Gelatin degradation by MMP19

Stable Identifier
R-NUL-2537524
Type
Reaction [omitted]
Species
Homo sapiens
Compartment
General
SVG |   | PPTX  | SBGN
Gelatin degradation by MMP19

Gelatin forms when collagen becomes partly or completely uncoiled, as opposed to 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

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

J. Biol. Chem. 2000
Participants
Catalyst Activity
Catalyst Activity
Title
metalloendopeptidase activity of MMP19 [extracellular region]
Physical Entity
Activity
Orthologous Events
Authored
Reviewed
Created
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