Evidence for the involvement of carnitine-dependent long-chain acyltransferases in neuronal triglyceride and phospholipid fatty acid turnover.

Abstract:

:This study focuses on the potential involvement of carnitine palmitoyltransferase (CPT) on the phospholipid and triglyceride fatty acid turnover in neurons. This category of enzymes, which has been identified in several rat brain tissues, is well known for its role in modulating cellular fatty acid oxidation. Neuronal cell cultures from rat brain cortex incorporated radioactive palmitate or oleate into phospholipids and triglycerides. The largest fraction of radioactive fatty acids was recovered in phosphatidylcholine followed by triglycerides and, to a lesser extent, phosphatidylethanolamine. CPT activity measured in neuronal lysates obtained from neurons treated with 40 microM 2-tetradecylglycidic acid (TDGA) was almost completely abolished. Furthermore, between 2 and 10 microM TDGA CPT activity dropped more rapidly than between 10 and 40 microM. When the cells were pretreated with TDGA, the incorporation process of either radioactive fatty acid into triglycerides was dose-dependently suppressed. Radioactive fatty acid incorporation into phosphatidylcholine was significantly decreased in cells treated with TDGA. In contrast, phosphatidylethanolamine reacylation was essentially not affected by the CPT inhibitor. Similar results on the fatty acid incorporation into triglycerides and phospholipids were observed with neurons treated with palmitoyl-DL-aminocarnitine (PAC), a reversible CPT inhibitor, which does not consume free CoA. These effects do not seem to be the result of an inhibitory activity toward one of the steps involved in the acylation-deacylation process of triglycerides or phospholipids, as cellular lysates from TDGA-treated cells or lysates containing PAC incorporated radioactive fatty acids at rates comparable to controls. Our results suggest that CPT may be an important partner in the pathway of phospholipid and triglyceride fatty acid turnover in neurons.

journal_name

J Neurochem

authors

Arduini A,Denisova N,Virmani A,Avrova N,Federici G,Arrigoni-Martelli E

doi

10.1046/j.1471-4159.1994.62041530.x

subject

Has Abstract

pub_date

1994-04-01 00:00:00

pages

1530-8

issue

4

eissn

0022-3042

issn

1471-4159

journal_volume

62

pub_type

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