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.
journal_name
Biochimiejournal_title
Biochimieauthors
Lindner HA,Täfler-Naumann M,Röhm KHdoi
10.1016/j.biochi.2007.12.006subject
Has Abstractpub_date
2008-05-01 00:00:00pages
773-80issue
5eissn
0300-9084issn
1638-6183pii
S0300-9084(08)00002-3journal_volume
90pub_type
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