Collagen type II degradation by MMP1,3,8,13,PRSS2

Stable Identifier
Reaction [transition]
Homo sapiens
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MMP1 (Welgus et al. 1981), MMP8 (Hasty et al. 1987), and MMP13 (Knauper et al. 1996, Mitchell et al. 1996, Billinghurst et al. 1997) known in the literature as collagenases I, II and III respectively are able to digest the intrahelical bonds of collagen type II, cleaving between amino acids Gly975 and Leu976 of the Uniprot canonical sequence. Human trypsin-2 is also capable of cleaving the triple helix of human cartilage collagen type II (Stenman et al. 2005).
Literature References
PubMed ID Title Journal Year
3038863 The collagen substrate specificity of human neutrophil collagenase

Hibbs, MS, Hasty, KA, Jeffrey, JJ, Welgus, HG

J Biol Chem 1987
6270089 The collagen substrate specificity of human skin fibroblast collagenase

Eisen, AZ, Jeffrey, JJ, Welgus, HG

J Biol Chem 1981
2005102 Sites of stromelysin cleavage in collagen types II, IX, X, and XI of cartilage

Lark, MW, Chun, LE, Eyre, DR, Wu, JJ

J Biol Chem 1991
8576151 Biochemical characterization of human collagenase-3

Smith, B, López-Otin, C, Knight, G, Knäuper, V, Murphy, G

J Biol Chem 1996
Catalyst Activity

serine-type endopeptidase activity of MMP1,3,8,13, PRSS2 [extracellular region]

Orthologous Events
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