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Am J Physiol Endocrinol Metab 291: E291-E297, 2006. First published February 14, 2006; doi:10.1152/ajpendo.00413.2005
0193-1849/06 $8.00
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Characterization of L-arginine transport in adrenal cells: effect of ACTH

Esteban M. Repetto,1 Vanesa Pannunzio,1 Francisco Astort,1 Camila Martinez Calejman,1 Marcos Besio Moreno,2,3 Omar P. Pignataro,2,3 and Cora B. Cymeryng1

1Departamento de Bioquímica Humana, Facultad de Medicina; 2Instituto de Biología y Medicina Experimental, and 3Departamento de Quimica Biológica Facultad de Cs Exactas y Naturale, Universidad de Buenos Aires, Buenos Aires, Argentina

Submitted 30 August 2005 ; accepted in final form 20 January 2006

Nitric oxide synthesis depends on the availability of its precursor L-arginine, which could be regulated by the presence of a specific uptake system. In the present report, the characterization of the L-arginine transport system in mouse adrenal Y1 cells was performed. L-arginine transport was mediated by the cationic/neutral amino acid transport system y+L and the cationic amino acid transporter (CAT) y+ in Y1 cells. These Na+-independent transporters were identified by their selectivity for neutral amino acids in both the presence and absence of Na+ and by the effect of N-ethylmaleimide. Transport data correlated to expression of genes encoding for CAT-1, CAT-2, CD-98, and y+LAT-2. A similar expression profile was detected in rat adrenal zona fasciculata. In addition, cationic amino acid uptake in Y1 cells was upregulated by ACTH and/or cAMP with a concomitant increase in nitric oxide (NO) production.

nitric oxide; adrenocorticotropic hormone; protein kinase A


Address for reprint requests and other correspondence: C. B. Cymeryng, Departamento de Bioquímica Humana, Facultad de Medicina, Universidad de Buenos Aires, Paraguay 2155 5° (1121ABG), Buenos Aires, Argentina (e-mail: cymeryng{at}fmed.uba.ar)






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