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Titolo:
EFFECT OF CONTINUOUS PHORBOL ESTER TREATMENT ON MUSCARINIC RECEPTOR-MEDIATED CALMODULIN REDISTRIBUTION IN SK-N-SH NEUROBLASTOMA-CELLS
Autore:
SHARIATMADAR Z; GOLDSMITH AM; GNEGY ME;
Indirizzi:
UNIV MICHIGAN,DEPT PHARMACOL,SCH MED,2220E MSRB 3 ANN ARBOR MI 48109 UNIV MICHIGAN,DEPT PHARMACOL,SCH MED ANN ARBOR MI 48109
Titolo Testata:
Journal of neurochemistry
fascicolo: 1, volume: 68, anno: 1997,
pagine: 40 - 46
SICI:
0022-3042(1997)68:1<40:EOCPET>2.0.ZU;2-A
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROTEIN-KINASE-C; NEURO-BLASTOMA CELLS; TYROSINE PHOSPHORYLATION; HUMAN PLATELETS; DIFFERENTIATION; EXPRESSION; INCREASE; GROWTH; INHIBITORS; ENTRY;
Keywords:
TRANSLOCATION; PROTEIN KINASE C; MYRISTOYLATED ALANINE-RICH C KINASE SUBSTRATE; CARBACHOL; DIFFERENTIATION; 43-KDA GROWTH-ASSOCIATED PROTEIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
38
Recensione:
Indirizzi per estratti:
Citazione:
Z. Shariatmadar et al., "EFFECT OF CONTINUOUS PHORBOL ESTER TREATMENT ON MUSCARINIC RECEPTOR-MEDIATED CALMODULIN REDISTRIBUTION IN SK-N-SH NEUROBLASTOMA-CELLS", Journal of neurochemistry, 68(1), 1997, pp. 40-46

Abstract

Stimulation of muscarinic receptors by carbachol and activation of protein kinase C elicits the translocation of calmodulin (CaM) from membranes to cytosol in the human neuroblastoma cell line SK-N-SH, Our previous studies have suggested a role for protein kinase C in the regulation of CaM redistribution, To explore further the role of protein kinase C in carbachol-induced calmodulin translocation, we treated cells for 17 h with 12-O-tetradecanoylphorbol 13-acetate (TPA) to down-regulate protein kinase C isozymes or 72 h to differentiate the cells, Treatment of SK-N-SH cells for 17 h with 70 nM TPA nearly abolished the effect of carbachol on CaM redistribution. After 72 h of TPA, however, the cells appeared differentiated, and the ability of carbachol to increase cytosolic CaM levels was restored. In untreated control cells, the carbachol-mediated increase in cytosolic CaM content was mimicked byTPA and blocked by pretreatment with the selective protein kinase C inhibitor Po 31-8220 at 10 mu M. In the 72-h TPA-treated cells, however, the ability of TPA to increase cytosolic CaM levels was significantly reduced, and the action of carbachol was no longer blocked by Po 31-8220, The effect of prolonged TPA treatment on select protein kinase Cisozymes was examined by immunoblotting, Treatment of cells for either 17 or 72 h abolished the alpha-isozyme in the cytosol and reduced (17 h) or abolished (72 h) the content in the membranes. In both 17- and72-h TPA-treated cells, the E-isozyme was nearly abolished in the cytosol and slightly reduced in the membranes. Some protein kinase C activity may have been maintained during TPA treatment because the basal level of phosphorylation of the protein kinase C substrate myristoylated alanine-rich C kinase substrate was enhanced in cells treated for either 17 or 72 h with TPA. The potential dissociation of carbachol and protein kinase C in eliciting increases in cytosolic CaM content was afunction of prolonged TPA treatment and not differentiation per se because carbachol-mediated increases in cytosolic CaM levels were inhibited by Ro 31-8220 in retinoic acid-differentiated SK-N-SH cells. This study demonstrates that continuous TPA treatment, although initially down-regulating the protein kinase C-mediated effect of carbachol on CaM redistribution, uncouples carbachol and protein kinase C at longer times.

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Documento generato il 04/04/20 alle ore 09:06:53