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Details on Person Gelatin is formed when collagen becomes partly or completely...

Class:IdSummation:1454743
_displayNameGelatin is formed when collagen becomes partly or completely...
_timestamp2012-10-29 15:21:16
created[InstanceEdit:1454796] Jupe, S, 2011-07-18
literatureReference[LiteratureReference:1454859] Collagenase unwinds triple-helical collagen prior to peptide bond hydrolysis
[LiteratureReference:2537480] H-ras oncogene-transformed human bronchial epithelial cells (TBE-1) secrete a single metalloprotease capable of degrading basement membrane collagen
[LiteratureReference:1602465] SV40-transformed human lung fibroblasts secrete a 92-kDa type IV collagenase which is identical to that secreted by normal human macrophages
[LiteratureReference:2537535] Gelatinases A and B
[LiteratureReference:1564207] Partial purification of collagenase and gelatinase from human polymorphonuclear leucocytes. Analysis of their actions on soluble and insoluble collagens
[LiteratureReference:2537496] Calprotectin inhibits matrix metalloproteinases by sequestration of zinc
[LiteratureReference:1458419] Stromelysin, a connective tissue-degrading metalloendopeptidase secreted by stimulated rabbit synovial fibroblasts in parallel with collagenase. Biosynthesis, isolation, characterization, and substrates
[LiteratureReference:2537473] Role of zinc-binding- and hemopexin domain-encoded sequences in the substrate specificity of collagenase and stromelysin-2 as revealed by chimeric proteins
[LiteratureReference:1564149] Macrophage metalloelastase degrades matrix and myelin proteins and processes a tumour necrosis factor-alpha fusion protein
[LiteratureReference:1458404] Biochemical characterization of human collagenase-3
[LiteratureReference:2537508] 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
[LiteratureReference:2537525] Catalytic activities and substrate specificity of the human membrane type 4 matrix metalloproteinase catalytic domain
[LiteratureReference:2537513] Purification of a gelatin-degrading type IV collagenase secreted by ras oncogene-transformed fibroblasts
[LiteratureReference:2537521] Biochemical characterization of the catalytic domain of human matrix metalloproteinase 19. Evidence for a role as a potent basement membrane degrading enzyme
[LiteratureReference:2537509] 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
modified[InstanceEdit:1454885] Jupe, S, 2011-07-18
[InstanceEdit:1458406] Jupe, S, 2011-07-21
[InstanceEdit:2537528] Jupe, S, 2012-10-29
textGelatin 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).
(summation)[BlackBoxEvent:1454757] Gelatin degradation by MMP1, 2, 3, 7, 8, 9, 12, 13 [Homo sapiens]
[BlackBoxEvent:2537499] Gelatin degradation by MMP19 [Homo sapiens]
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