TY - JOUR
T1 - Functional analysis of rat renal organic anion transporter OAT-K1
T2 - Bidirectional methotrexate transport in apical membrane
AU - Masuda, Satohiro
AU - Takeuchi, Ayako
AU - Saito, Hideyuki
AU - Hashimoto, Yukiya
AU - Inui, Ken Ichi
N1 - Funding Information:
We thank Dr. P. Agre, Department of Biological Chemistry and Medicine, School of Medicine, Johns Hopkins University, for providing the plasmid XβG expression vector. This work was supported by a Grand-in-Aid for Scientific Research from the Ministry of Education, Science, and Culture of Japan, by a Grand-in-Aid from the Japan Research Foundation for Clinical Pharmacology, and from the Uehara Memorial Foundation.
PY - 1999/10/1
Y1 - 1999/10/1
N2 - Renal organic anion transporter OAT-K1 was stably transfected in MDCK cells and examined for its transport characteristics and membrane localization. OAT-K1 mediated both uptake and efflux of methotrexate in the apical membranes. Immunoblotting showed that the apparent molecular mass of the expressed OAT-K1 was 50 kDa, which was comparable to that found in the rat renal brush-border membranes. The OAT-K1-mediated methotrexate transport was significantly inhibited in the presence of several organic anions such as folate and sulfobromophthalein. These findings suggest that OAT-K1 mediates bidirectional methotrexate transport across the apical membranes, and may be involved in the renal handling of methotrexate. Copyright (C) 1999 Federation of European Biochemical Societies.
AB - Renal organic anion transporter OAT-K1 was stably transfected in MDCK cells and examined for its transport characteristics and membrane localization. OAT-K1 mediated both uptake and efflux of methotrexate in the apical membranes. Immunoblotting showed that the apparent molecular mass of the expressed OAT-K1 was 50 kDa, which was comparable to that found in the rat renal brush-border membranes. The OAT-K1-mediated methotrexate transport was significantly inhibited in the presence of several organic anions such as folate and sulfobromophthalein. These findings suggest that OAT-K1 mediates bidirectional methotrexate transport across the apical membranes, and may be involved in the renal handling of methotrexate. Copyright (C) 1999 Federation of European Biochemical Societies.
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U2 - 10.1016/S0014-5793(99)01221-1
DO - 10.1016/S0014-5793(99)01221-1
M3 - Article
C2 - 10508931
AN - SCOPUS:0032859176
SN - 0014-5793
VL - 459
SP - 128
EP - 132
JO - FEBS Letters
JF - FEBS Letters
IS - 1
ER -