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| Home > Publications Database > Cytosolic Ca2+ regulates the energization of isolated brain mitochondria by formation of pyruvate through the malate-aspartate shuttle. > print |
| 001 | 136514 | ||
| 005 | 20240321220101.0 | ||
| 024 | 7 | _ | |a 10.1042/BJ20110765 |2 doi |
| 024 | 7 | _ | |a pmid:22295911 |2 pmid |
| 024 | 7 | _ | |a 0006-2936 |2 ISSN |
| 024 | 7 | _ | |a 0264-6021 |2 ISSN |
| 024 | 7 | _ | |a 0306-3275 |2 ISSN |
| 024 | 7 | _ | |a 0306-3283 |2 ISSN |
| 024 | 7 | _ | |a 1470-8728 |2 ISSN |
| 037 | _ | _ | |a DZNE-2020-02836 |
| 041 | _ | _ | |a English |
| 082 | _ | _ | |a 540 |
| 100 | 1 | _ | |a Gellerich, Frank Norbert |0 P:(DE-HGF)0 |b 0 |e Corresponding author |
| 245 | _ | _ | |a Cytosolic Ca2+ regulates the energization of isolated brain mitochondria by formation of pyruvate through the malate-aspartate shuttle. |
| 260 | _ | _ | |a London |c 2012 |b Portland Press67261 |
| 264 | _ | 1 | |3 online |2 Crossref |b Portland Press Ltd. |c 2012-04-16 |
| 264 | _ | 1 | |3 print |2 Crossref |b Portland Press Ltd. |c 2012-05-01 |
| 336 | 7 | _ | |a article |2 DRIVER |
| 336 | 7 | _ | |a Output Types/Journal article |2 DataCite |
| 336 | 7 | _ | |a Journal Article |b journal |m journal |0 PUB:(DE-HGF)16 |s 1709648813_29109 |2 PUB:(DE-HGF) |
| 336 | 7 | _ | |a ARTICLE |2 BibTeX |
| 336 | 7 | _ | |a JOURNAL_ARTICLE |2 ORCID |
| 336 | 7 | _ | |a Journal Article |0 0 |2 EndNote |
| 520 | _ | _ | |a The 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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| 536 | _ | _ | |a 344 - Clinical and Health Care Research (POF3-344) |0 G:(DE-HGF)POF3-344 |c POF3-344 |f POF III |x 1 |
| 588 | _ | _ | |a Dataset connected to CrossRef, PubMed, |
| 650 | _ | 7 | |a Malates |2 NLM Chemicals |
| 650 | _ | 7 | |a Aspartic Acid |0 30KYC7MIAI |2 NLM Chemicals |
| 650 | _ | 7 | |a malic acid |0 817L1N4CKP |2 NLM Chemicals |
| 650 | _ | 7 | |a Pyruvic Acid |0 8558G7RUTR |2 NLM Chemicals |
| 650 | _ | 7 | |a Calcium |0 SY7Q814VUP |2 NLM Chemicals |
| 650 | _ | 2 | |a Animals |2 MeSH |
| 650 | _ | 2 | |a Aspartic Acid: metabolism |2 MeSH |
| 650 | _ | 2 | |a Brain: metabolism |2 MeSH |
| 650 | _ | 2 | |a Calcium: metabolism |2 MeSH |
| 650 | _ | 2 | |a Cytosol: metabolism |2 MeSH |
| 650 | _ | 2 | |a Kinetics |2 MeSH |
| 650 | _ | 2 | |a Malates: metabolism |2 MeSH |
| 650 | _ | 2 | |a Mice |2 MeSH |
| 650 | _ | 2 | |a Mitochondria: metabolism |2 MeSH |
| 650 | _ | 2 | |a Oxidative Phosphorylation |2 MeSH |
| 650 | _ | 2 | |a Pyruvic Acid: metabolism |2 MeSH |
| 700 | 1 | _ | |a Gizatullina, Zemfira |b 1 |
| 700 | 1 | _ | |a Trumbekaite, Sonata |b 2 |
| 700 | 1 | _ | |a Korzeniewski, Bernard |b 3 |
| 700 | 1 | _ | |a Gaynutdinov, Timur |b 4 |
| 700 | 1 | _ | |a Seppet, Enn |b 5 |
| 700 | 1 | _ | |a Vielhaber, Stefan |0 P:(DE-2719)2000035 |b 6 |u dzne |
| 700 | 1 | _ | |a Heinze, Hans-Jochen |0 P:(DE-2719)2260426 |b 7 |u dzne |
| 700 | 1 | _ | |a Striggow, Frank |0 P:(DE-2719)9000420 |b 8 |e Last author |u dzne |
| 773 | 1 | 8 | |a 10.1042/bj20110765 |b : Portland Press Ltd., 2012-04-16 |n 3 |p 747-755 |3 journal-article |2 Crossref |t Biochemical Journal |v 443 |y 2012 |x 0264-6021 |
| 773 | _ | _ | |a 10.1042/BJ20110765 |g Vol. 443, no. 3, p. 747 - 755 |0 PERI:(DE-600)1473095-9 |n 3 |q 443:3<747 - 755 |p 747-755 |t Biochemical journal |v 443 |y 2012 |x 0264-6021 |
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