Analysis of Cationic Amino Acid Transport Activity in Canine Lens Epithelial Cells

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  • Ochiai Hideharu
    Research Institute of Biosciences, Azabu University, School of Veterinary Medicine, 1-17-71 Fuchinobe, Chuou-ku, Sagamihara, Kanagawa 252-5201, Japan
  • Moriyama Jun
    Research Institute of Biosciences, Azabu University, School of Veterinary Medicine, 1-17-71 Fuchinobe, Chuou-ku, Sagamihara, Kanagawa 252-5201, Japan
  • Kanemaki Nobuyuki
    Animal Teaching Hospital, Azabu University, School of Veterinary Medicine, 1-17-71 Fuchinobe, Chuou-ku, Sagamihara, Kanagawa 252-5201, Japan
  • Sato Reiichiro
    Laboratory of Gynecology and Obstetrics, Azabu University, School of Veterinary Medicine, 1-17-71 Fuchinobe, Chuou-ku, Sagamihara, Kanagawa 252-5201, Japan
  • Onda Ken
    Laboratory of Internal Medicine III, Azabu University, School of Veterinary Medicine, 1-17-71 Fuchinobe, Chuou-ku, Sagamihara, Kanagawa 252-5201, Japan

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抄録

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.

収録刊行物

  • Experimental Animals

    Experimental Animals 62 (4), 311-317, 2013

    公益社団法人 日本実験動物学会

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