DCN (decorin) degradation by MMP2, MMP3, MMP7

Stable Identifier
Reaction [transition]
Homo sapiens
DCN is cleaved by MMP2, 3 and 7, Decorin is cleaved by MMP2, 3 & 7
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DCN consists of a core protein of ?40 kDa attached to a single chondroitin or dermatan sulfate glycosaminoglycan (GAG) chain. It interacts with collagen types I, II (Vogel et al. 1984), III (Witos et al. 2011), VI (Bidanset et al. 1992) and XIV (Ehnis et al. 1997). DCN acts as a sink for all three isoforms of TGF-Beta, binding them while already bound to collagen (Markmann et al. 2000). Degradation of DCN by matrix metalloproteinases MMP2, 3 or 7 results in the release of TGF-beta (Imai et al. 1997). In addition, DCN binds to EGFR (Iozzo et al. 1999) causing prolonged down-regulation of EGFR-mediated mobilization of intracellular calcium (Csordás et al. 2000).

Literature References
PubMed ID Title Journal Year
9148753 Degradation of decorin by matrix metalloproteinases: identification of the cleavage sites, kinetic analyses and transforming growth factor-beta1 release

Imai, K, Hiramatsu, A, Fukushima, D, Pierschbacher, MD, Okada, Y

Biochem. J. 1997
Catalyst Activity

metalloendopeptidase activity of MMP2, MMP3, MMP7 [extracellular region]

Orthologous Events
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