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Carnitine palmitoyltransferase 2 (CPT2) is a mitochondrial enzyme that catalyzes the transfer of long-chain fatty acyl-CoA units to the two carnitine groups of L-carnitine. CPT2 is encoded by a single gene that produces two mRNA transcripts (CPT2a and CPT2b) that encode identical proteins. In this report, we identify and describe expression of CPT2 in the rat brain. We also show that brain CPT2 mRNA is regulated by the oxidative status of the cell. In primary cortical neurons, rat CPT2b mRNA levels increased approximately 1.7-fold in response to buthionine sulfoximine (BSO), a GSH synthesis inhibitor. This increase was associated with an approximately 2.5-fold increase in CPT2b enzyme activity. In contrast, the apparent Km of the enzyme for L-carnitine was unaffected by BSO. In rat hippocampal neurons, CPT2b mRNA levels were not affected by BSO or hydrogen peroxide. The apparent Km of CPT2 in these neurons was increased slightly by exposure to BSO. These findings suggest that CPT2b, a brain-specific variant of the mitochondrial enzyme CPT2, is regulated by mechanisms that are distinct from its relation to the overall regulation of CPT2 by cellular oxidative stress.Largely Unintended Consequences of the War on Terror

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