کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10802316 | 1055684 | 2013 | 10 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
The role of calcium in VDAC1 oligomerization and mitochondria-mediated apoptosis
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کلمات کلیدی
OligomerizationSTSRUROMMcyto cVDACVDAC1EGSPLBCa2 + - Ca2 +staurosporine - استوسوسورپینApoptosis - خزان یاختهایPlanar lipid bilayer - دو لایه لایه ای چربیruthenium red - رتنیم قرمزcytochrome c - سیتوکروم سیouter mitochondrial membrane - غشای بیرونی میتوکندریMitochondria - میتوکندریاvoltage-dependent anion channel - کانال آنیون وابسته به ولتاژ
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
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چکیده انگلیسی
The voltage-dependent anion channel (VDAC), located at the outer mitochondria membrane (OMM), mediates interactions between mitochondria and other parts of the cell by transporting anions, cations, ATP, Ca2Â +, and metabolites. Substantial evidence points to VDAC1 as being a key player in apoptosis, regulating the release of apoptogenic proteins from mitochondria, such as cytochrome c, and interacting with anti-apoptotic proteins. Recently, we demonstrated that VDAC1 oligomerization is a general mechanism common to numerous apoptogens acting via different initiating cascades and proposed that a protein-conducting channel formed within a VDAC1 homo/hetero oligomer mediates cytochrome c release. However, the molecular mechanism responsible for VDAC1 oligomerization remains unclear. Several studies have shown that mitochondrial Ca2Â + is involved in apoptosis induction and that VDAC1 possesses Ca2Â +-binding sites and mediates Ca2Â + transport across the OMM. Here, the relationship between the cellular Ca2Â + level, [Ca2Â +]i, VDAC1 oligomerization and apoptosis was studied. Decreasing [Ca2Â +]i using the cell-permeable Ca2Â + chelating reagent BAPTA-AM was found to inhibit VDAC1 oligomerization and apoptosis, while increasing [Ca2Â +]i using Ca2Â + ionophore resulted in VDAC1 oligomerization and apoptosis induction in the absence of apoptotic stimuli. Moreover, induction of apoptosis elevated [Ca2Â +]i, concomitantly with VDAC1 oligomerization. AzRu-mediated inhibition of mitochondrial Ca2Â + transport decreased VDAC1 oligomerization, suggesting that mitochondrial Ca2Â + is required for VDAC1 oligomerization. In addition, increased [Ca2Â +]i levels up-regulate VDAC1 expression. These results suggest that Ca2Â + promotes VDAC1 oligomerization via activation of a yet unknown signaling pathway or by increasing VDAC1 expression, leading to apoptosis. This article is part of a Special Issue entitled: 12th European Symposium on Calcium.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimica et Biophysica Acta (BBA) - Molecular Cell Research - Volume 1833, Issue 7, July 2013, Pages 1745-1754
Journal: Biochimica et Biophysica Acta (BBA) - Molecular Cell Research - Volume 1833, Issue 7, July 2013, Pages 1745-1754
نویسندگان
Nurit Keinan, Hadas Pahima, Danya Ben-Hail, Varda Shoshan-Barmatz,