کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1912102 | 1046863 | 2006 | 10 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Specific protein interaction of human Pag with Omi/HtrA2 and the activation of the protease activity of Omi/HtrA2
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کلمات کلیدی
Omi/HtrA2PRXPAGTSAOMIIPTGDTTROS - ROSTPx - TPXsodium dodecyl sulfate-polyacrylamide gel electrophoresis - الکتروفورز ژل دوده سولفات سدیم پلی آکریل آمیدSDS-PAGE - الکتروفورز ژل پلی آکریل آمیدProtein interaction - تعامل پروتئینOxidative stress - تنش اکسیداتیوPDZ domain - دامنه PDZdithiothreitol - دیتیوتریتولMolecular switch - سوئیچ مولکولیProtease activity - فعالیت پروتئازCell death - مرگ سلولی polymerase chain reaction - واکنش زنجیره ای پلیمرازPCR - واکنش زنجیرهٔ پلیمرازPeroxiredoxin - پروکسی ردوکسینReactive oxygen species - گونههای فعال اکسیژن
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
سالمندی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Specific protein interaction of human Pag with Omi/HtrA2 and the activation of the protease activity of Omi/HtrA2 Specific protein interaction of human Pag with Omi/HtrA2 and the activation of the protease activity of Omi/HtrA2](/preview/png/1912102.png)
چکیده انگلیسی
The human PAG gene product (hPag), one member of the TSA/AhpC family, is overexpressed by oxidative stress, which causes apoptosis. To investigate the apoptotic signal transduction mediated by hPag, hPag-binding protein was screened using the yeast two-hybrid system. Omi/HtrA2 was identified as the hPag-binding protein. Omi/HtrA2, a potent proapoptotic factor, is released from the mitochondria into the cytoplasm as the mature form showing serine protease activity during apoptosis in response to oxidative stress. We found that hPag was able to interact with the mature form of Omi/HtrA2, not with the precursor form of Omi/HtrA2. The binding of Omi/HtrA2 to hPag was shown to involve the PDZ-binding domain in Omi/HtrA2. Also, the carboxyl-terminal domain of hPag was shown to be critical for the protein interaction. Using the yeast two-hybrid system and in vitro binding assay, the reduced form of hPag was able to interact with Omi/HtrA2. Interestingly, the protease activity given by the mature form of Omi/HtrA2 was significantly activated by the binding to hPag. Taken together, these results suggest that the specific protein interaction may participate as a molecular switch in modulating cell death in response to oxidative stress.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Free Radical Biology and Medicine - Volume 40, Issue 2, 15 January 2006, Pages 275-284
Journal: Free Radical Biology and Medicine - Volume 40, Issue 2, 15 January 2006, Pages 275-284
نویسندگان
Seung-Keun Hong, Mee-Kyung Cha, Il-Han Kim,