کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8323866 | 1539900 | 2013 | 12 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Regulation of Akt-mTOR, ubiquitin-proteasome and autophagy-lysosome pathways in response to formoterol administration in rat skeletal muscle
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کلمات کلیدی
HprtFOXO3EpacIRS-1BNIP3CREBEDLGastrocnemiusATGIGF-1LC3BMuRF1sequestosome 1ERKmTORMuscle RING finger-1GABARAPL1MEF2BSA - BSAp62/SQSTM1 - P62 / SQSTM1bovine serum albumin - آلبومین سرم گاوactin beta - آکتین بتاinsulin receptor substrate-1 - انسولین گیرنده زیربخش 1extensor digitorum longus - اکستانسور بلند شست انگشتانChronic obstructive pulmonary disease - بیماری مزمن انسدادی ریهCOPD - بیماری مزمن انسدادی ریهforkhead box O3 - جعبه O3 جعبهInsulin growth factor-1 - عامل رشد انسولین- 1Actb - عملmyocyte enhancer factor 2 - فاکتور افزایش دهنده myocyte 2phosphatidylethanolamine - فسفاتیدیلتانولامینautophagy-related - مرتبط با autophagymammalian target of rapamycin - هدف پستانداران رپامایسینhypoxanthine guanine phosphoribosyl transferase - هیپوکسانتین گوانین فسفریبوسیل ترانسفرازcAMP response element binding protein - پروتئین اتصال دهنده عنصر پاسخ cAMPextracellular signal-regulated kinase - کیناز تنظیم شده سیگنال خارج سلولیGas - گاز
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
Administration of β2-agonists triggers skeletal muscle anabolism and hypertrophy. We investigated the time course of the molecular events responsible for rat skeletal muscle hypertrophy in response to 1, 3 and 10 days of formoterol administration (i.p. 2000 μg/kg/day). A marked hypertrophy of rat tibialis anterior muscle culminated at day 10. Phosphorylation of Akt, ribosomal protein S6, 4E-BP1 and ERK1/2 was increased at day 3, but returned to control level at day 10. This could lead to a transient increase in protein translation and could explain previous studies that reported increase in protein synthesis following β2-agonist administration. Formoterol administration was also associated with a significant reduction in MAFbx/atrogin-1 mRNA level (day 3), suggesting that formoterol can also affect protein degradation of MAFbx/atrogin1 targeted substrates, including MyoD and eukaryotic initiation factor-3f (eIF3-f). Surprisingly, mRNA level of autophagy-related genes, light chain 3 beta (LC3b) and gamma-aminobutyric acid receptor-associated protein-like 1 (Gabarapl1), as well as lysosomal hydrolases, cathepsin B and cathepsin L, was significantly and transiently increased after 1 and/or 3 days, suggesting that autophagosome formation would be increased in response to formoterol administration. However, this has to be relativized since the mRNA level of Unc-51-like kinase1 (Ulk1), BCL2/adenovirus E1B interacting protein3 (Bnip3), and transcription factor EB (TFEB), as well as the protein content of Ulk1, Atg13, Atg5-Atg12 complex and p62/Sqstm1 remained unchanged or was even decreased in response to formoterol administration. These results demonstrate that the effects of formoterol are mediated, in part, through the activation of Akt-mTOR pathway and that other signaling pathways become more important in the regulation of skeletal muscle mass with chronic administration of β2-agonists.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: The International Journal of Biochemistry & Cell Biology - Volume 45, Issue 11, November 2013, Pages 2444-2455
Journal: The International Journal of Biochemistry & Cell Biology - Volume 45, Issue 11, November 2013, Pages 2444-2455
نویسندگان
Olivier Roger Joassard, Adel Amirouche, Yann Simon Gallot, Marine Maud Desgeorges, Josiane Castells, Anne-Cécile Durieux, Phanélie Berthon, Damien Gilles Freyssenet,