Role of rBAT gene products in cystinuria
| Autor: | Susumu Kagawa, Ken-ichi Miyamoto, Kanako Katai, Kazumi Takada, Sawako Tatsumi, Eiji Takeda, Hiroko Segawa, Hiro-omi Kanayama, Kanako Sone, Hironori Yamamoto, Yutaka Taketani, Kyoko Morita |
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| Rok vydání: | 2014 |
| Předmět: |
Arginine
Urology Sodium Xenopus Mutant Cystine chemistry.chemical_element Biology chemistry.chemical_compound Leucine Animals Humans chemistry.chemical_classification Cystinuria Microvilli Activator (genetics) Wild type Biological Transport Amino acid Protein Structure Tertiary Amino Acid Transport Systems Neutral chemistry Biochemistry Mutagenesis Oocytes Amino Acid Transport Systems Basic |
| Zdroj: | International journal of urology : official journal of the Japanese Urological Association. 3 |
| ISSN: | 1442-2042 |
| Popis: | To investigate whether rBAT gene products function as a crystine transporter component or as a transport activator, we microinjected several C-terminal deletion mutants of rBAT cRNA into Xenopus oocytes, and measured transport activity for arginine, leucine and cystine in the presence and absence of sodium. Wild type rBAT significantly stimulated the uptake of all 3 amino acids 10-20 fold compared to control mutants. On the other hand, no mutant, except a Δ511-685 mutant, stimulated the uptake of these amino acids. However, the Δ511-685 mutant significantly increased the uptake of arginine. In the presence of sodium, the Δ511-685 mutant also increased the uptake of leucine. The Δ511-685 mutant did not stimulate crystine uptake in the presence and absence of sodium. Furthermore, inhibition of L-arginine uptake by L-homoserine was seen only in the presence of sodium. These results suggest that mutant rBAT stimulates the endogenous amino acid transport system y+ in oocytes. Finally, rBAT gene products, as the primary cause of cystinuria, may function as activators of the amino acid transport system in renal brush border membrane. |
| Databáze: | OpenAIRE |
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