Tyrosine Phosphatase 1B NO Attenuates Insulin Signaling and Motility in Aortic Smooth Muscle Cells via Protein

نویسندگان

  • Nair Sreejayan
  • Yi Lin
  • Aviv Hassid
چکیده

Mediated Mechanism − Tyrosine Phosphatase 1B NO Attenuates Insulin Signaling and Motility in Aortic Smooth Muscle Cells via Protein Print ISSN: 1079-5642. Online ISSN: 1524-4636 Copyright © 2002 American Heart Association, Inc. All rights reserved. Greenville Avenue, Dallas, TX 75231 is published by the American Heart Association, 7272 Arteriosclerosis, Thrombosis, and Vascular Biology doi: 10.1161/01.ATV.0000020550.65963.E9 2002;22:1086-1092; originally published online May 2, 2002; Arterioscler Thromb Vasc Biol. http://atvb.ahajournals.org/content/22/7/1086 World Wide Web at: The online version of this article, along with updated information and services, is located on the http://atvb.ahajournals.org/content/suppl/2002/07/15/22.7.1086.DC1.html Data Supplement (unedited) at:

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NO attenuates insulin signaling and motility in aortic smooth muscle cells via protein tyrosine phosphatase 1B-mediated mechanism.

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Hassid, Aviv, Shile Huang, and Jian Yao. Role of PTP-1B in aortic smooth muscle cell motility and tyrosine phosphorylation of focal adhesion proteins. Am. J. Physiol. 277 (Heart Circ. Physiol. 46): H192–H198, 1999.—Recent studies have focused attention on the role of protein tyrosine kinases in vascular smooth muscle cell biology, but similar information regarding protein tyrosine phosphatases ...

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Role of PTP-1B in aortic smooth muscle cell motility and tyrosine phosphorylation of focal adhesion proteins.

Recent studies have focused attention on the role of protein tyrosine kinases in vascular smooth muscle cell biology, but similar information regarding protein tyrosine phosphatases (PTP) is sparse. PTP-1B is a ubiquitous nonreceptor phosphatase with uncertain function and substrates that are mostly unidentified. We used antisense oligodeoxynucleotides (ODN) against PTP-1B to investigate the ro...

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تاریخ انتشار 2002