کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1251159 | 970890 | 2007 | 4 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Cyclin A-Cdk2 Phosphorylates BH3 only Protein Bad in vitro and in vivo
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موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی (عمومی)
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
Increasing evidence suggests that Cyclin A-Cdk2 activity is required in the apoptosis process induced by various stimuli. To determine a specific substrate of Cyclin A-Cdk2 for apoptosis, in this study, we carried out an in vitro kinase assay using immunoprecipitated complex Cyclin A-Cdk2 as an enzyme source, and recombinant protein GST-Bad as a substrate. Our study showed that Bad was clearly phosphorylated by Cyclin A-Cdk2 in vitro. To examine whether protein Bad can also be phosphorylated by Cyclin A-Cdk2 kinase in vivo, we transiently overexpressed protein Bad with Cyclin A or Cdk2-dn, a dominant negative version of Cdk2, in Hela cells and determined the phosphorylation status of protein Bad. The test showed that protein Bad was clearly phosphorylated in Cyclin A overexpressed cells, but not in Cdk2-dn or mock transfectent. Moreover, etoposide also caused the phosphorylation of endogenetic Bad. In conclusion, here we provide first time evidence that protein Bad can be a substrate of Cyclin A-Cdk2 apoptosis for in vitro and in vivo.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Chemical Research in Chinese Universities - Volume 23, Issue 5, September 2007, Pages 567-570
Journal: Chemical Research in Chinese Universities - Volume 23, Issue 5, September 2007, Pages 567-570
نویسندگان
Kan HE, Yue CHEN, Jing-hua LI, Zhuo ZHAN, Yong-ge WU, Wei KONG, Ying-hua JIN,