Abstract
Endothelial nitric oxide synthase (eNOS) is important for cardiovascular homeostasis, vessel remodeling, and angiogenesis. Given the impact of endothelium- derived nitric oxide (NO) in vascular biology, much work in the past several years has focused on the control of NO synthesis by regulatory proteins that influence its function. Indeed calcium-activated calmodulin is important for regulation of NOS activity. Herein we discuss why other proteins, in addition to calmodulin, are necessary for eNOS regulation and summarize the biology of negative and positive regulators of eNOS function in vitro, in cells, and in blood vessels.
Footnotes
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This work is supported by grants from the National Institutes of Health (RO1 HL57665, HL61371, and HL64793 to W.C.S.; T32HL10183 to D.F.) and a Grant-in-Aid from the American Heart Association (National Grant to W.C.S.). J.P.G. is the recipient of a fellowship from the Canadian Institutes of Health Research. W.C.S. is an Established Investigator of the American Heart Association.
- Abbreviations:
- NO
- nitric oxide
- eNOS
- endothelial NO synthase
- ACh
- acetylcholine
- B2
- bradykinin 2
- CaM
- calmodulin
- Erk
- extracellular signal-related kinase
- GA
- geldanamycin
- GST
- glutathioneS-transferase
- hsp90
- heat shock protein 90
- ID4
- intracellular domain 4
- IGF
- insulin-like growth factor
- NOSIP
- nitric oxide synthase interacting protein
- PI-3K
- phosphatidylinositol 3-kinase
- VEGF
- vascular endothelial growth factor
- Received February 2, 2001.
- Accepted May 25, 2001.
- The American Society for Pharmacology and Experimental Therapeutics
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Post-Translational Control of Endothelial Nitric Oxide Synthase: Why Isn't Calcium/Calmodulin Enough?
