Fatty acid desaturases and elongases (FADS/ELOVL)

Fatty acid desaturases and elongases represent a complex group of enzymes responsible for the biosynthesis of long-chain polyunsaturated fatty acids (LC-PUFAs) and the maintenance of cellular lipid homeostasis (Nakamura & Nara, 2004, PMID: 15159230). Desaturases, including Stearoyl-CoA desaturase (SCD) and the Fatty Acid Desaturase (FADS) family, introduce double bonds into fatty acyl chains, while the Elongation of Very Long chain fatty acids (ELOVL) proteins catalyze the addition of two-carbon units to extend these chains (UniProt P37173, O60427). These enzymes are critical for regulating membrane fluidity, providing precursors for signaling molecules like eicosanoids, and managing energy storage in the form of triglycerides (Jump et al., 2008, PMID: 18403517). Dysregulation of these pathways is a hallmark of metabolic diseases such as non-alcoholic fatty liver disease (NAFLD) and obesity, and is increasingly recognized as a driver of cancer progression by supporting rapid membrane synthesis and pro-survival signaling (Igal, 2010, PMID: 20335444). Pharmacological inhibitors, particularly those targeting SCD1 like Aramchol, have been developed to treat steatohepatitis and metabolic disorders, though their clinical utility is often limited by significant side effects in the skin and eyes due to the essential role of these enzymes in sebaceous gland function (Safadi et al., 2014, PMID: 24815804).

Other names

Fatty acid desaturase familyElongation of very long chain fatty acids protein familyStearoyl-CoA desaturaseDelta-6 desaturaseDelta-5 desaturaseDelta-9 desaturaseFatty acid elongaseFADS1FADS2SCD1ELOVL1-7

Inhibition of desaturation (insertion of double bonds) or elongation (addition of carbon pairs) to modulate the ratio of saturated to unsaturated fatty acids and reduce the production of pro-inflammatory lipid mediators.