Flight muscle carnitine palmitoyl transferase activity varies with substrate chain length and unsaturation in the hoary bat, Lasiurus cinereus

Edwin R Price, Liam McGuire, M Brock Fenton, Christopher G Guglielmo

Research output: Contribution to journalArticlepeer-review

Abstract

Fat is an important fuel for bats to support high metabolic rates in extended periods of flight. The fatty acid composition of adipose stores could affect whole animal exercise performance, as fatty acids vary in rates of mobilization and oxidation. A key step in the fatty acid oxidation pathway is transporting fatty acids from the cytosol into mitochondria, mediated by the enzyme carnitine palmitoyl transferase (CPT). Therefore, understanding the substrate preference patterns of CPT in bats is important for interpreting the consequences of adipose fatty acid profiles. We measured CPT activity with eight different fatty acyl CoA substrates (16:0, 16:17, 18:0, 18:19, 18:26, 18:33, 20:46, and 22:63) in the pectoralis muscle of migrating and nonmigrating hoary bats (Lasiurus cinereus (Beauvois, 1796)). The pattern of substrate preference was similar to the patterns previously reported for birds and rats and was not affected by migration. Generally, activity increased with the number of d
Original languageEnglish
Pages (from-to)173-176
JournalCanadian Journal of Zoology
StatePublished - Feb 2014

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