2010
DOI: 10.1111/j.1478-3231.2010.02309.x
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Matrix metalloproteinase-9-mediated type III collagen degradation as a novel serological biochemical marker for liver fibrogenesis

Abstract: The data suggest that MMP-9-mediated CO3 turnover is a central event in the pathogenesis of fibrosis, and that the neo-epitope generated may be a novel biochemical marker.

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Cited by 60 publications
(57 citation statements)
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“…When this C3M fragment was assessed in two separate animal models of liver fibrosis, the BDL and CCl4 animal models, a > 200% fold upregulation was observed, as well as a highly significant correlation to portal pressure. 60,356,357 These data strongly suggest that liver fibrosis is not merely an accumulation of ECM proteins, but a dynamic condition with accelerated ECM turnover, in which both tissue formation and tissue degradation are highly upregulated. In the case of liver fibrosis, ECM tissue formation outstrips tissue degradation, leading to a net accumulation of scar tissue over time.…”
Section: 311mentioning
confidence: 91%
“…When this C3M fragment was assessed in two separate animal models of liver fibrosis, the BDL and CCl4 animal models, a > 200% fold upregulation was observed, as well as a highly significant correlation to portal pressure. 60,356,357 These data strongly suggest that liver fibrosis is not merely an accumulation of ECM proteins, but a dynamic condition with accelerated ECM turnover, in which both tissue formation and tissue degradation are highly upregulated. In the case of liver fibrosis, ECM tissue formation outstrips tissue degradation, leading to a net accumulation of scar tissue over time.…”
Section: 311mentioning
confidence: 91%
“…For this purpose, matrix-metalloproteinases (MMPs) -1 (collagenase), -2 and -9 (gelatinases-A and -B), were investigated since these are typically up-regulated in aged skin where they degrade dermal collagens, elastic fibers and fibrillin-rich microfibrils (Ashworth et al, 1999;Kim et al, 2010; MANUSCRIPT 4 et al, 2010;Veidal et al, 2010). The major structural component of fibrillin-rich microfibrils, fibrillin-1, was also analysed, since it is a sensitive indicator of intrinsic and extrinsic skin aging (Naylor et al, 2011;Watson et al, 1999;2008;2014), along with mature collagen type I and III, since their expression decreases progressively during skin aging (Attia-Vigneau et al, 2014;Baroni Edo et al, 2012;Berneburg, 2008;Gilchrest, 2013;Langton et al, 2012).…”
Section: Introductionmentioning
confidence: 99%
“…29,30 Degradation of type I collagen was measured as MMP-2-, MMP-9-, and MMP-13-mediated fragments of type I collagen (C1M) and degradation of type III collagen as MMP-9-generated fragments of type III collagen (C3M). 31,32 Synthesis of type V collagen was measured as the C-terminal pro-peptide of type V procollagen (P5CP) and degradation of type V collagen as MMP-2-, and MMP-9-mediated fragments of type V collagen (C5M). 33,34 Synthesis of type IV collagen was measured as the N-terminal peptide of type IV pro-collagen (P4NP) and degradation as a pepsin/MMP-9-generated fragment of type IV collagen (C4M).…”
Section: Methodsmentioning
confidence: 99%