Malonyl-CoA decarboxylase is present in the cytosolic, mitochondrial and peroxisomal compartments of rat hepatocytes.

Détails

ID Serval
serval:BIB_065F31F66709
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Malonyl-CoA decarboxylase is present in the cytosolic, mitochondrial and peroxisomal compartments of rat hepatocytes.
Périodique
FEBS letters
Auteur⸱e⸱s
Joly E., Bendayan M., Roduit R., Saha A.K., Ruderman N.B., Prentki M.
ISSN
0014-5793 (Print)
ISSN-L
0014-5793
Statut éditorial
Publié
Date de publication
05/12/2005
Peer-reviewed
Oui
Volume
579
Numéro
29
Pages
6581-6586
Langue
anglais
Notes
Publication types: Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
Publication Status: ppublish
Résumé
A role for cytosolic malonyl-CoA decarboxylase (MCD) as a regulator of fatty acid oxidation has been postulated. However, there is no direct evidence that MCD is present in the cytosol. To address this issue, we performed cell fractionation and electron microscopic colloidal gold studies of rat liver to determine the location and activity of MCD. By both methods, substantial amounts of MCD protein and activity were found in the cytosol, mitochondria and peroxisomes, the latter with the highest specific activity. MCD species with different electrophoretic mobility were observed in the three fractions. The data demonstrate that active MCD is present in the cytosol, mitochondria and peroxisomes of rat liver, consistent with the view that MCD participates in the regulation of cytosolic malonyl-CoA levels and of hepatic fatty acid oxidation.

Mots-clé
Animals, Carboxy-Lyases/analysis, Carboxy-Lyases/physiology, Cell Fractionation, Cytosol/enzymology, Hepatocytes/cytology, Male, Microscopy, Electron, Mitochondria, Liver/enzymology, Peroxisomes/enzymology, Rats, Rats, Sprague-Dawley
Pubmed
Web of science
Création de la notice
15/09/2017 12:13
Dernière modification de la notice
20/08/2019 12:28
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