کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
5501062 | 1534621 | 2017 | 51 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Heat shock protein 22 (HSPB8) reduces the migration of hepatocellular carcinoma cells through the suppression of the phosphoinositide 3-kinase (PI3K)/AKT pathway
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کلمات کلیدی
EGFRHGFTGFPI3KDABSDSHspROCDAPIERK4′,6′-diamidino-2-phenylindole - 4 '، 6'-diamidino-2-phenylindoleHCC - HCCSmall interfering RNA - RNA تداخل کوچکsiRNA - siRNAAkt - آکتtransforming growth factor - تبدیل فاکتور رشدsodium dodecyl sulfate - سدیم دودسیل سولفاتHepatocyte growth factor - عامل رشد هپاتوسیتGrowth factor - فاکتور رشدphosphoinositide 3-kinase - فسفینوزیتید 3-کینازMigration - مهاجرتHeat shock protein - پروتئین شوک حرارتHepatocellular carcinoma - کارسینوم هپاتوسلولار(کارسینوم سلولهای استخوانی)extracellular signal-regulated kinase - کیناز تنظیم شده سیگنال خارج سلولیreceiver operating characteristic - گیرنده عامل عاملEpidermal growth factor receptor - گیرنده فاکتور رشد اپیدرمال
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
سالمندی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
Small heat shock proteins (HSPs) regulate a variety of cell functions. Among them, HSP22 and HSP20 are recognized to be ubiquitously expressed in various tissues. With regard to hepatocellular carcinoma (HCC) cells, we previously reported that phosphorylated HSP20 plays a suppressive role in transforming growth factor (TGF)-α-induced cell migration and invasion. In the present study, we investigated whether or not HSP22 is implicated in HCC cell migration. We detected HSP22 protein expression both in human HCC tumor (189.9 ± 68.4 ng/mg protein) and the adjacent non-tumor liver tissues (167.9 ± 94.6 ng/mg protein). The cases of low-quantity HSP22 protein level group (88.3 â§Â ng/mg protein, the optimum cut-off value of HSP22) were increased in tumor tissues compared with the adjacent non-tumor tissues. The migration of human HCC-derived HuH-7 cells stimulated by TGF-α or hepatocyte growth factor (HGF) was significantly enhanced by the knockdown of HSP22 expression. Down-regulation of HSP22 protein in the cells markedly strengthened the AKT phosphorylation induced by TGF-α or HGF. Inhibitors of the phosphoinositide 3-kinase (PI3K)/AKT pathway, which suppressed the TGF-α-induced migration, significantly reduced the amplification by HSP22 knockdown. PI3K but not AKT was coimmunoprecipitated with HSP22 in HuH-7 cells. In addition, in human HCC tissues, a significantly lower HSP22 protein level in tumor tissues than in adjacent non-tumor tissues was observed more frequently in cases of moderately or poorly differentiated HCC than well-differentiated HCC. Taken together, our results strongly suggest that HSP22 represses HCC progression, especially HCC cell migration, by the down-regulation of the PI3K/AKT signaling pathway.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease - Volume 1863, Issue 6, June 2017, Pages 1629-1639
Journal: Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease - Volume 1863, Issue 6, June 2017, Pages 1629-1639
نویسندگان
Rie Matsushima-Nishiwaki, Hidenori Toyoda, Reika Takamatsu, Eisuke Yasuda, Seiji Okuda, Atsuyuki Maeda, Yuji Kaneoka, Naoki Yoshimi, Takashi Kumada, Osamu Kozawa,