Tags

Type your tag names separated by a space and hit enter

Endogenous and synthetic MMP inhibitors in CNS physiopathology.
Prog Brain Res. 2014; 214:313-51.PB

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.

Authors+Show Affiliations

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.Neuroinfection Laboratory, Institute for Infectious Diseases, University of Bern, Bern, Switzerland.Neuroinfection Laboratory, Institute for Infectious Diseases, University of Bern, Bern, Switzerland.Iproteos S.L., Barcelona, Spain.Iproteos S.L., Barcelona, Spain.Iproteos S.L., Barcelona, Spain; Institute for Research in Biomedicine (IRB Barcelona), Barcelona, Spain.Neuroinfection Laboratory, Institute for Infectious Diseases, University of Bern, Bern, Switzerland; Biology Division, Spiez Laboratory, Swiss Federal Office for Civil Protection, Spiez, Switzerland.Aix Marseille Université, CNRS, UMR 7259, NICN, 13344, Marseille, France. Electronic address: michel.khrestchatisky@univ-amu.fr.

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't
Review

Language

eng

PubMed ID

25410364

Citation

Baranger, Kévin, et al. "Endogenous and Synthetic MMP Inhibitors in CNS Physiopathology." Progress in Brain Research, vol. 214, 2014, pp. 313-51.
Baranger K, Rivera S, Liechti FD, et al. Endogenous and synthetic MMP inhibitors in CNS physiopathology. Prog Brain Res. 2014;214:313-51.
Baranger, K., Rivera, S., Liechti, F. D., Grandgirard, D., Bigas, J., Seco, J., Tarrago, T., Leib, S. L., & Khrestchatisky, M. (2014). Endogenous and synthetic MMP inhibitors in CNS physiopathology. Progress in Brain Research, 214, 313-51. https://doi.org/10.1016/B978-0-444-63486-3.00014-1
Baranger K, et al. Endogenous and Synthetic MMP Inhibitors in CNS Physiopathology. Prog Brain Res. 2014;214:313-51. PubMed PMID: 25410364.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Endogenous and synthetic MMP inhibitors in CNS physiopathology. AU - Baranger,Kévin, AU - Rivera,Santiago, AU - Liechti,Fabian D, AU - Grandgirard,Denis, AU - Bigas,Judit, AU - Seco,Jesús, AU - Tarrago,Teresa, AU - Leib,Stephen L, AU - Khrestchatisky,Michel, PY - 2014/11/21/entrez PY - 2014/11/21/pubmed PY - 2015/8/20/medline KW - Alzheimer's disease KW - EAE KW - Synthetic MMP inhibitors KW - bacterial meningitis KW - multiple sclerosis SP - 313 EP - 51 JF - Progress in brain research JO - Prog Brain Res VL - 214 N2 - 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. SN - 1875-7855 UR - https://www.unboundmedicine.com/medline/citation/25410364/Endogenous_and_synthetic_MMP_inhibitors_in_CNS_physiopathology_ L2 - https://linkinghub.elsevier.com/retrieve/pii/B978-0-444-63486-3.00014-1 DB - PRIME DP - Unbound Medicine ER -