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000136514 0247_ $$2ISSN$$a1470-8728
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000136514 1001_ $$0P:(DE-HGF)0$$aGellerich, Frank Norbert$$b0$$eCorresponding author
000136514 245__ $$aCytosolic Ca2+ regulates the energization of isolated brain mitochondria by formation of pyruvate through the malate-aspartate shuttle.
000136514 260__ $$aLondon$$bPortland Press67261$$c2012
000136514 264_1 $$2Crossref$$3online$$bPortland Press Ltd.$$c2012-04-16
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000136514 520__ $$aThe glutamate-dependent respiration of isolated BM (brain mitochondria) is regulated by Ca2+(cyt) (cytosolic Ca2+) (S0.5=225±22 nM) through its effects on aralar. We now also demonstrate that the α-glycerophosphate-dependent respiration is controlled by Ca2+(cyt) (S0.5=60±10 nM). At higher Ca2+(cyt) (>600 nM), BM accumulate Ca2+ which enhances the rate of intramitochondrial dehydrogenases. The Ca2+-induced increments of state 3 respiration decrease with substrate in the order glutamate>α-oxoglutarate>isocitrate>α-glycerophosphate>pyruvate. Whereas the oxidation of pyruvate is only slightly influenced by Ca2+(cyt), we show that the formation of pyruvate is tightly controlled by Ca2+(cyt). Through its common substrate couple NADH/NAD+, the formation of pyruvate by LDH (lactate dehydrogenase) is linked to the MAS (malate-aspartate shuttle) with aralar as a central component. A rise in Ca2+(cyt) in a reconstituted system consisting of BM, cytosolic enzymes of MAS and LDH causes an up to 5-fold enhancement of OXPHOS (oxidative phosphorylation) rates that is due to an increased substrate supply, acting in a manner similar to a 'gas pedal'. In contrast, Ca2+(mit) (intramitochondrial Ca2+) regulates the oxidation rates of substrates which are present within the mitochondrial matrix. We postulate that Ca2+(cyt) is a key factor in adjusting the mitochondrial energization to the requirements of intact neurons.
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000136514 650_7 $$2NLM Chemicals$$aMalates
000136514 650_7 $$030KYC7MIAI$$2NLM Chemicals$$aAspartic Acid
000136514 650_7 $$0817L1N4CKP$$2NLM Chemicals$$amalic acid
000136514 650_7 $$08558G7RUTR$$2NLM Chemicals$$aPyruvic Acid
000136514 650_7 $$0SY7Q814VUP$$2NLM Chemicals$$aCalcium
000136514 650_2 $$2MeSH$$aAnimals
000136514 650_2 $$2MeSH$$aAspartic Acid: metabolism
000136514 650_2 $$2MeSH$$aBrain: metabolism
000136514 650_2 $$2MeSH$$aCalcium: metabolism
000136514 650_2 $$2MeSH$$aCytosol: metabolism
000136514 650_2 $$2MeSH$$aKinetics
000136514 650_2 $$2MeSH$$aMalates: metabolism
000136514 650_2 $$2MeSH$$aMice
000136514 650_2 $$2MeSH$$aMitochondria: metabolism
000136514 650_2 $$2MeSH$$aOxidative Phosphorylation
000136514 650_2 $$2MeSH$$aPyruvic Acid: metabolism
000136514 7001_ $$aGizatullina, Zemfira$$b1
000136514 7001_ $$aTrumbekaite, Sonata$$b2
000136514 7001_ $$aKorzeniewski, Bernard$$b3
000136514 7001_ $$aGaynutdinov, Timur$$b4
000136514 7001_ $$aSeppet, Enn$$b5
000136514 7001_ $$0P:(DE-2719)2000035$$aVielhaber, Stefan$$b6$$udzne
000136514 7001_ $$0P:(DE-2719)2260426$$aHeinze, Hans-Jochen$$b7$$udzne
000136514 7001_ $$0P:(DE-2719)9000420$$aStriggow, Frank$$b8$$eLast author$$udzne
000136514 77318 $$2Crossref$$3journal-article$$a10.1042/bj20110765$$b : Portland Press Ltd., 2012-04-16$$n3$$p747-755$$tBiochemical Journal$$v443$$x0264-6021$$y2012
000136514 773__ $$0PERI:(DE-600)1473095-9$$a10.1042/BJ20110765$$gVol. 443, no. 3, p. 747 - 755$$n3$$p747-755$$q443:3<747 - 755$$tBiochemical journal$$v443$$x0264-6021$$y2012
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