L-Arginine transport in adrenal cells. ACTH increases L-Arginine uptake and NO production

REPETTO E.M.; PANNUNZIO V.; ASTORT F.; MARTINEZ CALEJMAN C.; BESIO MORENO M.; PIGNATARO O.; CYMERYNG C. B.

AMERICAN JOURNAL OF PHYSIOLOGY-ENDOCRINOLOGY AND METABOLISM

American Physiological Society

Lugar: Bethesda, Maryland (EEUU); Año: 2006 vol. 291 p. 291 - 297

0193-1849

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 cationicamino 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.