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Titolo:
COORDINATE REGULATION OF NITRIC-OXIDE AND 1,25-DIHYDROXYVITAMIN-D PRODUCTION IN THE AVIAN MYELOMONOCYTIC CELL-LINE HD-11
Autore:
ADAMS JS; REN SY; ARBELLE JE; SHANY S; GACAD MA;
Indirizzi:
UNIV CALIF LOS ANGELES,CEDARS SINAI MED CTR,SCH MED,DIV ENDOCRINOL & METAB,B131 LOS ANGELES CA 90048 UNIV CALIF LOS ANGELES,CEDARS SINAI MED CTR,SCH MED,RES INST LOS ANGELES CA 90048 BEN GURION UNIV NEGEV,FAC MED IL-84101 BEER SHEVA ISRAEL
Titolo Testata:
Endocrinology
fascicolo: 5, volume: 136, anno: 1995,
pagine: 2262 - 2269
SICI:
0013-7227(1995)136:5<2262:CRONA1>2.0.ZU;2-U
Fonte:
ISI
Lingua:
ENG
Soggetto:
CULTURED ALVEOLAR MACROPHAGES; SARCOIDOSIS-ASSOCIATED HYPERCALCEMIA; VITAMIN-D; SERUM 1,25-DIHYDROXYVITAMIN-D; CALCIUM-CONCENTRATION; INTERFERON-GAMMA; L-ARGININE; SYNTHASE; EXPRESSION; KETOCONAZOLE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
48
Recensione:
Indirizzi per estratti:
Citazione:
J.S. Adams et al., "COORDINATE REGULATION OF NITRIC-OXIDE AND 1,25-DIHYDROXYVITAMIN-D PRODUCTION IN THE AVIAN MYELOMONOCYTIC CELL-LINE HD-11", Endocrinology, 136(5), 1995, pp. 2262-2269

Abstract

Cells of the monocyte/macrophage lineage are capable of both nitric oxide (NO) and 1,25-dihydroxyvitamin D [1, 25-(OH)(2)D] production through expression of inducible nitric oxide synthase (iNOS) and a putative 25-hydroxyvitamin D (25-OHD)-1-hydroxylase, respectively. We have recently reported that 1,25-(OH)(2)D synthesis in the chick myelomonocytic cell Line HD-11 is restricted by inhibition of iNOS. In the currentset of experiments, measuring nitrite, a stable water-soluble secreted metabolite of NO as an index of iNOS activity and 1,25-(OH)(2)D-3 inlipid extracts of cells incubated with 200 nM 25-OHD3 as an index of 1-hydroxylase activity, we demonstrate that NO and 1,25-(OH)(2)D production by HD-11 cells are temporally related, induced by the same kindsof activating agents, and coordinately regulated. NO and 1,25-(OH)(2)D-3 production by HD-11 cells was stimulated severalfold by the macrophage stimulators interferon-gamma and lipopolysaccharide and by an autologous, nonlipid, heat-labile factor with an apparent molecular mass approximate to 10,000 daltons. As expected NO synthesis was 1) dependent upon the presence of L-arginine in the extracellular medium, 2) subject to significant stimulation by N-W-hydroxy-L-arginine, an L-arginine-derived intermediate in NO biosynthesis, and by sodium nitroprusside, a non-L-arginine-dependent source of intracellular NO, and 3) inhibited by N-W-nitro-L-arginine methyl ester, a competitive inhibitor of iNOS. At high NO production rates, induced either by high-dose lipopolysaccharide or by sodium nitroprusside exposure, there was an apparentdownturn in 1,25(OH)(2)D-3 synthesis, suggesting functional dependence of the 1-hydroxylase on NO but ultimate inhibition of 1,25-(OH)(2)D-3 synthetic capacity at high levels of intracellular NO production. Onthe basis of these results we postulate that the macrophage 25-OHD-1-hydroxylation reaction may be dependent on iNOS-generated NO as a soluble source of electrons and regulated in an autocrine mode by a macrophage-derived NO stimulatory factor and NO itself.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 18/09/20 alle ore 11:11:49