کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10754214 | 1050351 | 2014 | 7 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
p32, a novel binding partner of Mcl-1, positively regulates mitochondrial Ca2+ uptake and apoptosis
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کلمات کلیدی
YFPY2HMcl-1GFPDMSO - DMSOp32 - P32Apoptosis - خزان یاختهایDimethyl sulfoxide - دیمتیل سولفواکسیدruthenium red - رتنیم قرمزCo-IP - شرکت-IPMitochondrial calcium uniporter - متخصص غدد لنفاوی کلسیم mitochondrialYeast two hybrid - مخمر دو مخلوطMitochondria - میتوکندریاCo-Immunoprecipitation - هم ایمن زداییyellow fluorescent protein - پروتئین فلورسنت زردgreen fluorescent protein - پروتئین فلورسنت سبزCalcium - کلسیم
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
Mcl-1 is a major anti-apoptotic Bcl-2 family protein. It is well known that Mcl-1 can interact with certain pro-apoptotic Bcl-2 family proteins in normal cells to neutralize their pro-apoptotic functions, thus prevent apoptosis. In addition, it was recently found that Mcl-1 can also inhibit mitochondrial calcium uptake. The detailed mechanism, however, is still not clear. Based on Yeast Two-Hybrid screening and co-immunoprecipitation, we identified a mitochondrial protein p32 (C1qbp) as a novel binding partner of Mcl-1. We found that p32 had a number of interesting properties: (1) p32 can positively regulate UV-induced apoptosis in HeLa cells. (2) Over-expressing p32 could significantly promote mitochondrial calcium uptake, while silencing p32 by siRNA suppressed it. (3) In p32 knockdown cells, Ruthenium Red treatment (an inhibitor of mitochondrial calcium uniporter) showed no further suppressive effect on mitochondrial calcium uptake. In addition, in Ruthenium Red treated cells, Mcl-1 also failed to suppress mitochondrial calcium uptake. Taken together, our findings suggest that p32 is part of the putative mitochondrial uniporter that facilitates mitochondrial calcium uptake. By binding to p32, Mcl-1 can interfere with the uniporter function, thus inhibit the mitochondrial Ca2+ uploading. This may provide a novel mechanism to explain the anti-apoptotic function of Mcl-1.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 451, Issue 2, 22 August 2014, Pages 322-328
Journal: Biochemical and Biophysical Research Communications - Volume 451, Issue 2, 22 August 2014, Pages 322-328
نویسندگان
Kang Xiao, Yinyin Wang, Zhijie Chang, Yuanzhi Lao, Donald C. Chang,