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Am J Physiol Regul Integr Comp Physiol 278: R1506-R1512, 2000;
0363-6119/00 $5.00
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Vol. 278, Issue 6, R1506-R1512, June 2000

Characterization of L-arginine transporters in rat renal inner medullary collecting duct

Feng Wu, Brian Cholewa, and David L. Mattson

Department of Physiology, Medical College of Wisconsin, Milwaukee, Wisconsin 53226

Previous work from our laboratory has demonstrated that the inner medullary collecting duct (IMCD) expresses a large amount of nitric oxide synthase (NOS) activity. The present study was designed to characterize the transport of NOS substrate, L-arginine, in a suspension of bulk-isolated IMCD cells from the Sprague-Dawley rat kidney. Biochemical transport studies demonstrated an L-arginine transport system in IMCD cells that was saturable and Na+ independent (n = 6). L-Arginine uptake by IMCD cells was inhibited by the cationic amino acids L-lysine, L-homoarginine, and L-ornithine (10 mmol/l each) and unaffected by the neutral amino acids L-leucine, L-serine, and L-glutamine. Both L-ornithine (n = 6) and L-lysine (n = 6) inhibited NOS enzymatic activity in a dose-dependent manner in IMCD cells, supporting the important role of L-arginine transport for NO production by this tubular segment. Furthermore, RT-PCR of microdissected IMCD confirmed the presence of cationic amino acid transporter CAT1 mRNA, whereas CAT2A, CAT2B, and CAT3 were not detected. These results indicate that L-arginine uptake by IMCD cells occurs via system y+, is encoded by CAT1, and may participate in the regulation of NO production in this renal segment.

kidney; kidney collecting duct; nitric oxide synthase


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