کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
5589593 | 1569820 | 2017 | 6 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
EZH2-mediated α-actin methylation needs lncRNA TUG1, and promotes the cortex cytoskeleton formation in VSMCs
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کلمات کلیدی
TUG1qRT-PCRlncRNAsPDGFEZH2PRC2VSMCsLong non-coding RNAs - RNA های بدون کدگذاری طولانیAngiotensin II - آنژیوتانسین دوenhancer of zeste homolog 2 - تقویت کننده یا ژنتیک همولوگ 2Ang II - دومVascular smooth muscle cells - سلول های عضلانی صاف عروقیplatelet-derived growth factor - فاکتور رشد حاصل از پلاکتquantitative real-time PCR - واکنش زنجیره ای پلیمراز واقعی در زمان واقعیpolycomb repressive complex 2 - پیچک سرکوبگر پلی کامب 2
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
ژنتیک
پیش نمایش صفحه اول مقاله

چکیده انگلیسی
Recent studies have revealed that long non-coding RNAs (lncRNAs) participate in vascular homeostasis and pathophysiological conditions development. But still very few literatures elucidate the regulatory mechanism of non-coding RNAs in this biological process. Here we identified lncRNA taurine up-regulated gene 1 (TUG1) in rat vascular smooth muscle cells (VSMCs), and got 4612 bp nucleotide sequence. The expression level of TUG1 RNA was increased in synthetic VSMCs by real-time PCR analysis. Meanwhile, the expression of enhancer of zeste homolog 2 (EZH2) (TUG1 binding protein) increased in cytoplasm of VSMCs under the same conditions. Immunofluoresce analysis displayed the colocalization of EZH2 with α-actin in cytoplasm and F-actin in cell edge ruffles. This leads us to hypothesize the existence of cytoplasmic TUG1/EZH2/α-actin complex. Using RNA pull down assay, we found that TUG1 interacted with both EZH2 and α-actin. Disruption of TUG1 abolished the interaction of EZH2 with α-actin, and accelerated depolymerization of F-actin in VSMCs. Based on EZH2 methyltransferase activity and the potential methylation sites in α-actin structure, we revealed that α-actin was lysine-methylated. Furthermore, the methylation of α-actin was inhibited by knockdown of TUG1. In conclusion, these findings partly suggested that EZH2-mediated methylation of α-actin may be dependent on TUG1, and thereby promotes cortex F-actin polymerization in synthetic VSMCs.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Gene - Volume 616, 15 June 2017, Pages 52-57
Journal: Gene - Volume 616, 15 June 2017, Pages 52-57
نویسندگان
Rong Chen, Peng Kong, Fan Zhang, Ya-Nan Shu, Xi Nie, Li-Hua Dong, Yan-Ling Lin, Xiao-Li Xie, Li-Li Zhao, Xiang-jian Zhang, Mei Han,