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中枢神经系统生理病理学中的内源性和合成基质金属蛋白酶抑制剂

Endogenous and synthetic MMP inhibitors in CNS physiopathology.

作者信息

Baranger Kévin, Rivera Santiago, Liechti Fabian D, Grandgirard Denis, Bigas Judit, Seco Jesús, Tarrago Teresa, Leib Stephen L, Khrestchatisky Michel

机构信息

Aix Marseille Université, CNRS, UMR 7259, NICN, 13344, Marseille, France; Neurology and Neuropsychology Department, AP-HM, Marseille, France.

Aix Marseille Université, CNRS, UMR 7259, NICN, 13344, Marseille, France.

出版信息

Prog Brain Res. 2014;214:313-51. doi: 10.1016/B978-0-444-63486-3.00014-1.

Abstract

Matrix metalloproteinases (MMPs, including the membrane-type MMPs (MT-MMPs)), a disintegrin and metalloproteinase (ADAM), and ADAM with thrombospondin motifs belong to the metzincins, a subclass of metalloproteinases that contain a Met residue and a Zn(2+) ion at the catalytic site necessary for enzymatic reaction. MMP proteolytic activity is mainly controlled by their natural tissue inhibitors of metalloproteinase (TIMP). A number of synthetic inhibitors have been developed to control deleterious MMP activity. The roles of MMPs and some of their ECM substrates in CNS physiology and pathology are covered by other chapters of the present volume and will thus not be addressed in depth. This chapter will focus (i) on the endogenous MMP inhibitors in the CNS, (ii) on MMP and TIMP regulations in three large classes of neuropathologic processes (inflammatory, neurodegenerative, and infectious), and (iii) on synthetic inhibitors of MMPs and the perspective of their use in different brain diseases.

摘要

基质金属蛋白酶(MMPs,包括膜型MMPs(MT - MMPs))、解整合素和金属蛋白酶(ADAM)以及具有血小板反应蛋白基序的ADAM属于金属锌蛋白酶,这是金属蛋白酶的一个亚类,在酶促反应所需的催化位点含有一个Met残基和一个Zn(2+)离子。MMP的蛋白水解活性主要由其天然的金属蛋白酶组织抑制剂(TIMP)控制。已经开发了许多合成抑制剂来控制有害的MMP活性。MMPs及其一些细胞外基质底物在中枢神经系统生理和病理中的作用在本卷的其他章节中已有阐述,因此不再深入探讨。本章将重点关注:(i)中枢神经系统中的内源性MMP抑制剂;(ii)在三类主要神经病理过程(炎症、神经退行性变和感染)中的MMP和TIMP调节;(iii)MMP的合成抑制剂及其在不同脑部疾病中的应用前景。

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