Elongation of very long chain fatty acids protein 5 (ELOVL5)

Elongation of very long chain fatty acids protein 5 (ELOVL5) is a transmembrane enzyme located in the endoplasmic reticulum that catalyzes the first step (condensation) in the elongation of polyunsaturated fatty acids, with a preference for substrates that are 18–20 carbons in length, including linoleic and alpha-linolenic acids. ELOVL5 is critical for the biosynthesis of long-chain polyunsaturated fatty acids (LC-PUFAs), which are essential for membrane structure, lipid signaling, and other cellular processes. The enzyme is widely expressed in several tissues, with notable abundance in the CNS, testis, and tissues associated with high PUFA metabolism. Pathogenic mutations in ELOVL5 cause spinocerebellar ataxia type 38 (SCA38), while aberrant ELOVL5 expression or activity has been associated with cancer cell proliferation, invasion, and altered lipid metabolism, suggesting it is a potential therapeutic target in oncology and neurology.

Other names

Very long chain fatty acid elongase 5ELOVL FA elongase 5hELO1HELO1dJ483K16.13-ketoacyl-CoA synthase ELOVL5fatty acid elongase 1homolog of yeast long chain polyunsaturated fatty acid elongation enzyme 2spinocerebellar ataxia 38 proteinvery long chain 3-ketoacyl-CoA synthase 5very long chain 3-oxoacyl-CoA synthase 5

Inhibitors or knockdown suppress PUFA elongation, affect lipid composition in cells, modulate cell signaling (e.g., suppressing the AKT-mTOR-STAT3 pathway in cancer)