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Analysis of cationic amino acid transport activity in canine lens epithelial cells.

ABSTRACT: Cationic amino acid transport activity in a canine lens epithelial cells (LEC) line was investigated. The transporter activity of arginine was 0.424 ± 0.047 nmol/mg protein min, while the presence of N-ethylmaleimide, an inhibitor of the canine cationic amino acid transporter (CAT), reduced transport activity by 30%. A full-length cDNA sequence of canine CAT1 was 2558 bp long and was predicted to encode the 629 amino acid polypeptides. The deduced amino acid sequence of canine CAT1 showed similarities of 92.1% and 88.6% to those of the human and mouse, respectively. Western blot analysis detected a band at 70 kDa in a membrane protein sample of LEC. RT-PCR analysis confirmed that CAT1 was ubiquitously detected in all tissues examined.

SUBMITTER: Ochiai H

PROVIDER: S-EPMC4160958 | biostudies-literature | 2013

REPOSITORIES: biostudies-literature

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Analysis of cationic amino acid transport activity in canine lens epithelial cells.

Ochiai Hideharu H Moriyama Jun J Kanemaki Nobuyuki N Sato Reiichiro R Onda Ken K

Experimental animals 20130101 4

Cationic amino acid transport activity in a canine lens epithelial cells (LEC) line was investigated. The transporter activity of arginine was 0.424 ± 0.047 nmol/mg protein min, while the presence of N-ethylmaleimide, an inhibitor of the canine cationic amino acid transporter (CAT), reduced transport activity by 30%. A full-length cDNA sequence of canine CAT1 was 2558 bp long and was predicted to encode the 629 amino acid polypeptides. The deduced amino acid sequence of canine CAT1 showed simila ...[more]

PMID: 24172195

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