ACSL4

ORLANDO, U.; MALOBERTI, P.M.; CASTILLO, A.F.; PODESTÁ, E.J

Encyclopedia of Signaling Molecules 2nd Edition.

Springer, New York. Plataforma: Meteor

Lugar: New York; Año: 2017; p. 1 - 8

The acyl-CoA synthetases (ACS) are enzymes that catalyze the production of acyl-CoA from fatty acids. The length of the carbon chain of the fatty acid species defines the substrate specificity for the different ACS. The presence of an ACS specific for arachidonate had been shown by enzymatic characterizations in 1985 (Laposata et al. 1985), and later the primary structure, enzymatic properties, and tissue expression of this newly identified ACS enzyme, designated ACS4 (later named ACSL4), were described by Kang et al. (1997). It belongs to the large family of mammalian long-chain acyl-CoA synthetases (ACSL), which activate fatty acids with chain lengths of 12-20 carbon atoms.The human and mouse genes for the ACSLs are termed ACSL1,3-6 and Acsl1,3-6, respectively. Each isoform has a substrate preference, subcellular localization, and tissue distribution and has been suggested to participate in the modulation of various pathophysiological events. Among the proteins in the family, ACSL4 has a strong preference for poly-unsaturated fatty acids, in particular arachidonic acid (AA) (Soupene and Kuypers 2008)