Reactome: A Curated Pathway Database

Gelatin degradation by MMP1, 2, 3, 7, 8, 9, 12, 13

Stable Identifier
Homo sapiens
Locations in the PathwayBrowser

Gelatin is formed when collagen becomes partly or completely uncoiled when compared with the regular triple helix structure of fibrillar collagen. In vivo, once collagens are initially cleaved into clasical 3/4 and 1/4 fragments (by collagenases) they rapidly denature at body temperature and are degraded by gelatinases and other nonspecific tissue proteinases (Chung et al. 2004) to a semi-solid colloid gel. MMP2 and MMP9 are the major gelatinases (Collier et al. 1988, Wilhelm et al. 1989) often referred to respectively as Gelatinase A and Gelatinase B (Murphy & Crabbe 1995). However many other MMPs have gelatinase activity, including MMP1 (Murphy et al. 1982, Isaksen & Fagerhol 2001, Chung et al. 2004), MMP3 (Chin et al. 1985, Isaksen & Fagerhol 2001), MMP7 (Isaksen & Fagerhol 2001), MMP8 (Isaksen & Fagerhol 2001) MMP10 (Sanches-Lopez et al. 1993), MMP12 (Chandler et al. 1996), MMP13 (Knäuper et al. 1993, Isaksen & Fagerhol 2001), MMP16 (Shofuda et al. 1997), MMP17 (Wang et al. 1999), MMP18 (Spinucci et al. 1988), MMP19 (Stracke et al. 2000) and MMP22 (Yang & Kurkinen 1998).

Literature References
PubMed ID Title Journal Year
10809722 Biochemical characterization of the catalytic domain of human matrix metalloproteinase 19. Evidence for a role as a potent basement membrane degrading enzyme J. Biol. Chem. 2000
11577169 Calprotectin inhibits matrix metalloproteinases by sequestration of zinc MP, Mol. Pathol. 2001
10551873 Catalytic activities and substrate specificity of the human membrane type 4 matrix metalloproteinase catalytic domain J. Biol. Chem. 1999
9651395 Cloning and characterization of a novel matrix metalloproteinase (MMP), CMMP, from chicken embryo fibroblasts. CMMP, Xenopus XMMP, and human MMP19 have a conserved unique cysteine in the catalytic domain J. Biol. Chem. 1998
9092507 Expression of three membrane-type matrix metalloproteinases (MT-MMPs) in rat vascular smooth muscle cells and characterization of MT3-MMPs with and without transmembrane domain J. Biol. Chem. 1997
2834383 H-ras oncogene-transformed human bronchial epithelial cells (TBE-1) secrete a single metalloprotease capable of degrading basement membrane collagen J. Biol. Chem. 1988
8920930 Macrophage metalloelastase degrades matrix and myelin proteins and processes a tumour necrosis factor-alpha fusion protein Biochem Biophys Res Commun 1996
2845110 Purification of a gelatin-degrading type IV collagenase secreted by ras oncogene-transformed fibroblasts J. Natl. Cancer Inst. 1988
8463259 Role of zinc-binding- and hemopexin domain-encoded sequences in the substrate specificity of collagenase and stromelysin-2 as revealed by chimeric proteins J. Biol. Chem. 1993
2551898 SV40-transformed human lung fibroblasts secrete a 92-kDa type IV collagenase which is identical to that secreted by normal human macrophages J Biol Chem 1989
Participant Of
This entity is regulated by:
Title Physical Entity Activity
metalloendopeptidase activity of MMP1-3, 7-9, 12, 13 [extracellular region] MMP1-3, 7-9, 12, 13 [extracellular region] metalloendopeptidase activity (0004222)
Orthologous Events