کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8298948 | 1537049 | 2010 | 10 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
The regulation of OXPHOS by extramitochondrial calcium
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کلمات کلیدی
ICDHIF1VDACPTPα-KGDHPDHATP-Mg/Pi carrierAralarDHAPCAGEGTACytochrome-c-oxidaseα-KGPDHcIMSAOACOXα-ketoglutarate - α-کتوگلووتراتα-ketoglutarate dehydrogenase - α-کتوگلووترات دهیدروژنازAdenylate kinase - آدنیلات کینازAminooxyacetate - آمینوسیسی سکتهethylene glycol tetraacetic acid - اتیلن گلیکول تتراستیک اسیدPermeability transition pore - افت فشار نفوذ پذیریPermeability transition - انتقال نفوذپذیریCSA - ایالات مؤتلفهٔ آمریکاIsocitrate dehydrogenase - ایزوسیترات دهیدروژنازMAS - بیشترHuntington's disease - بیماری هانتینگتونdihydroxyacetone phosphate - دی هیدروکسی استون فسفاتGPS - سامانه موقعیتیاب جهانیcyclosporin A - سیکلوسپورین AMalate–aspartate shuttle - شاتل مالتا-آسپارتاتOxidative phosphorylation - فسفوریلاسیون اکسیداتیوintermembrane space - فضای بین محوریRegulation - مقرراتwild type - نوع وحشیinhibitor protein - پروتئین مهار کنندهPorin - پوریpyruvate dehydrogenase - پیرووات دهیدروژنازpyruvate dehydrogenase complex - پیرووات دهیدروژناز پیچیدهvoltage dependent anion channel - کانال آنیونی وابسته به ولتاژCreatine kinase - کراتین کینازglycerol-3-phosphate - گلیسرول 3-فسفات
موضوعات مرتبط
علوم زیستی و بیوفناوری
علوم کشاورزی و بیولوژیک
دانش گیاه شناسی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
Despite extensive research, the regulation of mitochondrial function is still not understood completely. Ample evidence shows that cytosolic Ca2+ has a strategic task in co-ordinating the cellular work load and the regeneration of ATP by mitochondria. Currently, the paradigmatic view is that Cacyt2+ taken up by the Ca2+ uniporter activates the matrix enzymes pyruvate dehydrogenase, α-ketoglutarate dehydrogenase and isocitrate dehydrogenase. However, we have recently found that Ca2+ regulates the glutamate-dependent state 3 respiration by the supply of glutamate to mitochondria via aralar, a mitochondrial glutamate/aspartate carrier. Since this activation is not affected by ruthenium red, glutamate transport into mitochondria is controlled exclusively by extramitochondrial Ca2+. Therefore, this discovery shows that besides intramitochondrial also extramitochondrial Ca2+ regulates oxidative phosphorylation. This new mechanism acts as a mitochondrial “gas pedal”, supplying the OXPHOS with substrate on demand. These results are in line with recent findings of Satrustegui and Palmieri showing that aralar as part of the malate-aspartate shuttle is involved in the Ca2+-dependent transport of reducing hydrogen equivalents (from NADH) into mitochondria. This review summarises results and evidence as well as hypothetical interpretations of data supporting the view that at the surface of mitochondria different regulatory Ca2+-binding sites exist and can contribute to cellular energy homeostasis. Moreover, on the basis of our own data, we propose that these surface Ca2+-binding sites may act as targets for neurotoxic proteins such as mutated huntingtin and others. The binding of these proteins to Ca2+-binding sites can impair the regulation by Ca2+, causing energetic depression and neurodegeneration.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimica et Biophysica Acta (BBA) - Bioenergetics - Volume 1797, Issues 6â7, JuneâJuly 2010, Pages 1018-1027
Journal: Biochimica et Biophysica Acta (BBA) - Bioenergetics - Volume 1797, Issues 6â7, JuneâJuly 2010, Pages 1018-1027
نویسندگان
Frank N. Gellerich, Zemfira Gizatullina, Sonata Trumbeckaite, Huu P. Nguyen, Thilo Pallas, Odeta Arandarcikaite, Stephan Vielhaber, Enn Seppet, Frank Striggow,