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Malonyl-CoA decarboxylase is present in the cytosolic, mitochondrial and peroxisomal compartments of rat hepatocytes
| Title | Malonyl-CoA decarboxylase is present in the cytosolic, mitochondrial and peroxisomal compartments of rat hepatocytes |
| Publication Type | Journal Article |
| Year of Publication | 2005 |
| Authors | |
| Journal | FEBS Lett |
| Volume | 579 |
| Issue | 29 |
| Pagination | 6581-6 |
| Date Published | Dec 5 |
| Publication Language | eng |
| ISBN Number | 0014-5793 (Print) |
| Accession Number | 16298369 |
| Key Words | Rats, Sprague-Dawley, Mitochondria, Liver/enzymology, Microscopy, Electron, Male, Animals, Peroxisomes/enzymology, Hepatocytes/*cytology, Cytosol/*enzymology, Cell Fractionation, Carboxy-Lyases/*analysis/physiology |
| Abstract | 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. |
| Notes | R0I DK 19514/DK/NIDDK NIH HHS/United StatesJournal ArticleResearch Support, N.I.H., ExtramuralResearch Support, Non-U.S. Gov'tNetherlands |
| URL | http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=16298369 |
| Citation Key | 390 |
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