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Transport and metabolism of L-lactate occur in mitochondria from cerebellar granule cells and are modified in cells undergoing low potassium dependent apoptosis (Articolo in rivista)
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- Label
- Transport and metabolism of L-lactate occur in mitochondria from cerebellar granule cells and are modified in cells undergoing low potassium dependent apoptosis (Articolo in rivista) (literal)
- Anno
- 2007-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1016/j.bbabio.2007.08.003 (literal)
- Alternative label
Atlante A, de Bari L, Bobba A, Marra E, Passarella S, (2007)
Transport and metabolism of L-lactate occur in mitochondria from cerebellar granule cells and are modified in cells undergoing low potassium dependent apoptosis
in Biochimica et biophysica acta. Bioenergetics
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- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Atlante A, de Bari L, Bobba A, Marra E, Passarella S, (literal)
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- impact factor BBA-Bioenergetics anno 2007 : 3.835 (literal)
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- ISI Web of Science (WOS) (literal)
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- Istituto di Biomembrane e Bioenergetica, CNR Bari
Dipartimento di Scienze della Salute, Università del Molise, Campobasso. (literal)
- Titolo
- Transport and metabolism of L-lactate occur in mitochondria from cerebellar granule cells and are modified in cells undergoing low potassium dependent apoptosis (literal)
- Abstract
- Having confirmed that externally added L-lactate can enter cerebellar granule cells, we investigated whether and how L-lactate is metabolized
by mitochondria from these cells under normal or apoptotic conditions.
(1) L-lactate enters mitochondria, perhaps via an L-lactate/H+ symporter, and is oxidized in a manner stimulated byADP. The existence of an L-lactate
dehydrogenase, located in the innermitochondrial compartment, was shown by immunological analysis. Neither the protein level nor the Km and
Vmax values changed en route to apoptosis.
(2) In both normal and apoptotic cell homogenates, externally added L-lactate caused reduction of the intramitochondrial pyridine cofactors, inhibited
by phenylsuccinate. This process mirrored L-lactate uptake by mitochondria and occurred with a hyperbolic dependence on L-lactate
concentrations. Pyruvate appeared outside mitochondria as a result of external addition of L-lactate. The rate of the process depended on L-lactate
concentration and showed saturation characteristics. This shows the occurrence of an intracellular L-lactate/pyruvate shuttle, whose activity was
limited by the putative L-lactate/pyruvate antiporter. Both the carriers were different from the monocarboxylate carrier.
(3) L-lactate transport changed en route to apoptosis. Uptake increased in the early phase of apoptosis, but decreased in the late phase with
characteristics of a non-competitive like inhibition. In contrast, the putative L-lactate/pyruvate antiport decreased en route to apoptosis with
characteristics of a competitive like inhibition in early apoptosis, and a mixed non-competitive like inhibition in late apoptosis.
© 2007 Elsevier B.V. All rights reserved. (literal)
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