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

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

Stable Identifier

R-HSA-1454757

Type

Reaction [omitted]

Species

Homo sapiens

Compartment

extracellular region

ReviewStatus

5/5

Locations in the PathwayBrowser

Expand all

General

SBML | | PDF

SVG | | PPTX | SBGN

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

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