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Titolo:
OXIDIZED LOW-DENSITY-LIPOPROTEIN STIMULATES PROTEIN-KINASE-C (PKC) AND INDUCES EXPRESSION OF PKC-ISOTYPES VIA PROSTAGLANDIN-H-SYNTHASE IN P388D(1) MACROPHAGE-LIKE CELLS
Autore:
CLAUS R; FYRNYS B; DEIGNER HP; WOLF G;
Indirizzi:
UNIV HEIDELBERG,INST PHARMAZEUT CHEM,NEUENHEIMER FELD 364 D-69120 HEIDELBERG GERMANY UNIV HEIDELBERG,INST PHARMAZEUT CHEM D-69120 HEIDELBERG GERMANY
Titolo Testata:
Biochemistry
fascicolo: 15, volume: 35, anno: 1996,
pagine: 4911 - 4922
SICI:
0006-2960(1996)35:15<4911:OLSP(A>2.0.ZU;2-G
Fonte:
ISI
Lingua:
ENG
Soggetto:
RECEPTOR-MEDIATED ENDOCYTOSIS; MURINE PERITONEAL-MACROPHAGES; ARACHIDONIC-ACID METABOLISM; HUMAN MONOCYTE-MACROPHAGES; SCAVENGER-RECEPTOR; BACTERIAL LIPOPOLYSACCHARIDE; TYROSINE KINASES; ACTIVATION; SUBSTRATE; ENDOTOXIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
81
Recensione:
Indirizzi per estratti:
Citazione:
R. Claus et al., "OXIDIZED LOW-DENSITY-LIPOPROTEIN STIMULATES PROTEIN-KINASE-C (PKC) AND INDUCES EXPRESSION OF PKC-ISOTYPES VIA PROSTAGLANDIN-H-SYNTHASE IN P388D(1) MACROPHAGE-LIKE CELLS", Biochemistry, 35(15), 1996, pp. 4911-4922

Abstract

Treatment of cells with LPS-free oxLDL significantly enhanced proteinkinase C (PKC) activity in cell extracts from P383D(1) macrophage-like cells as determined by phosphorylation of histone H1 or Ac-MBP[4-14]substrate peptide. This effect was abolished by the PKC inhibitors H-7 and bisindolylmaleimide I while pertussis toxin failed to block stimulation. The phosphotransferase activity was also increased by acetylated LDL (acLDL) and maleylated albumin (malBSA), the oxLDL effect was inhibited by chloroquine which also blocked oxLDL-induced stimulation of tyrosine kinase activity. Marginal stimulation of PKC activity was observed when lipid extracts from oxLDL were used, indicating that uptake via scavenger receptors (SR) is mandatory. Polyinosinic acid (polyI) exhibited a concentration-dependent inhibition of the oxLDL-induced effect suggesting that SR II/I but not CD36 interactions are critical to PKC activation. Modified (lipo)proteins increased the concentration of diacylglycerol and differentially affected the levels of individual PKC isoenzymes predominantly in the cytosolic fraction. Changes ofactivity induced by oxLDL could be primarily assigned to alterations of the activities and levels of the isoenzymes beta and delta. Treatment with oxLDL, acLDL, and malBSA was also accompanied by increased production of prostaglandins as well as by an enhanced level of cyclooxygenase 2 (COX 2) as determined by Western blot analysis. Effecs of oxLDL on PKC activity/expression was supressed by the cyclooxygenase inhibitors indomethacin, by pre-exposure to the inhibitor of both lipoxygenase and cyclooxygenase, yl)-7-phenyl-2,2-dihydro-1H-pyrrolizine-5-ylacetic acid (ML 3000), and by treatment with the specific COX 2-inhibitor -(2-cyclohexyloxy-4-nitrophenyl)methanesulfonamide (NS-398). These results indicate that oxLDL, acLDL, and malBSA exhibit a COX 2-dependent and isotype specific effect on PKC in P388D(1) cells following uptake via SR II/I and subsequent lysosomal degradation.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/02/20 alle ore 09:07:10