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Titolo:
PARALLEL REGULATION OF ARGININE TRANSPORT AND NITRIC-OXIDE SYNTHESIS BY ANGIOTENSIN-II IN VASCULAR SMOOTH-MUSCLE CELLS - ROLE OF PROTEIN-KINASE-C
Autore:
RIVERACORREA M; ALTIERI PI; ESCOBALES N;
Indirizzi:
UNIV PUERTO RICO,SCH MED,DEPT PHYSIOL,GPO BOX 365067 SAN JUAN PR 00936 UNIV PUERTO RICO,SCH MED,DEPT PHYSIOL SAN JUAN PR 00936 UNIV PUERTO RICO,SCH MED,DEPT MED SAN JUAN PR 00936
Titolo Testata:
Amino acids
fascicolo: 2, volume: 11, anno: 1996,
pagine: 153 - 170
SICI:
0939-4451(1996)11:2<153:PROATA>2.0.ZU;2-A
Fonte:
ISI
Lingua:
ENG
Soggetto:
AMINO-ACID-TRANSPORT; SPONTANEOUSLY HYPERTENSIVE RATS; SYSTEM-L; PROLIFERATION; EXPRESSION; ATHEROSCLEROSIS; MECHANISMS; INHIBITION; INDUCTION; SYNTHASE;
Keywords:
AMINO ACIDS; ARGININE TRANSPORT; NITRIC OXIDE; SMOOTH MUSCLE CELLS; ANGIOTENSIN II; PROTEIN KINASE C;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
53
Recensione:
Indirizzi per estratti:
Citazione:
M. Riveracorrea et al., "PARALLEL REGULATION OF ARGININE TRANSPORT AND NITRIC-OXIDE SYNTHESIS BY ANGIOTENSIN-II IN VASCULAR SMOOTH-MUSCLE CELLS - ROLE OF PROTEIN-KINASE-C", Amino acids, 11(2), 1996, pp. 153-170

Abstract

Experiments were performed to characterize arginine transport in vascular smooth muscle cells (SMCs) and the effect of angiotensin II (Ang II) on this process. In addition, the role of arginine transport in the cytokine-induced nitric oxide (NO) production was assessed. Argininetransport takes place through Na+-independent (approximate to 60%) and Na+-dependent pathways (approximate to 40%). The Na+-independent arginine uptake appears to be mediated by system y(+) because of its sensitivity to cationic amino acids such as lysine, ornithine and homoarginine. The transport system was relatively insensitive to acidificationof the extracellular medium. By contrast, the Na+-dependent pathway is consistent with system B-0,B-+ since it was inhibited by both cationic and neutral amino acids (i.e., glutamine, phenylalanine, and asparagine), and did not accept Li+ as a Na+ replacement. Treatment of SMCs with 100 nM Ang II significantly inhibited the Na+-dependent arginine transport without affecting systems y(+), A, and L. This effect occurred in a dose-dependent manner (IC50 of 8.9 +/- 0.9 nM) and is mediatedby the AT-1 receptor subtype because it was blocked by DUP 753, a non-peptide antagonist of this receptor. The inhibition of system B-0,B-by Ang II is mediated by protein kinase C (PKC) because it was mimicked by phorbol esters (phorbol 12-myristate 13-acetate) and was inhibited by staurosporine. Ang II also inhibited the IL-1 beta induced nitrite accumulation by SMCs. This action was also inhibited by staurosporine and reproduced with phorbol esters, suggesting a coupling between arginine uptake and NO synthesis through a PKC-dependent mechanism. However, arginine supplementation in the medium (10 mM) failed to preventthe inhibitory action of Ang IT on NO synthesis. These findings suggest that although Ang II inhibits concomitantly arginine transport and NO synthesis in SMCs, the reduction of NO synthesis is not associated with alterations in the cellular transport of arginine.

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Documento generato il 28/01/21 alle ore 07:05:27