% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@ARTICLE{Gellerich:136514,
      author       = {Gellerich, Frank Norbert and Gizatullina, Zemfira and
                      Trumbekaite, Sonata and Korzeniewski, Bernard and
                      Gaynutdinov, Timur and Seppet, Enn and Vielhaber, Stefan and
                      Heinze, Hans-Jochen and Striggow, Frank},
      title        = {{C}ytosolic {C}a2+ regulates the energization of isolated
                      brain mitochondria by formation of pyruvate through the
                      malate-aspartate shuttle.},
      journal      = {Biochemical journal},
      volume       = {443},
      number       = {3},
      issn         = {0264-6021},
      address      = {London},
      publisher    = {Portland Press67261},
      reportid     = {DZNE-2020-02836},
      pages        = {747-755},
      year         = {2012},
      abstract     = {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.},
      keywords     = {Animals / Aspartic Acid: metabolism / Brain: metabolism /
                      Calcium: metabolism / Cytosol: metabolism / Kinetics /
                      Malates: metabolism / Mice / Mitochondria: metabolism /
                      Oxidative Phosphorylation / Pyruvic Acid: metabolism /
                      Malates (NLM Chemicals) / Aspartic Acid (NLM Chemicals) /
                      malic acid (NLM Chemicals) / Pyruvic Acid (NLM Chemicals) /
                      Calcium (NLM Chemicals)},
      cin          = {AG Düzel / U Clinical Researchers - Magdeburg / AG
                      Striggow},
      ddc          = {540},
      cid          = {I:(DE-2719)5000006 / I:(DE-2719)7000000 /
                      I:(DE-2719)5000045},
      pnm          = {342 - Disease Mechanisms and Model Systems (POF3-342) / 344
                      - Clinical and Health Care Research (POF3-344)},
      pid          = {G:(DE-HGF)POF3-342 / G:(DE-HGF)POF3-344},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:22295911},
      doi          = {10.1042/BJ20110765},
      url          = {https://pub.dzne.de/record/136514},
}