Dietary Linoleic Acid Alters .ALPHA.-Amino-.BETA.-carboxymuconate-.EPSILON.-semialdehyde Decarboxylase (ACMSD), a Key Enzyme of Niacin Synthesis from Tryptophan, in the Process of Protein Expression in Rat Liver.

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Abstract
α-Amino-β-carboxymuconate-8-semialdehyde decarboxylase (ACMSD) [EC 4.1.1.45] is a key enzyme of niacin synthesis from tryptophan. In this study, we examined whether dietary linoleic acid alters the protein expression of ACMSD in rat liver. Antibody against rat liver ACMSD was prepared by injecting mice with the purified enzyme. With the use of this polyclonal antibody and analysis by two-dimensional electrophoresis, we studied the mechanism by which the level of liver ACMSD activity was varied in rats fed a linoleic acid diet. In the rats fed a dietary linoleic acid (L), ACMSD protein levels in the liver were strongly suppressed as compared with the rats fed a fat-free diet (FF). These results suggest that the expression level of ACMSD might be modulated by linoleic acid or their metabolites.

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