TitleMammalian fatty acid elongases.
Publication TypeJournal Article
Year of Publication2009
AuthorsJump DB
JournalMethods Mol Biol
Date Published2009
KeywordsAcetyltransferases, Animals, Chromatography, High Pressure Liquid, Lipid Metabolism, Male, Mice, Mice, Inbred C57BL, Microsomes, Rats, Rats, Sprague-Dawley, Substrate Specificity

Very long chain fatty acids confer functional diversity on cells by variations in their chain length and degree of unsaturation. Microsomal fatty acid elongation represents the major pathway for determining the chain length of saturated, monounsaturated, and polyunsaturated fatty acids in cellular lipids. The overall reaction for fatty acid elongation involves four enzymes and utilizes malonyl CoA, NADPH, and fatty acyl CoA as substrates. While the fundamental pathway and its requirements have been known for many years, recent advances have revealed a family of enzymes involved in the first step of the reaction, i.e., the condensation reaction. Seven fatty acid elongase subtypes (Elovl #1-7) have been identified in the mouse, rat, and human genomes. These enzymes determine the rate of overall fatty acid elongation. Moreover, these enzymes also display differential substrate specificity, tissue distribution, and regulation, making them important regulators of cellular lipid composition as well as specific cellular functions. Herein, methods are described to measure elongase activity, analyze elongation products, and alter cellular elongase expression.

Alternate JournalMethods Mol. Biol.
PubMed ID19763486
PubMed Central IDPMC2764369
Grant ListR01 DK043220 / DK / NIDDK NIH HHS / United States
R01 DK043220-16 / DK / NIDDK NIH HHS / United States
DK43220 / DK / NIDDK NIH HHS / United States