کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10795249 | 1052563 | 2016 | 31 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Differential susceptibility of mitochondrial complex II to inhibition by oxaloacetate in brain and heart
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کلمات کلیدی
DDM2,3-dimethoxy-5-methyl-6-(3-methyl-2-butenyl)-1,4-benzoquinoneflavin adenine dinucleotideGOT1SDHTCAHexaamminerutheniumMitochondrial complex IIOxaloacetateOAAI/R - I / Rn-dodecyl β-d-maltoside - n-dodecyl β-d-مالتوزیدA/D - آگهیreverse electron transfer - انتقال الکترون معکوس استActive/de-active transition - انتقال فعال / غیرفعالHAR - اندIschemia - ایسکمیischemia/reperfusion - ایسکمی / رپرفیوژنFAD - بدRET - حقSMP - دانشکده دبیرستانSubmitochondrial particles - ذرات ریزsuccinate dehydrogenase - سوکسیناد دهیدروژنازKrebs cycle - چرخه Krebstricarboxylic acid cycle - چرخه اسید تریکاربوکیلیک
موضوعات مرتبط
علوم زیستی و بیوفناوری
علوم کشاورزی و بیولوژیک
دانش گیاه شناسی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Differential susceptibility of mitochondrial complex II to inhibition by oxaloacetate in brain and heart Differential susceptibility of mitochondrial complex II to inhibition by oxaloacetate in brain and heart](/preview/png/10795249.png)
چکیده انگلیسی
Mitochondrial Complex II is a key mitochondrial enzyme connecting the tricarboxylic acid (TCA) cycle and the electron transport chain. Studies of complex II are clinically important since new roles for this enzyme have recently emerged in cell signalling, cancer biology, immune response and neurodegeneration. Oxaloacetate (OAA) is an intermediate of the TCA cycle and at the same time is an inhibitor of complex II with high affinity (Kd ~ 10â 8 M). Whether or not OAA inhibition of complex II is a physiologically relevant process is a significant, but still controversial topic. We found that complex II from mouse heart and brain tissue has similar affinity to OAA and that only a fraction of the enzyme in isolated mitochondrial membranes (30.2 ± 6.0% and 56.4 ± 5.6% in the heart and brain, respectively) is in the free, active form. Since OAA could bind to complex II during isolation, we established a novel approach to deplete OAA in the homogenates at the early stages of isolation. In heart, this treatment significantly increased the fraction of free enzyme, indicating that OAA binds to complex II during isolation. In brain the OAA-depleting system did not significantly change the amount of free enzyme, indicating that a large fraction of complex II is already in the OAA-bound inactive form. Furthermore, short-term ischemia resulted in a dramatic decline of OAA in tissues, but it did not change the amount of free complex II. Our data show that in brain OAA is an endogenous effector of complex II, potentially capable of modulating the activity of the enzyme.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimica et Biophysica Acta (BBA) - Bioenergetics - Volume 1857, Issue 9, September 2016, Pages 1561-1568
Journal: Biochimica et Biophysica Acta (BBA) - Bioenergetics - Volume 1857, Issue 9, September 2016, Pages 1561-1568
نویسندگان
Anna Stepanova, Yevgeniya Shurubor, Federica Valsecchi, Giovanni Manfredi, Alexander Galkin,