Variant estrogen receptor-c-Src molecular interdependence and c-Src structural requirements for endothelial NO synthase activation.

Variant estrogen receptor-c-Src molecular interdependence and c-Src structural requirements for endothelial NO synthase activation. Research Abstract Details 

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Variant estrogen receptor-c-Src molecular interdependence and c-Src structural requirements for endothelial NO synthase activation. Abstract Text:

Lei Li,Koji Hisamoto,Kyung Hee Kim,M Page Haynes,Philip M Bauer,Archana Sanjay,Mark Collinge,Roland Baron,William C Sessa,Jeffrey R Bender,Lei Li,Koji Hisamoto,Kyung Hee Kim,M Page Haynes,Philip M Bauer,Archana Sanjay,Mark Collinge,Roland Baron,William C Sessa,Jeffrey R Bender,

Little is known about the tyrosine kinase c-Src's function in the systemic circulation, in particular its role in arterial responses to hormonal stimuli. In human aortic and venous endothelial cells, c-Src is indispensable for 17beta-estradiol (E2)-stimulated phosphatidylinositol 3-kinase/Akt/endothelial NO synthase (eNOS) pathway activation, a possible mechanism in E2-mediated vascular protection. Here we show that c-Src supports basal and E2-stimulated NO production and is required for E2-induced vasorelaxation in murine aortas. Only membrane c-Src is structurally and functionally involved in E2-induced eNOS activation. Independent of c-Src kinase activity, c-Src is associated with an N-terminally truncated estrogen receptor alpha variant (ER46) and eNOS in the plasma membrane through its "open" (substrate-accessible) conformation. In the presence of E2, c-Src kinase is activated by membrane ER46 and in turn phosphorylates ER46 for subsequent ER46 and c-Src membrane recruitment, the assembly of an eNOS-centered membrane macrocomplex, and membrane-initiated eNOS activation. Overall, these results provide insights into a critical role for the tyrosine kinase c-Src in estrogen-stimulated arterial responses, and in membrane-initiated rapid signal transduction, for which obligate complex assembly and localization require the c-Src substrate-accessible structure.

Variant estrogen receptor-c-Src molecular interdependence and c-Src structural requirements for endothelial NO synthase activation. Publishing Authors By Initials

L Li,K Hisamoto,KH Kim,MP Haynes,PM Bauer,A Sanjay,M Collinge,R Baron,WC Sessa,JR Bender,L Li,K Hisamoto,KH Kim,MP Haynes,PM Bauer,A Sanjay,M Collinge,R Baron,WC Sessa,JR Bender,

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Variant estrogen receptor-c-Src molecular interdependence and c-Src structural requirements for endothelial NO synthase activation. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Proceedings of the National Academy of Sciences of

VOLUME: 104

Page Numbers: 16468-73

Journal Abbreviation: Proc. Natl. Acad. Sci. U.S.A.

ISSN: 0027-8424

DAY: 5

MONTH: 10

YEAR: 2007

Variant estrogen receptor-c-Src molecular interdependence and c-Src structural requirements for endothelial NO synthase activation. Information

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LANGUAGE: eng

NlmUniqueID: 7505876

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Grant and Affiliation Information for Variant estrogen receptor-c-Src molecular interdependence and c-Src structural requirements for endothelial NO synthase activation.

AFFILIATION: Division of Cardiovascular Medicine, Department of Internal Medicine, Yale University School of Medicine, 300 Cedar Street, New Haven, CT 06520, USA.

Country: United States

AGENCY: United States NHLBI

GRANT: R01HL 67182

ACRONYM: HL

MEDLINETA: Proc Natl Acad Sci U S A

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