Tissue mRNA expression in rat of newly described matrix metalloproteinases

Bernal, Fabián; Hartung, Hans‐Peter; Kieseier, Bernd C.

doi:10.4067/s0716-97602005000200016

Cited by 31 publications

(26 citation statements)

References 13 publications

(12 reference statements)

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“…MMP-24 is also expressed in tubular epithelial cells along the nephron of human kidney (49,68). mRNA for MMP-24, -25, -27, and -28 has also been detected in the rat kidney (7). In mouse kidney, TIMP-1 is expressed at low levels, TIMPs-2 and -3 at high levels, and TIMP-4 is not expressed (28).…”

Section: Renal Mmpsmentioning

confidence: 99%

Role of matrix metalloproteinases in renal pathophysiologies

Catania¹,

Chen²,

Parrish³

2007

American Journal of Physiology-Renal Physiology

345

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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Section: Renal Mmpsmentioning

confidence: 99%

Role of matrix metalloproteinases in renal pathophysiologies

Catania¹,

Chen²,

Parrish³

2007

American Journal of Physiology-Renal Physiology

345

314

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“…Bone, kidney, heart [117] MMP-28 (epilysin) Skin (KC), brain, lung heart, kidney, testis, placenta, colon, intestine, pancreas [118] Fb: fibroblasts; KC: keratinocytes; EC: endothelial cells.…”

Section: Mmp-27mentioning

confidence: 99%

Biological role of matrix metalloproteinases: a critical balance

Löffek

Schilling

2010

European Respiratory Journal

615

369

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Matrix metalloproteinases (MMPs) are members of the metzincin group of proteases which share the conserved zinc-binding motif in their catalytic active site. It was originally thought that their main function is to degrade the various components of the extracellular matrix (ECM), yet recent studies have led us to appreciate their significance as regulators of extracellular tissue signalling networks. Due to the broad spectrum of their substrate specificity, MMPs contribute to the homeostasis of many tissues and participate in several physiological processes, such as bone remodelling, angiogenesis, immunity and wound healing. MMP activity is tightly controlled at the level of transcription, pro-peptide activation and inhibition by tissue inhibitors of MMPs. Dysregulated MMP activity leads to pathological conditions such as arthritis, inflammation and cancer, thus highlighting MMPs as promising therapeutic targets. Analysis of MMP mutant mice has proved to be an essential tool for the identification of novel functions and interactions of single MMP members. Advancing our understanding of the MMP contribution to tissue homeostasis will lead us to identify causal relationships between their dysregulation and the development of disease pathologies, thus guiding us to successful MMP-directed therapies.

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“…Structure and function Matrix metalloproteinase-28 (MMP-28), also known as epilysin, is a newly discovered MMP expressed in a number of normal tissues, such as testis, lung, intestine, heart brain and skin (Bernal et al, 2005;Illman et al, 2001;Lohi et al, 2001) as well as in a variety of tumors and tumor cell lines .…”

Section: Mmp-28mentioning

confidence: 99%

Human matrix metalloproteinases: An ubiquitarian class of enzymes involved in several pathological processes

Sbardella

Fasciglione

Gioia

et al. 2012

Molecular Aspects of Medicine

208

212

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a b s t r a c tHuman matrix metalloproteinases (MMPs) belong to the M10 family of the MA clan of endopeptidases. They are ubiquitarian enzymes, structurally characterized by an active site where a Zn 2+ atom, coordinated by three histidines, plays the catalytic role, assisted by a glutamic acid as a general base. Various MMPs display different domain composition, which is very important for macromolecular substrates recognition. Substrate specificity is very different among MMPs, being often associated to their cellular compartmentalization and/or cellular type where they are expressed. An extensive review of the different MMPs structural and functional features is integrated with their pathological role in several types of diseases, spanning from cancer to cardiovascular diseases and to neurodegeneration. It emerges a very complex and crucial role played by these enzymes in many physiological and pathological processes.

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Tissue mRNA expression in rat of newly described matrix metalloproteinases

Cited by 31 publications

References 13 publications

Role of matrix metalloproteinases in renal pathophysiologies

Role of matrix metalloproteinases in renal pathophysiologies

Biological role of matrix metalloproteinases: a critical balance

Human matrix metalloproteinases: An ubiquitarian class of enzymes involved in several pathological processes

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