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

Stable Identifier
Reaction [omitted]
Homo sapiens
Locations in the PathwayBrowser
SVG |   | PPTX  | SBGN
Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout
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
8920930 Macrophage metalloelastase degrades matrix and myelin proteins and processes a tumour necrosis factor-alpha fusion protein

Wells, G, Lury, J, Chandler, S, Cossins, J

Biochem Biophys Res Commun 1996
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

Miyazaki, K, Shofuda, K, Miki, K, Nishihashi, A, Yasumitsu, H

J. Biol. Chem. 1997
10551873 Catalytic activities and substrate specificity of the human membrane type 4 matrix metalloproteinase catalytic domain

Ye, QZ, Dyer, RD, Johnson, AR, Wang, Y

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

Yang, M, Kurkinen, M

J. Biol. Chem. 1998
8463259 Role of zinc-binding- and hemopexin domain-encoded sequences in the substrate specificity of collagenase and stromelysin-2 as revealed by chimeric proteins

Behrendtsen, O, Sanchez-Lopez, R, Werb, Z, Alexander, CM, Breathnach, R

J. Biol. Chem. 1993
10809722 Biochemical characterization of the catalytic domain of human matrix metalloproteinase 19. Evidence for a role as a potent basement membrane degrading enzyme

Murphy, G, Knäuper, V, López-Otin, C, Stracke, JO, Hutton, M, Stewart, M, Pendás, AM, Smith, B

J. Biol. Chem. 2000
2551898 SV40-transformed human lung fibroblasts secrete a 92-kDa type IV collagenase which is identical to that secreted by normal human macrophages

Eisen, AZ, Marmer, BL, Goldberg, GI, Grant, GA, Collier, IE, Wilhelm, SM

J Biol Chem 1989
2834383 H-ras oncogene-transformed human bronchial epithelial cells (TBE-1) secrete a single metalloprotease capable of degrading basement membrane collagen

Kronberger, A, Bauer, EA, Eisen, AZ, Collier, IE, He, CS, Seltzer, JL, Grant, GA, Marmer, BL, Goldberg, GI, Wilhelm, SM

J. Biol. Chem. 1988
11577169 Calprotectin inhibits matrix metalloproteinases by sequestration of zinc

Fagerhol, MK, Isaksen, B

MP, Mol. Pathol. 2001
2845110 Purification of a gelatin-degrading type IV collagenase secreted by ras oncogene-transformed fibroblasts

Wieman, JM, Ramamurthy, N, Lysik, RM, Imhof, B, Spinucci, C, Nagase, H, Liotta, LA, Zucker, S

J. Natl. Cancer Inst. 1988
Catalyst Activity

metalloendopeptidase activity of MMP1-3, 7-9, 12, 13 [extracellular region]

Orthologous Events
Cite Us!