Collagen type VI degradation by MMP2,9,11

Stable Identifier
Reaction [transition]
Homo sapiens
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Type VI collagen aggregates into distinctive microfibrils known as beaded filaments that form an independent microfibrillar network in virtually all connective tissues except for bone (von der Mark et al. 1984). It plays a role in the maintenance of tissue integrity since it participates in both cell-matrix and matrix-matrix interactions, interacting with many other ECM proteins including fibronectin (Chang et al. 1997), type IV collagen (Kuo et al. 1997), type II collagen, decorin and biglycan (Bidanset et al. 1992). Collagen type VI has been described as a connecting protein (Gelse et al. 2003).

Collagen type VI is resistant to digestion by many MMPs but is cleaved by MMP2 (Myint et al. 1996, Veidal et al. 2011), MMP9 (Veidal et al. 2011) and MMP11 (Motrescu et al. 2008).
Literature References
PubMed ID Title Journal Year
18622425 Matrix metalloproteinase-11/stromelysin-3 exhibits collagenolytic function against collagen VI under normal and malignant conditions

Stoll, I, Etique, N, Motrescu, ER, Tomasetto, C, Blaise, S, Chenard, MP, Rio, MC, Messaddeq, N

Oncogene 2008
21935455 MMP mediated degradation of type VI collagen is highly associated with liver fibrosis--identification and validation of a novel biochemical marker assay

Veidal, SS, Leeming, DJ, Nawrocki, A, Zheng, Q, Karsdal, MA, Larsen, MR, Vassiliadis, E, Vainer, B, Luo, Y, Nguyen, QH, Hägglund, P

PLoS One 2011
Catalyst Activity

metalloendopeptidase activity of MMP2,9,11 [extracellular region]

Orthologous Events
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