کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10817015 | 1058623 | 2008 | 9 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
ATM protein kinase mediates full activation of Akt and regulates glucose transporter 4 translocation by insulin in muscle cells
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کلمات کلیدی
Ataxia-telangiectasiaQUICKIGFPGLUT4A-TIRS-1PI 3-kinase - PI 3-کینازAkt - آکتGlucose uptake - جذب گلوکزglucose transporter 4 - حمل کننده گلوکز 4ATM - خودپردازinsulin receptor substrate 1 - زیر بغل گیرنده انسولین 1Insulin signaling - سیگنالینگ انسولینquantitative insulin sensitivity check index - شاخص کنترل حساسیت به انسولین کمیMuscle - عضلهPhosphotidylinositol 3-kinase - فسفودیدیلینواستیل 3-کینازInsulin resistance - مقاومت به انسولینwild type - نوع وحشیGreen fluorescence protein - پروتئین فلورسانس سبزkinase dead - کیناز مرده استinsulin receptor - گیرنده انسولین
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: ATM protein kinase mediates full activation of Akt and regulates glucose transporter 4 translocation by insulin in muscle cells ATM protein kinase mediates full activation of Akt and regulates glucose transporter 4 translocation by insulin in muscle cells](/preview/png/10817015.png)
چکیده انگلیسی
Ataxia-telangiectasia (A-T) is an autosomal recessive disorder characterized by cerebellar ataxia and oculocutaneous telangiectasias. Patients with A-T also have high incidences of type 2 diabetes mellitus. The gene mutated in this disease, ATM (A-T, mutated), encodes a protein kinase. Previous studies have demonstrated that cytoplasmic ATM is an insulin-responsive protein and a major upstream activator of Akt following insulin treatment. To further investigate the function of ATM in insulin signal transduction, insulin resistance was induced in rats by feeding them a high-fat diet. Muscle tissue of rats with insulin resistance had both dramatically reduced ATM levels and substantially decreased Akt phosphorylation at Ser473 in comparison to that of regular chow-fed controls. The decreased ATM expression suggests that ATM is involved in the development of insulin resistance through down-regulation of Akt activity. The role of ATM in activation of Akt was further confirmed in mouse embryonic fibroblast (MEF) A29 (ATM+/+) and A38 (ATMâ/â) cells. In addition, insulin-mediated Akt phosphorylation in mouse L6 muscle cells was greatly reduced by KU-55933, a specific inhibitor of ATM. A 2-deoxyglucose incorporation assay showed that this inhibitor also caused a significant reduction in insulin-mediated glucose uptake in L6 cells. An immunofluorescence experiment demonstrated that in L6 cells transfected with wild-type (WT) ATM, insulin caused a dramatic increase of the cell surface glucose transporter 4 (GLUT4), while in cells transfected with kinase-dead (KD) ATM, translocation of GLUT4 to the cell surface in response to insulin was markedly inhibited.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Cellular Signalling - Volume 20, Issue 8, August 2008, Pages 1555-1563
Journal: Cellular Signalling - Volume 20, Issue 8, August 2008, Pages 1555-1563
نویسندگان
Marie-Jo Halaby, Jody C. Hibma, Jinghua He, Da-Qing Yang,