کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10738859 | 1046838 | 2005 | 13 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Signal transduction pathways leading to increased eIF4E phosphorylation caused by oxidative stress
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کلمات کلیدی
DPIMAP kinase kinase kinasePDK1PP2PKRphorbol 12-myristate 13-acetateRTKHCRImmunoprecipitateGCsEBSSBSOS6KTSCPI3KMBPTORFBSDMEMEGFphosphoinositide-dependent protein kinase 1eIF - EIFPMA - LDC هاbuthionine sulfoximine - بوته یون سولفسیمیمOxidative stress - تنش اکسیداتیوFree radicals - رادیکال آزادfetal bovine serum - سرم جنین گاوepidermal growth factor - عامل رشد اپیدرمیInitiation factors - عوامل آغازگرEukaryotic Initiation Factor - عوامل آغازگر یوکاریوتیPhosphatidylinositol 3-kinase - فسفاتیدیلینواستیل 3-کینازPhosphorylation - فسفریلاسیونDulbecco's Modified Essential Medium - متوسط ضروری اصلاح شده DulbeccoSignal transduction - هدایت سیگنالtarget of rapamycin - هدف از رپامایسینeIF4E-binding protein - پروتئین اتصال دهنده eIF4Eribosomal protein S6 kinase - پروتئین ریبوزومی S6 کینازMyelin basic protein - پروتئین پایه میلینPERK - پرکTuberous sclerosis complex - کمپلکس توبروس اسکلروزیسReceptor Tyrosine Kinase - گیرنده تیروزین کیناز
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
سالمندی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
Phosphorylation of eIF4E is associated with increased activity of the translational machinery. Oxidative stress of resident vascular cells and macrophages potently enhances eIF4E phosphorylation. Oxidative stress activates numerous intracellular signaling pathways, including MAP-family kinase pathways and pathways leading to S6 kinase activation. The activation of MAP-family kinase pathways leads to the activation of Mnk and hence eIF4E phosphorylation, whereas the S6 kinase pathway is not involved, based on insensitivity to its inhibitors rapamycin and wortmannin. Ca-dependent pathways have been implicated in eIF4E phosphorylation, but the oxidative stress response pathway targeting eIF4E does not appear to require their participation. The results suggest that the potent activation of ERK and p38 protein kinases is sufficient to account for the enhanced eIF4E phosphorylation. Either is independently sufficient to effect the change, as neither PD098059 (Erk pathway inhibitor) nor SB202190 (p38 pathway inhibitor) alone can block the response, but when combined the response is almost completely abrogated. Mnk activation by oxidative stress leading to enhanced eIF4E phosphorylation may play a role in promoting stress-induced hyperproliferative diseases, such as smooth muscle cell proliferation and hypertrophy in cardiovascular disease, as the synthesis of several key regulators of cell growth has been shown to be held in check by moderation of eIF4E activity.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Free Radical Biology and Medicine - Volume 38, Issue 5, 1 March 2005, Pages 631-643
Journal: Free Radical Biology and Medicine - Volume 38, Issue 5, 1 March 2005, Pages 631-643
نویسندگان
Roger F. Duncan, Hazel Peterson, Alex Sevanian,