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Titolo:
Activation of phospholipase D by PKC and GTP gamma S in human neuroblastoma cells overexpressing MARCKS
Autore:
Morash, SC; Byers, DM; Cook, HW;
Indirizzi:
Dalhousie Univ, Dept Pediat, Atlantic Res Ctr, Halifax, NS B3H 4H7, CanadaDalhousie Univ Halifax NS Canada B3H 4H7 Ctr, Halifax, NS B3H 4H7, Canada Dalhousie Univ, Dept Biochem, Halifax, NS B3H 4H7, Canada Dalhousie Univ Halifax NS Canada B3H 4H7 hem, Halifax, NS B3H 4H7, Canada Dalhousie Univ, Dept Mol Biol, Halifax, NS B3H 4H7, Canada Dalhousie UnivHalifax NS Canada B3H 4H7 iol, Halifax, NS B3H 4H7, Canada
Titolo Testata:
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR AND CELL BIOLOGY OF LIPIDS
fascicolo: 2-3, volume: 1487, anno: 2000,
pagine: 177 - 189
SICI:
1388-1981(20000927)1487:2-3<177:AOPDBP>2.0.ZU;2-3
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROTEIN-KINASE-C; ADP-RIBOSYLATION FACTOR; PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE; PHOSPHATIDIC-ACID; PHOSPHORYLATION SITES; MEMBRANE DOMAINS; PLASMA-MEMBRANE; GLIOMA-CELLS; RAT-BRAIN; IN-VIVO;
Keywords:
phospholipase D; myristoylated alanine-rich C kinase substrate; protein kinase C; SK-N-MC human neuroblastoma cells;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
52
Recensione:
Indirizzi per estratti:
Indirizzo: Cook, HW Dalhousie Univ, Dept Pediat, Atlantic Res Ctr, 5849 Univ Ave, Halifax, NS B3H 4H7, Canada Dalhousie Univ 5849 Univ Ave Halifax NS Canada B3H4H7 H7, Canada
Citazione:
S.C. Morash et al., "Activation of phospholipase D by PKC and GTP gamma S in human neuroblastoma cells overexpressing MARCKS", BBA-MOL C B, 1487(2-3), 2000, pp. 177-189

Abstract

Regulation of phospholipase D (PLD) activity participating in signal transduction involves complex interactions with small G-proteins (ARF, Rho) and protein kinase C isoforms (PKC alpha). In SK-N-MC human neuroblastoma cells, phorbol ester (TPA) activation of PLD was enhanced by overexpressing myristoylated alanine-rich C kinase substrate (MARCKS). To study MARCKS interactions with PLD, we investigated PLD isoform expression and activation by TPA and GTP gamma S in intact and digitonin-permeabilized clones transfected with MARCKS (M22). PLD2 was in both cytosol and membrane fractions while PLD1 was primarily membrane-associated in both vector control and M22 cells; location or quantities were unaltered by TPA treatment. TPA-stimulated PLD activity was higher in both intact and digitonin-permeabilized M22 cells than in vector controls. In contrast, GTP gamma S-stimulated PLD activity wasindependent of MARCKS expression but was additive with MARCKS-PKC-dependent activation in permeabilized cells. Combinations of PKC inhibition and downregulation in intact and permeabilized (with GTP gamma S present) cells indicated that a PKC-mediated phosphorylation event was necessary in intact cells without access to GTP gamma S, stimulation of PLD mediated by GTP gamma S was independent of PKC, and PLD activation by PKC in permeabilized cells was kinase-independent. Western blot analysis showed that MARCKS, PKC alpha, PLD1 and PLD2 were present in a detergent-insoluble fraction (DIF); GTPgamma S increased recovery of PLD2 in DIF. Disruption of cholesterol-rich DIFs with digitonin, cyclodextrin or filipin potentiated activation of PLD by TPA. Our studies suggest that activation of PLD by PKC requires MARCKS and can involve both phosphorylation-independent and -dependent processes. As PLD activation by GTP gamma S is PKC-MARCKS-independent, MARCKS may provide a fine tuning component in conjunction with G-protein-mediated mechanisms for regulation of PLD. (C) 2000 Elsevier Science B.V. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 08/04/20 alle ore 11:59:27