Studies on the intracellular localization of acetyl-CoA carboxylase
| Autor: | Ronald J.A. Wanders, Caspaar Bijleveld, Math J.H. Geelen, Guillermo Velasco, Manuel Guzmán |
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| Přispěvatelé: | Other departments, Faculteit der Geneeskunde |
| Jazyk: | angličtina |
| Rok vydání: | 1997 |
| Předmět: |
Male
Biophysics Biology Biochemistry behavioral disciplines and activities chemistry.chemical_compound medicine Animals Carnitine Rats Wistar Molecular Biology Beta oxidation Carnitine O-Palmitoyltransferase Acetyl-CoA carboxylase Cell Biology Okadaic acid Peroxisome Subcellular localization Rats Pyruvate carboxylase medicine.anatomical_structure Liver chemistry Hepatocyte Acetyl-CoA Carboxylase Subcellular Fractions medicine.drug |
| Zdroj: | Biochemical and biophysical research communications, 233(1), 253-257. Academic Press Inc. Biochemical and Biophysical Research Communications, 233, 253-257. Academic Press Inc. |
| ISSN: | 0006-291X |
| DOI: | 10.1006/bbrc.1997.6437 |
| Popis: | The present work was performed to identify the subcellular localization of hepatic acetyl-CoA carboxylase (ACC). Cellular organelles involved in fatty acid oxidation that contain a malonyl-CoA sensitive carnitine palmitoyltransferase (CPT) activity or that are linked to the control of this activity were analysed for the presence of ACC. No significant amount of ACC was observed in the mitochondrial fraction prepared from isolated rat hepatocytes. Furthermore, no association of ACC activity and mass with isolated hepatic peroxisomes could be detected. Incubation of isolated hepatocytes with compounds known to affect the integrity of the cytoskeleton like okadaic acid or taxol indicates that ACC is associated with this subcellular structure of the hepatocyte. Such association may allow for efficient regulation of CPT activity and thus of fatty acid oxidation. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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