TY - JOUR
T1 - p-aminohippuric acid transport at renal apical membrane mediated by human inorganic phosphate transporter NPT1
AU - Uchino, Hiroshi
AU - Tamai, Ikumi
AU - Yamashita, Katsumi
AU - Minemoto, Yuzuru
AU - Sai, Yoshimichi
AU - Yabuuchi, Hikaru
AU - Miyamoto, Ken Ichi
AU - Takeda, Eiji
AU - Tsuji, Akira
PY - 2000/4/2
Y1 - 2000/4/2
N2 - Organic anions are secreted into urine via organic anion transporters across the renal basolateral and apical membranes. However, no apical membrane transporter for organic anions such as p-aminohippuric acid (PAH) has yet been identified. In the present study, we showed that human NPT1, which is present in renal apical membrane, mediates the transport of PAH. The K(m) value for PAH uptake was 2.66 mM and the uptake was chloride ion sensitive. These results are compatible with those reported for the classical organic anion transport system at the renal apical membrane. PAH transport was inhibited by various anionic compounds. Human NPT1 also accepted uric acid, benzylpenicillin, faropenem, and estradiol-17β-glucuronide as substrates. Considering its chloride ion sensitivity, Npt1 is expected to function for secretion of PAH from renal proximal tubular cells. This is the first molecular demonstration of an organic anion transport function for PAH at the renal apical membrane. (C) 2000 Academic Press.
AB - Organic anions are secreted into urine via organic anion transporters across the renal basolateral and apical membranes. However, no apical membrane transporter for organic anions such as p-aminohippuric acid (PAH) has yet been identified. In the present study, we showed that human NPT1, which is present in renal apical membrane, mediates the transport of PAH. The K(m) value for PAH uptake was 2.66 mM and the uptake was chloride ion sensitive. These results are compatible with those reported for the classical organic anion transport system at the renal apical membrane. PAH transport was inhibited by various anionic compounds. Human NPT1 also accepted uric acid, benzylpenicillin, faropenem, and estradiol-17β-glucuronide as substrates. Considering its chloride ion sensitivity, Npt1 is expected to function for secretion of PAH from renal proximal tubular cells. This is the first molecular demonstration of an organic anion transport function for PAH at the renal apical membrane. (C) 2000 Academic Press.
UR - http://www.scopus.com/inward/record.url?scp=0034595094&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0034595094&partnerID=8YFLogxK
U2 - 10.1006/bbrc.2000.2407
DO - 10.1006/bbrc.2000.2407
M3 - Article
C2 - 10733936
AN - SCOPUS:0034595094
SN - 0006-291X
VL - 270
SP - 254
EP - 259
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 1
ER -