Metalloproteases

Nagase, Hideaki

doi:10.1002/0471140864.ps2104s24

Cited by 21 publications

(23 citation statements)

References 26 publications

(26 reference statements)

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“…The term metallo-proteases encompasses esopeptidase and endopeptidase involved in many biological processes, such as morphogenesis, metabolism of biologically active peptides and hormones, development, regulation of cell cycle, cell proliferation, migration, adhesion and antibiotics metabolism (Nagase, 2001). In the MEROPS database, metallo-protease families are grouped into 14 different clans, namely MA, MC, MD, ME, MJ, MK, MM, MO, MP (these requiring only one catalytic metal ion) and MF, MG, MH, MQ (these containing two metal ions acting co-catalytically).…”

Section: Introductionmentioning

confidence: 99%

“…Human metallo-peptidases play important roles in a variety of biological processes and the unbalance of their activity and expression is often at the basis of diseases like cancer, neurodegeneration, inflammation, arthritis, cardiovascular diseases. For this reason, they have been historically represented an intriguing drug targets, even though their therapeutical inhibition have raised many questions, since (i) the activity of these enzymes is pleiotropic so that their inhibition could negatively modulate some cellular functions; (ii) a large number of inhibitors are not selective for a single enzyme (Nagase, 2001). For a detailed properties of a single enzyme, it is possible to refer to the ''Handbook of Proteolytic enzymes'' (Barret et al, 2004).…”

Section: Introductionmentioning

confidence: 99%

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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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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

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

View full text Add to dashboard Cite

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“…All MMPs are synthesized as prepro-enzyme and secreted as inactive pro-MMPs in most cases. Many of MMPs are inducible to growth factors, cytokines, physical stress, oncogenic cellular transformation, and chemical agents [Nagase and Woessner, 1999]. The enhanced MMP gene expression may be down-regulated by suppressive factors such as transforming growth factor b, retinoic acid, and glucocorticoid.…”

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confidence: 99%

Soluble glucocorticoid‐induced tumor necrosis factor receptor (sGITR) increased MMP‐9 activity in murine macrophage

Lee

Shin

Kwon

et al. 2003

J of Cellular Biochemistry

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Glucocorticoid induced tumor necrosis factor receptor (GITR), a new TNFR family, increased production of matrix matalloproteinase (MMP-9) in murine macrophages. Murine macrophages produced a band of gelatinolytic activity at 100 kDa when stimulated for 18 h with soluble GITR. MMP-9 was identified by gelatin zymography and Western blot. Previous results demonstrated that murine macrophages express GITR and GITR ligand constitutively. Induction of MMP-9 was synergistic with co-treatment of INF-gamma. MMPs could play a critical role in progression and promotion of tissue injury after inflammation stimulated by GITR/ligand system.

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“…Under normal physiological conditions, MMP activities are exactly regulated at the transcription level, at precursor zymogen activation, through interaction with specific ECM components and by inhibition of endogenous inhibitors (TIMPs) [14]. TIMPs are specific inhibitors of MMPs that participate in controlling the local activities of MMPs in tissues [15].…”

Section: Introductionmentioning

confidence: 99%

Circulating and adipose tissue matrix metalloproteinases in cardiometabolic risk environments: pathophysiological aspects

Berg

Schreier

Miksztowicz

2014

Hormone Molecular Biology and Clinical Investigation

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Matrix metalloproteinases (MMPs) play an important role during physiological tissue remodeling in embryonic development and angiogenesis, as well as in pathophysiological conditions such as obesity and development and vulnerability of atherosclerotic plaque. Moreover, MMP circulating levels have emerged as potential biomarkers of cardiovascular disease. MMP expression and activity are regulated by different factors such as insulin resistance and obesity. Expanded fat tissue has been demonstrated to be an active organ, where MMPs also exert a role in adipogenesis, angiogenesis, and proliferation of extracellular matrix (ECM). However, the lack of association between adipose tissue and plasma levels of some MMPs, specifically MMP-2 and MMP-9, suggests that this tissue is not a major contributor to circulating gelatinases. MMPs are also co-expressed or co-repressed in response to inflammatory adipocytokines, like adiponectin and leptin. Adiponectin may also play a protective role in plaque rupture through selectively increasing the tissue inhibitor of metalloproteinase (TIMP) expression. Leptin induces the expression of MMP-2 activators as well as the expression of MMP-2, MMP-9, and TIMP-1 in different human cells. Furthermore, sex hormones also participate in MMP regulation. In postmenopausal women, hormone replacement therapy produces an increase in MMP activity, leading to a breakdown in ECM homeostasis and accelerated progression of vascular pathologies. Besides, in men, an inverse relationship between testosterone levels and MMP-2 activity has been described. It is still necessary to go forward in the study of MMPs in different metabolic situations to corroborate their role as vulnerable plaque biomarkers.

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Metalloproteases

Cited by 21 publications

References 26 publications

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

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

Soluble glucocorticoid‐induced tumor necrosis factor receptor (sGITR) increased MMP‐9 activity in murine macrophage

Circulating and adipose tissue matrix metalloproteinases in cardiometabolic risk environments: pathophysiological aspects

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