title: Alteration of p66shc is associated with endothelial dysfunction in the abdominal aortic coarctation of rats.
abstract: To examine the role of p66shc in endothelial dysfunction, we investigated the endothelium-dependent relaxation, protein expression and superoxide production in abdominal aortic coarctation rats. Endothelium-dependent relaxation to acetylcholine was impaired only in the aortic segments above the aortic coarctation (35.0+/-7.1% vs. 86.6+/-6.0% for sham control at 1 microM Ach). The aortic segments exposed to increased blood pressure showed a decreased phosphorylation of endothelial nitric oxide synthase, an increased phosphorylation of p66shc, and an increased superoxide production. Angiotensin II elicited a significantly increased phosphorylation of p66shc in the endothelial cells. Taken together, these findings suggest that the increased phosphorylation of p66shc is one of the important mediators in the impaired endothelium-dependent relaxation of aortic coarctation rats.
authors.affiliation: Infection Signaling Network Research Center, Research Institutes of Biomedical Sciences, Department of Physiology, College of Medicine, Chungnam National University, 6 Munhwa-dong, Jung-gu, Daejeon, Republic of Korea.
authors.forename: Sang Ki
authors.initials: SK
authors.lastname: Lee
authors.forename: Hyo Shin
authors.initials: HS
authors.lastname: Kim
authors.forename: Yun Jeong
authors.initials: YJ
authors.lastname: Song
authors.forename: Hee Kyoung
authors.initials: HK
authors.lastname: Joo
authors.forename: Ji Young
authors.initials: JY
authors.lastname: Lee
authors.forename: Kwon Ho
authors.initials: KH
authors.lastname: Lee
authors.forename: Eun Jung
authors.initials: EJ
authors.lastname: Cho
authors.forename: Chung-Hyun
authors.initials: CH
authors.lastname: Cho
authors.forename: Jin Bong
authors.initials: JB
authors.lastname: Park
authors.forename: Byeong Hwa
authors.initials: BH
authors.lastname: Jeon
mesh_terms: D048868:Adaptor Proteins, Signal Transducing / Q000378:metabolism*; D000803:Angiotensin I / Q000494:pharmacology; D000818:Animals; D001017:Aortic Coarctation / Q000150:complications / Q000503:physiopathology*; D004195:Disease Models, Animal; D004730:Endothelium, Vascular / Q000378:metabolism / Q000503:physiopathology*; D006973:Hypertension / Q000209:etiology / Q000503:physiopathology*; D051379:Mice; D052250:Nitric Oxide Synthase Type III / Q000378:metabolism; D010766:Phosphorylation / Q000187:drug effects; D051381:Rats; D017207:Rats, Sprague-Dawley; D055765:Shc Signaling Adaptor Proteins; D000071425:Src Homology 2 Domain-Containing, Transforming Protein 1; D013482:Superoxide Dismutase / Q000378:metabolism; D013481:Superoxides / Q000378:metabolism
chemical_list: D048868:Adaptor Proteins, Signal Transducing; D055765:Shc Signaling Adaptor Proteins; C528034:Shc1 protein, mouse; C528035:Shc1 protein, rat; D000071425:Src Homology 2 Domain-Containing, Transforming Protein 1; D013481:Superoxides; D000803:Angiotensin I; D052250:Nitric Oxide Synthase Type III; D013482:Superoxide Dismutase