Regulation of protein function by S-nitrosation and S-glutathionylation: processes and targets in cardiovascular pathophysiology

Autor: Pierre Leroy, Alfonso Pompella, Caroline Gaucher, Isabelle Lartaud, Alessandro Corti, Eugenia Belcastro
Přispěvatelé: Cibles thérapeutiques, formulation et expertise pré-clinique du médicament (CITHEFOR), Université de Lorraine (UL), Medical School [Pisa], University of Pisa - Università di Pisa
Rok vydání: 2017
Předmět:
0301 basic medicine
Nitrosation
Clinical Biochemistry
Cell
S-glutathionylation
RNS
[SDV.BC.BC]Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC]
medicine.disease_cause
Nitric Oxide
Biochemistry
Nitric oxide
03 medical and health sciences
chemistry.chemical_compound
cardiovascular diseases
glutathione
mixed disulfides
nitric oxide
ROS
S-nitrosation
Animals
Cardiovascular Diseases
Glutathione
Humans
Molecular Biology
[SDV.MHEP.CSC]Life Sciences [q-bio]/Human health and pathology/Cardiology and cardiovascular system
[SDV.BC.IC]Life Sciences [q-bio]/Cellular Biology/Cell Behavior [q-bio.CB]
medicine
S-Glutathionylation
[SDV.IB.BIO]Life Sciences [q-bio]/Bioengineering/Biomaterials
[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry
Molecular Biology/Biomolecules [q-bio.BM]
030104 developmental biology
medicine.anatomical_structure
chemistry
Function (biology)
Oxidative stress
Cysteine
Zdroj: Biological Chemistry
Biological Chemistry, De Gruyter, 2017, 398 (12), pp.1267-1293. ⟨10.1515/hsz-2017-0150⟩
ISSN: 1437-4315
1431-6730
DOI: 10.1515/hsz-2017-0150⟩
Popis: Decades of chemical, biochemical and pathophysiological research have established the relevance of post-translational protein modifications induced by processes related to oxidative stress, with critical reflections on cellular signal transduction pathways. A great deal of the so-called ‘redox regulation’ of cell function is in fact mediated through reactions promoted by reactive oxygen and nitrogen species on more or less specific aminoacid residues in proteins, at various levels within the cell machinery. Modifications involving cysteine residues have received most attention, due to the critical roles they play in determining the structure/function correlates in proteins. The peculiar reactivity of these residues results in two major classes of modifications, with incorporation of NO moieties (S-nitrosation, leading to formation of proteinS-nitrosothiols) or binding of low molecular weight thiols (S-thionylation, i.e. in particularS-glutathionylation,S-cysteinylglycinylation andS-cysteinylation). A wide array of proteins have been thus analyzed in detail as far as their susceptibility to either modification or both, and the resulting functional changes have been described in a number of experimental settings. The present review aims to provide an update of available knowledge in the field, with a special focus on the respective (sometimes competing and antagonistic) roles played by proteinS-nitrosations andS-thionylations in biochemical and cellular processes specifically pertaining to pathogenesis of cardiovascular diseases.
Databáze: OpenAIRE
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