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Difference between revisions of "Gellerich 2012 Biochem J"

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{{Publication
{{Publication
|title=Gellerich FN, Gizatullina Z, Trumbeckaite S, Korzeniewski B, Gaynutdinov T, Seppet E, Vielhaber S, Heinze HJ, Striggow F (2012) Cytosolic Ca<sup>2+</sup> regulates the energisation of isolated brain mitochondria by formation of pyruvate through the malate-aspartate shuttle. Biochem J 443: 747-755.
|title=Gellerich FN, Gizatullina Z, Trumbeckaite S, Korzeniewski B, Gaynutdinov T, Seppet E, Vielhaber S, Heinze HJ, Striggow F (2012) Cytosolic Ca<sup>2+</sup> regulates the energisation of isolated brain mitochondria by formation of pyruvate through the malate-aspartate shuttle. Biochem J 443:747-55.
|info=[http://www.ncbi.nlm.nih.gov/pubmed/22295911 PMID: 22295911]
|info=[http://www.ncbi.nlm.nih.gov/pubmed/22295911 PMID: 22295911]
|authors=Gellerich FN, Gizatullina Z, Trumbeckaite S, Korzeniewski B, Gaynutdinov T, Seppet E, Vielhaber S, Heinze HJ, Striggow F
|authors=Gellerich FN, Gizatullina Z, Trumbeckaite S, Korzeniewski B, Gaynutdinov T, Seppet E, Vielhaber S, Heinze HJ, Striggow F
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|organism=Mouse
|organism=Mouse
|tissues=Nervous system
|tissues=Nervous system
|preparations=Isolated Mitochondria
|preparations=Isolated mitochondria
|enzymes=Complex III
|enzymes=Complex III
|couplingstates=OXPHOS
|couplingstates=OXPHOS
|instruments=Oxygraph-2k
|instruments=Oxygraph-2k
}}
}}

Revision as of 11:14, 24 February 2015

Publications in the MiPMap
Gellerich FN, Gizatullina Z, Trumbeckaite S, Korzeniewski B, Gaynutdinov T, Seppet E, Vielhaber S, Heinze HJ, Striggow F (2012) Cytosolic Ca2+ regulates the energisation of isolated brain mitochondria by formation of pyruvate through the malate-aspartate shuttle. Biochem J 443:747-55.

Β» PMID: 22295911

Gellerich FN, Gizatullina Z, Trumbeckaite S, Korzeniewski B, Gaynutdinov T, Seppet E, Vielhaber S, Heinze HJ, Striggow F (2012) Biochem J

Abstract: The glutamate-dependent respiration of isolated brain mitochondria (BM) is regulated by cytosolic Ca2+ (Ca2+cyt) (S0.5 = 225 Β± 22 nM) through its effects on aralar. We now also demonstrate that the a-glycerophosphate-dependent respiration is controlled by Ca2+cyt (S0.5 = 60 Β± 10 nM). At higher Ca2+cyt (< 600 nM), BM accumulate Ca2+ which enhances the rate of action of intramitochondrial dehydrogenases. The highest Ca2+-induced increments of state 3 respiration decrease with substrate in the order glutamate < a-ketoglutarate < isocitrate < a-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 lactate dehydrogenase (LDH) is linked to the malate-aspartate shuttle (MAS) with aralar as a central component. A rise of Ca2+cyt in a reconstituted system consisting of BM, cytosolic enzymes of MAS and LDH causes an up to five-fold enhancement of OXPHOS rates that is due to an increased substrate supply, acting in a manner similar to a "gas pedal". In contrast, mitochondrial Ca2+ (Ca2+mit) regulates the oxidation rates of substrates which are present within mitochondrial matrix. We postulate that Ca2+cyt is a key factor in adjusting the mitochondrial energisation to the requirements of intact neurons. β€’ Keywords: lactate dehydrogenase (LDH); malate-aspartate shuttle (MAS); mitochondrial substrate supply; aralar; pyruvate precursors; intramitochondrial dehydrogenases

β€’ O2k-Network Lab: DE_Magdeburg_Gellerich FN


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Organism: Mouse  Tissue;cell: Nervous system  Preparation: Isolated mitochondria  Enzyme: Complex III 

Coupling state: OXPHOS 

HRR: Oxygraph-2k