Collagen type I degradation by MMP1,2,8,13, 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) known in the literature as collagenases I, II and III respectively are able to digest the intrahelical bonds of collagen type I. MMP2, also known as Gelatinase-A, was found to cleave collagen type I fibrils (Aimes & Quigley 1995). Though this was disputed (Seltzre & Eisen 1999) there is a structural explanation for the apparent discrepancies in experimental data (Patterson et al. 2001). In addition trypsin-2 is able to degrade native soluble type I collagen (Moilanen et al. 2003). Degradation is represented here at a theoretical end point where every alpha strand has been cleaved.

Literature References
PubMed ID Title Journal Year
15257288 Collagenase unwinds triple-helical collagen prior to peptide bond hydrolysis

Visse, R, Fields, GB, Lauer-Fields, JL, Nagase, H, Yoshida, N, Dinakarpandian, D, Chung, L

EMBO J 2004
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
7890717 Matrix metalloproteinase-2 is an interstitial collagenase. Inhibitor-free enzyme catalyzes the cleavage of collagen fibrils and soluble native type I collagen generating the specific 3/4- and 1/4-length fragments

Quigley, JP, Aimes, RT

J Biol Chem 1995
8576151 Biochemical characterization of human collagenase-3

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

J Biol Chem 1996
Catalyst Activity

metalloendopeptidase activity of MMP1,2,8,13, PRSS2 [extracellular region]

Orthologous Events
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