Abstract
Mammalian aminoacylase-1 (Acy1) participates in the breakdown of N-acetylated amino acids during intracellular protein catabolism. Acy1 is most abundantly expressed in the kidney tubular epithelium. Lately, Acy1 deficiency was identified in children with increased urinary excretion of several N-acetylamino acids. Here we report detailed N-acetylamino acid specificity profiles for human and porcine Acy1 based on steady state kinetic measurements. We found that LLC-PK1 cells, a model of the porcine kidney proximal tubular epithelium, robustly express Acy1. For the first time, we demonstrate uptake and utilization of N-acteylleucine and -methionine in replacement of the free amino acid, respectively, in cultured epithelial cells. Our data are consistent with a specific role of kidney Acy1 in the salvage of amino acids originating from systemic degradation of N-acetylated proteins.
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