during spontaneous preterm labor.
Obstetric Labor, Premature
The preterm labor associated ADAMTS2 gene is induced by glucocorticoids.
Osteoarthritis
Association of a nsSNP in ADAMTS14 to some osteoarthritis phenotypes.
Osteoarthritis
Genetic association analysis of the IGFBP7, ADAMTS3, and IL8 genes as the potential osteoarthritis susceptibility that maps to chromosome 4q.
Osteoarthritis
[Association between ADAMTS14 gene polymorphism and the temporomandibular joint osteoarthritis in Chinese Han females].
Osteoarthritis, Knee
ADAMTS14 gene polymorphism associated with knee osteoarthritis in Thai women.
Osteoarthritis, Knee
Lack of association between MMP13 (rs3819089), ADAM12 (rs3740199-rs1871054) and ADAMTS14 (rs4747096) genotypes and advanced-stage knee osteoarthritis.
Osteogenesis Imperfecta
A heterozygous defect for structurally altered pro-alpha 2 chain of type I procollagen in a mild variant of osteogenesis imperfecta. The altered structure decreases the thermal stability of procollagen and makes it resistant to procollagen N-proteinase.
Osteogenesis Imperfecta
Substitution of serine for glycine 883 in the triple helix of the pro alpha 1 (I) chain of type I procollagen produces osteogenesis imperfecta type IV and introduces a structural change in the triple helix that does not alter cleavage of the molecule by procollagen N-proteinase.
Osteosarcoma
IL-6 upregulates a disintegrin and metalloproteinase with thrombospondin motifs 2 (ADAMTS-2) in human osteosarcoma cells mediated by JNK pathway.
Osteosarcoma
SP1-mediated downregulation of ADAMTS3 gene expression in osteosarcoma models.
Osteosarcoma
Transforming growth factor-beta induces secretion of activated ADAMTS-2. A procollagen III N-proteinase.
Purpura, Thrombotic Thrombocytopenic
The ADAMTS(L) family and human genetic disorders.
Sleep Apnea Syndromes
Association between the ADAMTS proteinases and obstructive sleep apnea.
Squamous Cell Carcinoma of Head and Neck
Decreased Cytoplasmic Expression of ADAMTS14 Is Correlated with Reduced Survival Rates in Oral Squamous Cell Carcinoma Patients.
Stomach Neoplasms
Overexpression of ADAMTS-2 in tumor cells and stroma is predictive of poor clinical prognosis in gastric cancer.
Stroke
ADAMTS genes and the risk of cerebral aneurysm.
Stroke
ADAMTS12, a new candidate gene for pediatric stroke.
Urinary Incontinence
The role of ADAMTS-2, collagen type-1, TIMP-3 and papilin levels of uterosacral and cardinal ligaments in the etiopathogenesis of pelvic organ prolapse among women without stress urinary incontinence.
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metabolism
-
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
-
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
-
mice with inactivation of both alleles of procollagen N-proteinase (ADAMTS-2) exhibit no difference between knockout mice and their wild type littermates
malfunction
-
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
-
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
-
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
-
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
-
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
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