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Titolo:
POSTTRANSCRIPTIONAL REGULATION OF APOLIPOPROTEIN-E EXPRESSION IN MOUSE MACROPHAGES BY PHORBOL ESTER
Autore:
DORY L;
Indirizzi:
UNIV TENNESSEE CTR HLTH SCI,DEPT PHARMACOL,874 UNION AVE MEMPHIS TN 38163
Titolo Testata:
Biochemical journal
, volume: 292, anno: 1993,
parte:, 1
pagine: 105 - 111
SICI:
0264-6021(1993)292:<105:PROAEI>2.0.ZU;2-9
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROTEIN KINASE-C; MURINE PERITONEAL-MACROPHAGES; E-GENE-EXPRESSION; HUMAN MONOCYTE-MACROPHAGES; E MESSENGER-RNA; LIPOPROTEIN-LIPASE; 3T3-L1 ADIPOCYTES; APOPROTEIN-E; RAT-LIVER; CELL-LINE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
48
Recensione:
Indirizzi per estratti:
Citazione:
L. Dory, "POSTTRANSCRIPTIONAL REGULATION OF APOLIPOPROTEIN-E EXPRESSION IN MOUSE MACROPHAGES BY PHORBOL ESTER", Biochemical journal, 292, 1993, pp. 105-111

Abstract

Phorbol ester-mediated differentiation of THP-1 cells (a human monocytic cell line) into mature macrophages is associated with a transcriptional induction of apolipoprotein E (apoE) expression [Auwerx, Deeb, Brunzell, Peng and Chait (1988) Biochemistry 27, 2651-2655]. Endotoxin,on the other hand, which may also act through activation of protein kinase C, is a potent inhibitor of apoE expression in mouse macrophages[Werb and Chin (1983)J. Biol. Chem. 258, 10642-10648]. The present experiments examine the effect of phorbol ester, an activator of proteinkinase C, on the apoE expression in mouse thioglycollate-elicited peritoneal macrophages. Phorbol ester inhibits apoE expression in a specific, time- and dose-dependent manner. A 75 % inhibition in the rate ofapoE secretion, but not that of total protein, was observed followinga 4.5 h incubation with 160 nM phorbol ester, although nearly full inhibition was obtained with 40 nM. The changes in apoE secretion were paralleled by similar changes in apoE synthesis, indicating synthesis as the primary site of action. The decreased rates of apoE synthesis are shown not to be due to increased apoE degradation. The profound inhibition of apoE synthesis was not accompanied by significant changes inapoE mRNA levels at any concentration of phorbol ester (up to 16 muM), or length of treatment (up to 24 h), suggesting a post-transcriptional locus of regulation of apoE expression. Although the early changes in apoE synthesis correlate with increased microsomal protein kinase Cactivity, the suppression of apoE expression persists even during conditions of nearly complete (> 95 %) loss of protein kinase C activity,suggesting that the direct or indirect effect of protein kinase C on apoE expression is mediated by a stable phosphorylated protein, or that the observed effects are mediated through a protein kinase C speciesthat is not readily downregulated by phorbol esters. The presented studies clearly demonstrate the potential importance of the translational regulation of apoE expression through the protein kinase C signal transduction pathway.

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Documento generato il 25/02/20 alle ore 11:17:19