Decreased collagen-degrading activity could be a marker of prolonged mesangial matrix expansion

Tomita, Masayuki; Koike, Hiroko; Han, Gi Dong; Shimizu, Fujio; Kawachi, Hiroshi

doi:10.1007/s10157-003-0258-7

Cited by 20 publications

(21 citation statements)

References 29 publications

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“…54 Impaired expression of MMP-9 has been suggested to contribute to mesangial expansion in rat models of GN, 55 and CGN is augmented in MMP-9-deficient mice, due to impaired fibrinolysis. 56 Our results showed significantly augmented renal MMP-9 activity in PAR-2-deficient mice with CGN but no change in MMP-2 activity.…”

Section: Discussionmentioning

confidence: 99%

Protease-Activated Receptor-2 Augments Experimental Crescentic Glomerulonephritis

Moussa

Apostolopoulos

Davenport

et al. 2007

The American Journal of Pathology

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Section: Discussionmentioning

confidence: 99%

Protease-Activated Receptor-2 Augments Experimental Crescentic Glomerulonephritis

Moussa

Apostolopoulos

Davenport

et al. 2007

The American Journal of Pathology

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“…Experimentally, MMP-9 is upregulated in models of FSGS, lupus nephritis, and Thy1.1 nephritis, a model for membranoproliferative glomerulonephritis (MPGN) (69,81,128,132). However, impaired resolution of disease appears to be associated with a paradoxical decrease in MMP-9 late in the course of Thy1.1 nephritis (128).…”

Section: Mmps In Renal Pathologymentioning

confidence: 99%

Matrix metalloproteinases in kidney homeostasis and diseases

Tan

Liu

2012

American Journal of Physiology-Renal Physiology

221

219

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“…The expression of MMP-9 appears to be mainly confined to the glomerulus (39,46,55,71), although there are reports of expression in the proximal and distal tubules of the monkey (60) and in the rabbit collecting duct (62). MMP-13 and -14 are localized in the glomerulus in rats (84); however, these studies investigated mRNA expression in isolated glomeruli and did not investigate expression along the entire nephron. MMP-14 is also expressed in distal tubules in a mouse model of polycystic kidney disease (PKD) (59).…”

Section: Renal Mmpsmentioning

confidence: 99%

“…In mouse kidney, TIMP-1 is expressed at low levels, TIMPs-2 and -3 at high levels, and TIMP-4 is not expressed (28). TIMP-1 is expressed in the glomerulus in rats (84) and humans (79,80). In addition, TIMP-3 is detected in the rat kidney (89), and human glomeruli express TIMP-1 and -2 mRNA (15).…”

Section: Renal Mmpsmentioning

confidence: 99%

“…2). MMP-2 is expressed in the collecting duct in the rabbit (62), the glomerulus and proximal tubules of rats (39,71,84), and in the proximal and distal tubules in the monkey (60). MMP-3 is not detected in the proximal tubules of rats (71) but is expressed in the proximal and distal tubules of the monkey (60), as well as in the glomerulus and some tubular epithelial cells in humans (79).…”

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Role of matrix metalloproteinases in renal pathophysiologies

Catania¹,

Chen²,

Parrish³

2007

American Journal of Physiology-Renal Physiology

348

314

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Matrix metalloproteinases (MMPs) are a large family of proteinases that remodel extracellular matrix (ECM) components and cleave a number of cell surface proteins. MMP activity is regulated via a number of mechanisms, including inhibition by tissue inhibitors of metalloproteinases (TIMPs). Originally thought to cleave only ECM proteins, MMP substrates are now known to include signaling molecules (growth factor receptors) and cell adhesion molecules. Recent data suggest a role for MMPs in a number of renal pathophysiologies, both acute and chronic. This review will focus on the expression and localization of MMPs and TIMPs in the kidney, as well as summarizing the current information linking these proteins to acute kidney injury, glomerulosclerosis/tubulointerstitial fibrosis, chronic allograft nephropathy, diabetic nephropathy, polycystic kidney disease, and renal cell carcinoma.acute kidney injury; chronic allograft nephropathy; diabetic nephropathy; glomerulosclerosis; MMP; polycystic kidney disease; tissue inhibitor of metalloproteinase; tubulointerstitial fibrosis; renal cell carcinoma MATRIX METALLOPROTEINASES (MMPs) are zinc-containing endopeptidases that are involved in remodeling the extracellular matrix (ECM) and are crucial for tissue development and homeostasis. All MMPs are multidomain enzymes, generally consisting of a prodomain, a catalytic domain, a hinge region, and a hemopexin-like domain. Most MMPs are secreted as proMMPs; activation usually requires cleavage of the prodomain by plasmin or other MMPs (88). The propeptide sequence contains a conserved cysteine switch (PRCGXPD) to stabilize and inhibit the catalytic zinc ion, which is bound in a conserved HEXGHXXGXXH motif (53). The hemopexin-like domain is characterized by a "propeller" of four twisted ␤-sheets, which are thought to confer substrate recognition (53). Together, the hinge region and the hemopexin-like domain unravel substrate proteins for subsequent degradation. Originally thought to cleave only ECM proteins, this family of enzymes is now known to cleave a number of non-ECM substrates as well. For example, cell adhesion molecules (cadherins and integrins) and both growth factors and their receptors (TGF-␤, FGF-R1) are targeted by MMPs (74).Tissue inhibitors of metalloproteinases (TIMPs) are endogenous, specific inhibitors that bind and inhibit MMPs. Four TIMPs (TIMP-1-4) have been identified in vertebrates; these proteins share a similar structure which fits into the active site of the MMP catalytic domain. TIMPs inhibit all MMPs, except TIMP-1, which does not inhibit . A number of other MMP inhibitors have been identified, including RECK (81), ␣2-macroglobulin (4), and tissue factor pathway inhibitor-2 (33).MMPs are classified into six groups based on substrate and sequence homology: collagenases, gelatinases, stromelysins, matrilysins, membrane-type matrix metalloproteinases and "other MMPs" (Fig. 1). Collagenases [MMP-1, -8 (neutrophil collagenase), -13, and -18 (Xenopus laevis collagenase)] cleave collagens I, II, and III at a...

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Decreased collagen-degrading activity could be a marker of prolonged mesangial matrix expansion

Cited by 20 publications

References 29 publications

Protease-Activated Receptor-2 Augments Experimental Crescentic Glomerulonephritis

Protease-Activated Receptor-2 Augments Experimental Crescentic Glomerulonephritis

Matrix metalloproteinases in kidney homeostasis and diseases

Role of matrix metalloproteinases in renal pathophysiologies

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