Intricate Functions of Matrix Metalloproteinases in Physiological and Pathological Conditions
Identifieur interne : 000C33 ( Main/Merge ); précédent : 000C32; suivant : 000C34Intricate Functions of Matrix Metalloproteinases in Physiological and Pathological Conditions
Auteurs : Rahul Mittal [États-Unis] ; Amit P. Patel ; Luca H. Debs ; Desiree Nguyen ; Kunal Patel ; M'Hamed Grati ; Jeenu Mittal ; Denise Yan ; Prem Chapagain [États-Unis] ; Xue Zhong Liu [États-Unis]Source :
- Journal of Cellular Physiology [ 0021-9541 ] ; 2016-12.
Abstract
Matrix metalloproteinases (MMPs) are a diverse group of proteolytic enzymes and play an important role in the degradation and remodeling of the extracellular matrix (ECM). In normal physiological conditions, MMPs are usually minimally expressed. Despite their low expression, MMPs have been implicated in many cellular processes ranging from embryological development to apoptosis. The activity of MMPs is controlled at three different stages: (1) transcription; (2) zymogen activation; and (3) inhibition of active forms by tissue inhibitor metalloproteinases (TIMPs). They can collectively degrade any component of ECM and basement membrane, and their excessive activity has been linked to numerous pathologies mainly including, but not limited to, tumor invasion and metastasis. The lack of information about several MMPs and the steady stream of new discoveries suggest that there is much more to be studied in this field. In particular, there is a need for controlling their expression in disease states. Various studies over the past 30 years have found that each MMP has a specific mode of activation, action, and inhibition. Drugs specifically targeting individual MMPs could revolutionize the treatment of a great number of health conditions and tremendously reduce their burden. In this review article, we have summarized the recent advances in understanding the role of MMPs in physiological and pathological conditions. J. Cell. Physiol. 231: 2599–2621, 2016. © 2016 Wiley Periodicals, Inc.
Ribbon diagram of the full structure of MMP‐9 created with Swiss‐model and rendered with Pymol showing pro and catalytic domains.
Url:
DOI: 10.1002/jcp.25430
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Debs</name><affiliation><wicri:noCountry code="subField">Miami</wicri:noCountry></affiliation></author><author><name sortKey="Nguyen, Desiree" sort="Nguyen, Desiree" uniqKey="Nguyen D" first="Desiree" last="Nguyen">Desiree Nguyen</name><affiliation><wicri:noCountry code="subField">Miami</wicri:noCountry></affiliation></author><author><name sortKey="Patel, Kunal" sort="Patel, Kunal" uniqKey="Patel K" first="Kunal" last="Patel">Kunal Patel</name><affiliation><wicri:noCountry code="subField">Miami</wicri:noCountry></affiliation></author><author><name sortKey="Grati, M Hamed" sort="Grati, M Hamed" uniqKey="Grati M" first="M'Hamed" last="Grati">M'Hamed Grati</name><affiliation><wicri:noCountry code="subField">Miami</wicri:noCountry></affiliation></author><author><name sortKey="Mittal, Jeenu" sort="Mittal, Jeenu" uniqKey="Mittal J" first="Jeenu" last="Mittal">Jeenu Mittal</name><affiliation><wicri:noCountry code="subField">Miami</wicri:noCountry></affiliation></author><author><name sortKey="Yan, Denise" sort="Yan, Denise" uniqKey="Yan D" first="Denise" last="Yan">Denise Yan</name><affiliation><wicri:noCountry code="subField">Miami</wicri:noCountry></affiliation></author><author><name sortKey="Chapagain, Prem" sort="Chapagain, Prem" uniqKey="Chapagain P" first="Prem" last="Chapagain">Prem Chapagain</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">Floride</region></placeName><wicri:cityArea>Department of Physics, Florida International University, Miami</wicri:cityArea></affiliation><affiliation></affiliation></author><author><name sortKey="Liu, Xue Zhong" sort="Liu, Xue Zhong" uniqKey="Liu X" first="Xue Zhong" last="Liu">Xue Zhong Liu</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">Floride</region></placeName><wicri:cityArea>Department of Otolaryngology, University of Miami Miller School of Medicine, Miami</wicri:cityArea></affiliation><affiliation></affiliation><affiliation></affiliation><affiliation wicri:level="1"><country wicri:rule="url">États-Unis</country></affiliation></author></analytic><monogr></monogr><series><title level="j" type="main">Journal of Cellular Physiology</title><title level="j" type="alt">JOURNAL OF CELLULAR PHYSIOLOGY</title><idno type="ISSN">0021-9541</idno><idno type="eISSN">1097-4652</idno><imprint><biblScope unit="vol">231</biblScope><biblScope unit="issue">12</biblScope><biblScope unit="page" from="2599">2599</biblScope><biblScope unit="page" to="2621">2621</biblScope><biblScope unit="page-count">23</biblScope><date type="published" when="2016-12">2016-12</date></imprint><idno type="ISSN">0021-9541</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0021-9541</idno></seriesStmt></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Matrix metalloproteinases (MMPs) are a diverse group of proteolytic enzymes and play an important role in the degradation and remodeling of the extracellular matrix (ECM). In normal physiological conditions, MMPs are usually minimally expressed. Despite their low expression, MMPs have been implicated in many cellular processes ranging from embryological development to apoptosis. The activity of MMPs is controlled at three different stages: (1) transcription; (2) zymogen activation; and (3) inhibition of active forms by tissue inhibitor metalloproteinases (TIMPs). They can collectively degrade any component of ECM and basement membrane, and their excessive activity has been linked to numerous pathologies mainly including, but not limited to, tumor invasion and metastasis. The lack of information about several MMPs and the steady stream of new discoveries suggest that there is much more to be studied in this field. In particular, there is a need for controlling their expression in disease states. Various studies over the past 30 years have found that each MMP has a specific mode of activation, action, and inhibition. Drugs specifically targeting individual MMPs could revolutionize the treatment of a great number of health conditions and tremendously reduce their burden. In this review article, we have summarized the recent advances in understanding the role of MMPs in physiological and pathological conditions. J. Cell. Physiol. 231: 2599–2621, 2016. © 2016 Wiley Periodicals, Inc.</div><div type="abstract" xml:lang="en">Ribbon diagram of the full structure of MMP‐9 created with Swiss‐model and rendered with Pymol showing pro and catalytic domains.</div></front></TEI></record>Pour manipuler ce document sous Unix (Dilib)
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