Regulation of NADPH oxidase-mediated superoxide production by acetylation and deacetylation

0546151 - FZÚ 2022 RIV CH eng J - Journal Article
Xia, N. - Tenzer, S. - Lunov, Oleg - Karl, M. - Simmet, T. - Daiber, A. - Münzel, T. - Reifenberg, G. - Förstermann, U. - Li, H.
Regulation of NADPH oxidase-mediated superoxide production by acetylation and deacetylation.
Frontiers in Physiology. Roč. 12, Aug. (2021), č. článku 693702. ISSN 1664-042X. E-ISSN 1664-042X
Institutional support: RVO:68378271
Keywords : NADPH oxidase * acetylation and deacetylation * oxidative stress
OECD category: Biochemistry and molecular biology
Impact factor: 4.755, year: 2021
Method of publishing: Open access

Oral treatment of apolipoprotein E-knockout (ApoE-KO) mice with the putative sirtuin 1 (SIRT1) activator resveratrol led to a reduction of nicotinamide adenine dinucleotide phosphate (NADPH) oxidase activity in the heart. In contrast, the SIRT1 inhibitor EX527 enhanced the superoxide production in isolated human polymorphonuclear granulocytes. In human monocytic THP-1 cells, phorbol ester-stimulated superoxide production was enhanced by inhibitors of histone deacetylases (HDACs including quisinostat, trichostatin A (TSA), PCI34051, and tubastatin A) and decreased by inhibitors of histone acetyltransferases [such as garcinol, curcumin, and histone acetyltransferase (HAT) Inhibitor II]. These results indicate that protein acetylation and deacetylation may represent crucial mechanisms regulating NADPH oxidase-mediated superoxide production.

Permanent Link: http://hdl.handle.net/11104/0322796