Differential carnitine/acylcarnitine translocase expression defines distinct metabolic signatures in skeletal muscle cells (Articolo in rivista)

Type
Label
  • Differential carnitine/acylcarnitine translocase expression defines distinct metabolic signatures in skeletal muscle cells (Articolo in rivista) (literal)
Anno
  • 2005-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1002/jcp.20239 (literal)
Alternative label
  • Peluso G.; Petillo O.; Margarucci S.; Grippo P.; Melone M.A.B.; Tuccillo F.; Calvani M. (2005)
    Differential carnitine/acylcarnitine translocase expression defines distinct metabolic signatures in skeletal muscle cells
    in Journal of cellular physiology (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Peluso G.; Petillo O.; Margarucci S.; Grippo P.; Melone M.A.B.; Tuccillo F.; Calvani M. (literal)
Pagina inizio
  • 439 (literal)
Pagina fine
  • 446 (literal)
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  • 203 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 2 (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • National Cancer Institute-INT ''Fondazione G. Pascale,'' Naples, Italy Institute of Protein Biochemistry-IBP, CNR, Naples, Italy Department of Experimental Medicine, School of Medicine, Second University of Naples, Naples, Italy Institute of Neurological Science, School of Medicine, Second University of Naples, Naples, Italy Scientific Department--Sigma-Tau, Pomezia, Rome, Italy (literal)
Titolo
  • Differential carnitine/acylcarnitine translocase expression defines distinct metabolic signatures in skeletal muscle cells (literal)
Abstract
  • Import of acylcarnitine into mitochondrial matrix through carnitine/acylcarnitine-translocase (CACT) is fundamental for lipid catabolism. To probe the effect of CACT down-expression on lipid metabolism in muscle, human myocytes were stably transfected with CACT-antisense construct. In presence of low concentration of palmitate, transfected cells showed decreased palmitate oxidation and acetyl-carnitine content, increased palmitoyl-carnitine level, and reduced insulin-dependent decrease of fatty acylcarnitine-to-fatty acyl-CoA ratio. The augmented palmitoyl-carnitine synthesis, also in the presence of insulin, could be related to an altered regulation of carnitine-palmitoyl-transferase 1 (CPT 1) by malonyl-CoA, whose synthesis is dependent by the availability of cytosolic acetyl-groups. Indeed, all the described effects were completely overcome by CACT neo-expression by recombinant adenovirus vector or by addition of acetyl-carnitine to cultures. Acetyl-carnitine effect was related to an increase of malonyl-CoA and was abolished by down-expression, via antisense RNA strategy, of acetyl-CoA carboxylase-ƒÒ, the mitochondrial membrane enzyme involved in the direct CPT 1 inhibition via malonyl-CoA synthesis. Thus, in our experimental model the modulation of CACT expression has consequences for CPT 1 activity, while the biologic effects of acetyl-carnitine are not associated with a generic supply of energy compounds but to the anaplerotic property of the molecule. (literal)
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