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Titolo:
Disruption of beta(2)-integrin-cytoskeleton coupling abolishes the signaling capacity of these integrins on granulocytes
Autore:
Hellberg, C; Ydrenius, L; Axelsson, L; Andersson, T;
Indirizzi:
Univ Lund, Div Expt Pathol, Dept Lab Med, UMAS, Malmo, Sweden Univ Lund Malmo Sweden v Expt Pathol, Dept Lab Med, UMAS, Malmo, Sweden Linkoping Univ, Dept Cell Biol, S-58185 Linkoping, Sweden Linkoping Univ Linkoping Sweden S-58185 Biol, S-58185 Linkoping, Sweden
Titolo Testata:
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
fascicolo: 1, volume: 265, anno: 1999,
pagine: 164 - 169
SICI:
0006-291X(19991111)265:1<164:DOBCAT>2.0.ZU;2-5
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROTEIN-KINASE-C; LIGAND-RECEPTOR COMPLEXES; FORMYL PEPTIDE RECEPTORS; TUMOR-NECROSIS-FACTOR; GTP-BINDING PROTEINS; SRC FAMILY KINASES; HUMAN-NEUTROPHILS; TYROSINE PHOSPHORYLATION; ACTIN POLYMERIZATION; LEUKOCYTE ADHESION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
48
Recensione:
Indirizzi per estratti:
Indirizzo: Andersson, T Univ Lund, Malmo Univ Hosp, Div Expt Pathol, Entrance 78, S-20502 Malmo, Sweden Univ Lund Entrance 78 Malmo Sweden S-20502 502 Malmo, Sweden
Citazione:
C. Hellberg et al., "Disruption of beta(2)-integrin-cytoskeleton coupling abolishes the signaling capacity of these integrins on granulocytes", BIOC BIOP R, 265(1), 1999, pp. 164-169

Abstract

Integrin-dependent adhesion and dynamic modulations of the actin network are prerequisites for normal cell locomotion. To investigate whether the actin microfilamentous system does play a role in regulation of beta(2)-integrin-induced signalling, we pretreated granulocytes with staurosporine, a well-known protein kinase inhibitor that has also been shown to disrupt the cytoskeleton of intact cells. Pretreatment with staurosporine completely inhibited the beta(2-)integrin-induced Ca2+ signal and also its ability to trigger actin polymerisation. This inhibition was not related to phosphorylation of the CD18-chain of the beta(2)-integrin, nor to inhibition of protein kinases. Instead, association of beta(2)-integrins with the cortical cytoskeleton, which was observed in untreated cells, was abolished after exposure to staurosporine, indicating that beta(2)-integrin signalling depends on integrin-cytoskeleton interaction. These results suggest not only that the actin network provides an adhesive link to the extracellular matrix and a driving force for the locomotory response, but also that it participates in regulation of beta(2)-integrin signalling during granulocyte locomotion. (C) 1999 Academic Press.

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Documento generato il 16/07/20 alle ore 06:38:51