کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10904064 | 1086556 | 2014 | 9 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
PPARγ1 phosphorylation enhances proliferation and drug resistance in human fibrosarcoma cells
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کلمات کلیدی
PCNACDKRSG5-FUCKIPTMFACSPPARγ3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide - 3- (4،5-dimethylthiazol-2-yl) -2،5-difenyltetrazolium bromideMTT - MTTProliferating Cell Nuclear Antigen - آنتیژن هسته ای تکثیر سلولیPPRE - ارسالpost-translational modifications - تغییرات پس از ترجمه، پیرایش پساترجمهCell proliferation - تکثیر سلولیfluorescence-activated cell sorting - دسته بندی سلول های فعال فلورسنسrosiglitazone - روزیگلیتازون5-fluorouracil - فلوروراسیل-۵، فلوئورواوراسیلDrug resistance - مقاومت داروییcyclin-dependent kinase inhibitor - مهار کننده کیناز وابسته به سیکلینPropidium iodide - پروتئین یدیدCell cycle - چرخه سلولیcyclin-dependent kinase - کییناز وابسته به سیکلینperoxisome proliferator-activated receptor γ - گیرنده پروتئین کننده پروکسیوم فعال γ
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
تحقیقات سرطان
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
Post-translational regulation plays a critical role in the control of cell growth and proliferation. The phosphorylation of peroxisome proliferator-activated receptor γ (PPARγ) is the most important post-translational modification. The function of PPARγ phosphorylation has been studied extensively in the past. However, the relationship between phosphorylated PPARγ1 and tumors remains unclear. Here we investigated the role of PPARγ1 phosphorylation in human fibrosarcoma HT1080 cell line. Using the nonphosphorylation (Ser84 to alanine, S84A) and phosphorylation (Ser84 to aspartic acid, S84D) mutant of PPARγ1, the results suggested that phosphorylation attenuated PPARγ1 transcriptional activity. Meanwhile, we demonstrated that phosphorylated PPARγ1 promoted HT1080 cell proliferation and this effect was dependent on the regulation of cell cycle arrest. The mRNA levels of cyclin-dependent kinase inhibitor (CKI) p21Waf1/Cip1 and p27Kip1 descended in PPARγ1S84D stable HT1080 cell, whereas the expression of p18INK4C was not changed. Moreover, compared to the PPARγ1S84A, PPARγ1S84D up-regulated the expression levels of cyclin D1 and cyclin A. Finally, PPARγ1 phosphorylation reduced sensitivity to agonist rosiglitazone and increased resistance to anticancer drug 5-fluorouracil (5-FU) in HT1080 cell. Our findings establish PPARγ1 phosphorylation as a critical event in human fibrosarcoma growth. These findings raise the possibility that chemical compounds that prevent the phosphorylation of PPARγ1 could act as anticancer drugs.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Experimental Cell Research - Volume 322, Issue 1, 10 March 2014, Pages 30-38
Journal: Experimental Cell Research - Volume 322, Issue 1, 10 March 2014, Pages 30-38
نویسندگان
Xiaojuan Pang, Yuxin Shu, Zhiyuan Niu, Wei Zheng, Haochen Wu, Yan Lu, Pingping Shen,