Rat organic solute carrier protein 1 (rOscp1) mediated the transport of organic solutes in Xenopus laevis oocytes: isolation and pharmacological characterization of rOscp1.

Rat organic solute carrier protein 1 (rOscp1) mediated the transport of organic solutes in Xenopus laevis oocytes: isolation and pharmacological characterization of rOscp1. Research Abstract Details 

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Rat organic solute carrier protein 1 (rOscp1) mediated the transport of organic solutes in Xenopus laevis oocytes: isolation and pharmacological characterization of rOscp1. Abstract Text:

Hisanori Izuno,Yasuna Kobayashi,Yutaka Sanada,Daisuke Nihei,Masako Suzuki,Noriko Kohyama,Masayuki Ohbayashi,Toshinori Yamamoto,Hisanori Izuno,Yasuna Kobayashi,Yutaka Sanada,Daisuke Nihei,Masako Suzuki,Noriko Kohyama,Masayuki Ohbayashi,Toshinori Yamamoto,Hisanori Izuno,Yasuna Kobayashi,Yutaka Sanada,Daisuke Nihei,Masako Suzuki,Noriko Kohyama,Masayuki Ohbayashi,Toshinori Yamamoto,

Rat organic solute carrier protein 1 (rOscp1) was isolated from a rat testis cDNA library. Isolated rOscp1 cDNA consisted of 1089 base pairs that encoded a 363-amino acid protein, and the amino acid sequence was 88% and 93% identical to that of human OSCP1 (hOSCP1) and mouse Oscp1 (mOscp1), respectively. The message for rOscp1 is highly detected in rat testis. When expressed in X. oocytes, rOscp1 mediated the high affinity transport of p-aminohippurate (PAH) with a Km value of 15.7+/-1.9 microM, and rOscp1-mediated organic solutes were exhibited in time- and Na+-independent manners. rOscp1 also transported various structurally heterogenous compounds such as testosterone, dehydroepiandrosterone sulfate (DHEA-S), and taurocholate with some differences in substrate specificity compared with hOSCP1. Immunohistochemical analysis revealed that the rOscp1 protein is localized in the basal membrane side of Sertoli cells as observed in mouse testis [Kobayashi et al., 2007; Kobayashi, Y., Tsuchiya, A., Hayashi, T., Kohyama, N., Ohbayashi, M., Yamamoto, T., 2007. Isolation and characterization of polyspecific mouse organic solute carrier protein 1 (mOscp1). Drug Metabolism and Disposition 35 (7), 1239-1245]. Thus, the present results indicate that a newly isolated cDNA clone, rOscp1, is a polyspecific organic solute carrier protein with some differences in substrate specificity compared with human and mouse OSCP1.

Rat organic solute carrier protein 1 (rOscp1) mediated the transport of organic solutes in Xenopus laevis oocytes: isolation and pharmacological characterization of rOscp1. Publishing Authors By Initials

H Izuno,Y Kobayashi,Y Sanada,D Nihei,M Suzuki,N Kohyama,M Ohbayashi,T Yamamoto,H Izuno,Y Kobayashi,Y Sanada,D Nihei,M Suzuki,N Kohyama,M Ohbayashi,T Yamamoto,H Izuno,Y Kobayashi,Y Sanada,D Nihei,M Suzuki,N Kohyama,M Ohbayashi,T Yamamoto,

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Rat organic solute carrier protein 1 (rOscp1) mediated the transport of organic solutes in Xenopus laevis oocytes: isolation and pharmacological characterization of rOscp1. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Life sciences

VOLUME: 81

Page Numbers: 1183-92

Journal Abbreviation: Life Sci.

ISSN: 0024-3205

DAY: 19

MONTH: 08

YEAR: 2007

Rat organic solute carrier protein 1 (rOscp1) mediated the transport of organic solutes in Xenopus laevis oocytes: isolation and pharmacological characterization of rOscp1. Information

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LANGUAGE: eng

NlmUniqueID: 375521

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AFFILIATION: Department of Surgery, School of Medicine, Showa University Fujigaoka Hospital,1-30 Fujigaoka, Aoba-ku, Yokohama-shi, Kanagawa 227-8501, Japan.

Country: England

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