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Titolo:
Acyl-CoA : retinal acyltransferase (ARAT) and lecithin : retinol acyltransferase (LRAT) activation during the lipocyte phenotype induction in hepaticstellate cells
Autore:
Fortuna, VA; Trugo, LC; Borojevic, R;
Indirizzi:
Inst Ciencias Biomed, Dept Histol & Embriol, Rio De Janeiro, Brazil Inst Ciencias Biomed Rio De Janeiro Brazil riol, Rio De Janeiro, Brazil Inst Quim, Dept Bioquim, Rio De Janeiro, Brazil Inst Quim Rio De JaneiroBrazil m, Dept Bioquim, Rio De Janeiro, Brazil Univ Fed Rio de Janeiro, Hosp Univ Clementino Fraga Filho, Programa Avancado Biol Celular Aplicada Med, Rio De Janeiro, Brazil Univ Fed Rio de Janeiro Rio De Janeiro Brazil d, Rio De Janeiro, Brazil
Titolo Testata:
JOURNAL OF NUTRITIONAL BIOCHEMISTRY
fascicolo: 11, volume: 12, anno: 2001,
pagine: 610 - 621
SICI:
0955-2863(200111)12:11<610:A:RA(A>2.0.ZU;2-J
Fonte:
ISI
Lingua:
ENG
Soggetto:
RAT-LIVER MICROSOMES; VITAMIN-A STATUS; BINDING-PROTEINS; ESTER STORAGE; METABOLISM; ESTERIFICATION; ROLES; DISTRIBUTIONS; LOCALIZATION; MORPHOLOGY;
Keywords:
vitamin A; esterification; ARAT; LRAT; hepatic stellate cells; liver;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Citazioni:
46
Recensione:
Indirizzi per estratti:
Indirizzo: Borojevic, R Inst Ciencias Biomed, Dept Histol & Embriol, Rio De Janeiro, Brazil Inst Ciencias Biomed Rio De Janeiro Brazil Janeiro, Brazil
Citazione:
V.A. Fortuna et al., "Acyl-CoA : retinal acyltransferase (ARAT) and lecithin : retinol acyltransferase (LRAT) activation during the lipocyte phenotype induction in hepaticstellate cells", J NUTR BIOC, 12(11), 2001, pp. 610-621

Abstract

We have examined retinal esterification in the established GRX cell line, representative of hepatic stellate cells, and in primary cultures of ex vivo purified murine hepatic stellate cells. The metabolism of [H-3]retinol was compared in cells expressing the myofibroblast or the lipocyte phenotype,under the physiological retinal concentrations. Retinyl esters were the major metabolites, whose production was dependent upon both acyl-CoA:retinol acyltransferase (ARAT) and lecithin:retinol acyltransferase (LRAT). Lipocytes had a significantly higher esterification capacity than myofibroblasts. In order to distinguish the intrinsic enzyme activity from modulation of retinol uptake and CRBP-retinal content of the cytosol in the studied cells, we monitored enzyme kinetics in the purified microsomal fraction. We found that both LRAT and ARAT activities were induced during the conversion of myofibroblasts to lipocytes. LRAT induction was dependent upon retinoic acid,while that of ARAT was dependent upon the overall induction of the fat storing phenotype. The fatty acid composition of retinyl-esters suggested a preferential inclusion of exogenous fatty acids into retinyl esters. We conclude that both LRAT and ARAT participate in retinol esterification in hepatic stellate cells: LRAT's activity correlates with the vitamin A status, while ARAT depends upon the availability of fatty acyl-CoA and the overall lipid metabolism in hepatic stellate cells. (C) 2001 Elsevier Science Inc. Allrights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/04/20 alle ore 18:59:25