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Vol. 56, Issue 3, 570-580, September 1999
Gilead Sciences, Foster City, California (T.C., D.C.L., M.D.F.,
D.B.M.); and Laboratory of Pharmacology and Chemistry, National
Institute of Environmental Health Sciences, Research Triangle Park,
North Carolina (J.B.P., D.H.S)
Nephrotoxicity is the dose-limiting clinical adverse effect of
cidofovir and adefovir, two potent antiviral therapeutics. Because
renal uptake likely plays a role in the etiology of cidofovir- and
adefovir-associated nephrotoxicity, we attempted to identify a renal
transporter capable of interacting with these therapeutics. A cDNA
clone was isolated from a human renal library and designated human
organic anion transporter 1 (hOAT1). Northern analysis detected a
specific 2.5-kilobase pair hOAT1 transcript only in human kidney. However, reverse transcription-polymerase chain reaction
revealed hOAT1 expression in human brain and skeletal muscle, as well. Immunoblot analysis of human kidney cortex demonstrated that hOAT1 is
an 80- to 90-kilodalton heterogeneous protein modified by abundant N-glycosylation. Xenopus laevis oocytes
expressing hOAT1 supported probenecid-sensitive uptake of
[3H]p-aminohippurate
(Km = 4 µM), which was
trans-stimulated in oocytes preloaded with glutarate.
Importantly, both hOAT1 and rat renal organic anion transporter 1 (rROAT1) mediated saturable, probenecid-sensitive uptake of cidofovir,
adefovir, and other nucleoside phosphonate antivirals. The affinity of
hOAT1 toward cidofovir and adefovir (Km = 46 and
30 µM, respectively) was 5- to 9-fold higher compared with rROAT1
(Km = 238 and 270 µM, respectively). These
data indicate that hOAT1 may significantly contribute to the
accumulation of cidofovir and adefovir in renal proximal tubules and,
thus, play an active role in the mechanism of nephrotoxicity associated
with these antiviral therapeutics.
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