Nitric oxide and heme-NO stimulate superoxide production by NADPH oxidase 5. Free Radic Biol Med 2021 Aug 20;172:252-263
Date
06/18/2021Pubmed ID
34139309Pubmed Central ID
PMC8355125DOI
10.1016/j.freeradbiomed.2021.06.008Scopus ID
2-s2.0-85109100150 (requires institutional sign-in at Scopus site) 8 CitationsAbstract
Nitric oxide (NO) is a ubiquitous cell signaling molecule which mediates widespread and diverse processes in the cell. These NO dependent effects often involve activation (e.g. NO binding to the heme group of soluble guanylyl cyclase for cGMP production) or inactivation (e.g. S-nitrosation) of protein targets. We studied the effect of NO and heme-NO on the transmembrane signaling enzyme NADPH oxidase 5 (NOX5), a heme protein which produces superoxide in response to increases in intracellular calcium. We found that treatment with NO donors increases NOX5 activity through heme-dependent effects, and that this effect could be recapitulated by the addition of heme-NO. This work adds to our understanding of NOX5 regulation in the cell but also provides a framework for understanding how NO could cause widespread changes in hemeprotein activity based on different affinities for heme v. heme-NO, and helps explain the opposing roles NO plays in activation and inactivation of hemeprotein targets.
Author List
Sweeny EA, Hunt AP, Batka AE, Schlanger S, Lehnert N, Stuehr DJAuthor
Elizabeth Sweeny PhD Assistant Professor in the Biochemistry department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
Guanylate CyclaseHeme
NADPH Oxidase 5
NADPH Oxidases
Nitric Oxide
Soluble Guanylyl Cyclase
Superoxides
