کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10804410 | 1057265 | 2005 | 11 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Positive and negative regulation of insulin signaling through IRS-1 phosphorylation
دانلود مقاله + سفارش ترجمه
دانلود مقاله ISI انگلیسی
رایگان برای ایرانیان
کلمات کلیدی
Inhibitor kappa B kinasemTORERKIRSIKKPKBPTBaPKCIRS1APs - AP هاPI 3-kinase - PI 3-کینازphosphotyrosine binding - اتصال فسفاتیروسینinsulin receptor substrate - انسولین بستر گیرندهSerine phosphorylation - فسفریلاسیون سریالphosphoinositide 3-kinase - فسفینوزیتید 3-کینازInsulin resistance - مقاومت به انسولینmammalian target of rapamycin - هدف پستانداران رپامایسینatypical protein kinase C - پروتئین نایاکی کیناز Cprotein kinase B - پروتئین کیناز BCaP - کلاه لبه دارextracellular signal-regulated kinase - کیناز تنظیم شده سیگنال خارج سلولیKinases - کینازهاGab1 - گاو 1
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
This review will provide insight on the current understanding of the regulation of insulin signaling in both physiological and pathological conditions through modulations that occur with regards to the functions of the insulin receptor substrate 1 (IRS1). While the phosphorylation of IRS1 on tyrosine residue is required for insulin-stimulated responses, the phosphorylation of IRS1 on serine residues has a dual role, either to enhance or to terminate the insulin effects. The activation of PKB in response to insulin propagates insulin signaling and promotes the phosphorylation of IRS1 on serine residue in turn generating a positive-feedback loop for insulin action. Insulin also activates several kinases and these kinases act to induce the phosphorylation of IRS1 on specific sites and inhibit its functions. This is part of the negative-feedback control mechanism induced by insulin that leads to termination of its action. Agents such as free fatty acids, cytokines, angiotensin II, endothelin-1, amino acids, cellular stress and hyperinsulinemia, which induce insulin resistance, lead to both activation of several serine/threonine kinases and phosphorylation of IRS1. These agents negatively regulate the IRS1 functions by phosphorylation but also via others molecular mechanisms (SOCS expression, IRS degradation, O-linked glycosylation) as summarized in this review. Understanding how these agents inhibit IRS1 functions as well as identification of kinases involved in these inhibitory effects may provide novel targets for development of strategies to prevent insulin resistance.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimie - Volume 87, Issue 1, January 2005, Pages 99-109
Journal: Biochimie - Volume 87, Issue 1, January 2005, Pages 99-109
نویسندگان
Philippe Gual, Yannick Le Marchand-Brustel, Jean-François Tanti,