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Technetium‐99m‐MAG3 as a transport substrate of rat renal organic anion transporter‐1
Author(s) -
Shikano N.,
Kawai K.,
Ishikawa N.,
Kubodera A.
Publication year - 2001
Publication title -
journal of labelled compounds and radiopharmaceuticals
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.432
H-Index - 47
eISSN - 1099-1344
pISSN - 0362-4803
DOI - 10.1002/jlcr.25804401222
Subject(s) - chemistry , organic anion transporter 1 , organic anion , transporter , epithelial polarity , xenopus , symporter , kidney , substrate (aquarium) , cotransporter , proximal tubule , ion transporter , technetium , membrane transport , biochemistry , membrane , endocrinology , ion , nuclear chemistry , biology , sodium , ecology , organic chemistry , gene
The first step of technetium‐99m‐mercaptoacetylglycylglycylglycine ( 99m Tc‐MAG 3 ) secretion by the proximal tubule cells is the extraction of 99m Tc‐MAG 3 from the peritubular plasma by proximal tubule cells through the basolateral membrane. The evidence for 99m Tc‐MAG 3 being excreted from renal proximal tubules via rat organic anion transporter 1 (OAT1) by molecular biological experiments with expressed OAT1 in Xenopus laevis oocytes was discussed. Inhibition studies of 99m Tc‐MAG 3 revealed that OAT1 mediated Na + ‐independent 99m Tc‐MAG 3 uptake, and that this transport was energy‐independent. Accumulated dicarboxylate, such as glutarate, stimulated 99m Tc‐MAG 3 uptake. Tc‐99m‐MAG 3 , as well as paminohippurate (PAH), and o ‐iodohippurate (OIH), was confirmed to be a transport substrate of OAT1 by the uptake of expressed oocytes.