A novel mitochondrial carnitine-acylcarnitine translocase induced by partial hepatectomy and fasting.

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Sekoguchi E, Sato N, Yasui A, Fukada S, Nimura Y, Aburatani H, Ikeda K, Matsuura A

A novel mitochondrial carnitine-acylcarnitine translocase induced by partial hepatectomy and fasting.

J Biol Chem. 2003 Oct 3;278(40):38796-802. Epub 2003 Jul 25.

PubMed ID
12882971 [ View in PubMed
]
Abstract

The carnitine-dependent transport of long-chain fatty acids is essential for fatty acid catabolism. In this system, the fatty acid moiety of acyl-CoA is transferred enzymatically to carnitine, and the resultant product, acylcarnitine, is imported into the mitochondrial matrix through a transporter named carnitine-acylcarnitine translocase (CACT). Here we report a novel mammalian protein homologous to CACT. The protein, designated as CACL (CACT-like), is localized to the mitochondria and has palmitoylcarnitine transporting activity. The tissue distribution of CACL is similar to that of CACT; both are expressed at a higher level in tissues using fatty acids as fuels, except in the brain, where only CACL is expressed. In addition, CACL is induced by partial hepatectomy or fasting. Thus, CACL may play an important role cooperatively with its homologue CACT in a stress-induced change of lipid metabolism, and may be specialized for the metabolism of a distinct class of fatty acids involved in brain function.

DrugBank Data that Cites this Article

Drug Targets
DrugTargetKindOrganismPharmacological ActionActions
LevocarnitineMitochondrial carnitine/acylcarnitine carrier proteinProteinHumans
Unknown
Not AvailableDetails
LevocarnitineMitochondrial carnitine/acylcarnitine carrier protein CACLProteinHumans
Unknown
Not AvailableDetails