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Cited by 993

The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.

Adiponectin Stimulates Production of Nitric Oxide in Vascular Endothelial Cells

Open access
Chen, Hui, Montagnani, Monica, Funahashi, Tohru, Shimomura, Iichiro, Quon, Michael J.·2003·Journal of Biological Chemistry
DOI 10.1074/jbc.m307878200
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Abstract

Adiponectin is secreted by adipose cells and mimics many metabolic actions of insulin. However, mechanisms by which adiponectin acts are poorly understood. The vascular action of insulin to stimulate endothelial production of nitric oxide (NO), leading to vasodilation and increased blood flow is an important component of insulin-stimulated whole body glucose utilization. Therefore, we hypothesized that adiponectin may also stimulate production of NO in endothelium. Bovine aortic endothelial cells in primary culture loaded with the NO-specific fluorescent dye 4,5-diaminofluorescein diacetate (DAF-2 DA) were treated with lysophosphatidic acid (LPA) (a calcium-releasing agonist) or adiponectin (10 microg/ml bacterially produced full-length adiponectin). LPA treatment increased production of NO by approximately 4-fold. Interestingly, adiponectin treatment significantly increased production of NO by approximately 3-fold. Preincubation of cells with wortmannin (phosphatidylinositol 3-kinase inhibitor) blocked only adiponectin- but not LPA-mediated production of NO. Using phospho-specific antibodies, we observed that either adiponectin or insulin treatment (but not LPA treatment) caused phosphorylation of both Akt at Ser473 and endothelial nitric-oxide synthase (eNOS) at Ser1179 that was inhibitable by wortmannin. We next transfected bovine aortic endothelial cells with dominant-inhibitory mutants of Akt (Akt-AAA) or AMP-activated protein kinase (AMPK) (AMPKK45R). Neither mutant affected production of NO in response to LPA treatment. Importantly, only AMPKK45R, but not Akt-AAA, caused a significant partial inhibition of NO production in response to adiponectin. Moreover, AMPK-K45R inhibited phosphorylation of eNOS at Ser1179 in response to adiponectin but not in response to insulin. We conclude that adiponectin has novel vascular actions to directly stimulate production of NO in endothelial cells using phosphatidylinositol 3-kinase-dependent pathways involving phosphorylation of eNOS at Ser1179 by AMPK. Thus, the effects of adiponectin to augment metabolic actions of insulin in vivo may be due, in part, to vasodilator actions of adiponectin.

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Metadata

Authors
Chen, H., Montagnani, M., Funahashi, T., Shimomura, I., & Quon, M. J.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
2003-11
Volume
278
Issue
45
Pages
45021-45026
ISSN
0021-9258 (ISSN-L)
DOI
10.1074/jbc.m307878200
OpenAlex
W2055378578
Cited by
993
References
7
FWCI
31.16
Type
journal article
Language
en
Open access
hybrid

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