| Literature DB >> 25658730 |
Minh Vu Chuong Nguyen1, Bernard Lardy2, Marie-Hélène Paclet2, Francis Rousset1, Sylvie Berthier1, Athan Baillet3, Laurent Grange3, Philippe Gaudin3, Françoise Morel1.
Abstract
NADPH oxidases, Nox, are a family of isoenzymes, composed of seven members, whose sole function is to produce reactive oxygen species (ROS). Although Nox catalyze the same enzymatic reaction, they acquired from a common ancestor during evolution, specificities related to their tissue expression, subcellular localization, activation mechanisms and regulation. Their functions could vary depending on the pathophysiological state of the tissues. Indeed, ROS are not only bactericidal weapons in phagocytes but also essential cellular signaling molecules and their overproduction is involved in chronic diseases and diseases of aging. The understanding of the mechanisms involved in the function of Nox and the emergence of Nox inhibitors, require a thorough knowledge of their nature and structure. The objectives of this review are to highlight, in a structure/function approach, the main similar and differentiated properties shared by the human Nox isoenzymes.Entities:
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Year: 2015 PMID: 25658730 DOI: 10.1051/medsci/20153101012
Source DB: PubMed Journal: Med Sci (Paris) ISSN: 0767-0974 Impact factor: 0.818