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Titolo:
Stimulus-induced selective association of actin-associated proteins (alpha-actinin) and protein kinase C isoforms with the cytoskeleton of human neutrophils
Autore:
Niggli, V; Djafarzadeh, S; Keller, H;
Indirizzi:
Univ Bern, Dept Pathol, CH-3010 Bern, Switzerland Univ Bern Bern Switzerland CH-3010 ept Pathol, CH-3010 Bern, Switzerland
Titolo Testata:
EXPERIMENTAL CELL RESEARCH
fascicolo: 2, volume: 250, anno: 1999,
pagine: 558 - 568
SICI:
0014-4827(19990801)250:2<558:SSAOAP>2.0.ZU;2-X
Fonte:
ISI
Lingua:
ENG
Soggetto:
NADPH OXIDASE COMPLEX; OKADAIC ACID; POLYMORPHONUCLEAR LEUKOCYTES; PHOSPHATASE-ACTIVITY; CHEMOTACTIC FACTOR; FLUID PINOCYTOSIS; FILAMENT TURNOVER; PHORBOL ESTER; CALYCULIN-A; F-ACTIN;
Keywords:
neutrophils; cytoskeleton; alpha-actinin; protein kinase C; phosphatase 2A;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
38
Recensione:
Indirizzi per estratti:
Indirizzo: Niggli, V Univ Bern, Dept Pathol, Murtenstr 31, CH-3010 Bern, Switzerland Univ Bern Murtenstr 31 Bern Switzerland CH-3010 rn, Switzerland
Citazione:
V. Niggli et al., "Stimulus-induced selective association of actin-associated proteins (alpha-actinin) and protein kinase C isoforms with the cytoskeleton of human neutrophils", EXP CELL RE, 250(2), 1999, pp. 558-568

Abstract

We report a selective, differential stimulus-dependent enrichment of the actin-associated protein a-actinin and of isoforms of the signaling enzyme protein kinase C (PKC) in the neutrophil cytoskeleton. Chemotactic peptide, activators of PKC, and cell adhesion all induce a significant increase in the amount of cytoskeletal alpha-actinin and actin. Increased association ofPKC beta I and beta II with the cytoskeletal fraction of stimulated cells was also observed, with phorbol ester being more effective than chemotacticpeptide. A fraction of phosphatase 2A was constitutively associated with the cytoskeleton independent of cell activation. None of the stimuli promoted association of vinculin or myosin II with the cytoskeleton. Phosphatase inhibitors okadaic acid and calyculin A prevented increases in cytoskeletal actin, alpha-actinin, and PKC beta II induced by phorbol ester, suggesting the requirement for phosphatase activity in these events. Increases in cytoskeletal alpha-actinin and PKC beta II showed differing sensitivity to agents that prevent actin polymerization (cytochalasin D, latrunculin A). Latrunculin A (1 mu M) completely blocked PMA-induced increases in cytoskeletal alpha-actinin but reduced cytoskeletal recruitment of PHC beta II only by 16%. Higher concentrations of latrunculin A (4 mu M), which almost abolishedthe cytoskeletal actin pool, reduced cytoskeletal PKC beta II by 43%. In conclusion, a selective enrichment of cytoskeletal and signaling proteins inthe cytoskeleton of human neutrophils is induced by specific stimuli. (C) 1999 Academic Press.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 06/04/20 alle ore 21:28:54