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Titolo:
STIMULUS-INDUCED DISSOCIATION OF ALPHA-SUBUNITS OF HETEROTRIMERIC GTP-BINDING PROTEINS FROM THE CYTOSKELETON OF HUMAN NEUTROPHILS
Autore:
SARNDAHL E; BOKOCH GM; STENDAHL O; ANDERSSON T;
Indirizzi:
LINKOPING UNIV,DEPT MED MICROBIOL S-58185 LINKOPING SWEDEN LINKOPING UNIV,DEPT CELL BIOL S-58185 LINKOPING SWEDEN SCRIPPS CLIN & RES FDN,RES INST,DEPT IMMUNOL LA JOLLA CA 92037 SCRIPPS CLIN & RES FDN,RES INST,DEPT CELL BIOL LA JOLLA CA 92037
Titolo Testata:
Proceedings of the National Academy of Sciences of the United Statesof America
fascicolo: 14, volume: 90, anno: 1993,
pagine: 6552 - 6556
SICI:
0027-8424(1993)90:14<6552:SDOAOH>2.0.ZU;2-D
Fonte:
ISI
Lingua:
ENG
Soggetto:
LIGAND-RECEPTOR COMPLEXES; HUMAN-GRANULOCYTES; ACTIN POLYMERIZATION; PLASMA-MEMBRANE; ASSOCIATION; TRANSIENT; PROFILIN;
Keywords:
SIGNAL TRANSDUCTION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
24
Recensione:
Indirizzi per estratti:
Citazione:
E. Sarndahl et al., "STIMULUS-INDUCED DISSOCIATION OF ALPHA-SUBUNITS OF HETEROTRIMERIC GTP-BINDING PROTEINS FROM THE CYTOSKELETON OF HUMAN NEUTROPHILS", Proceedings of the National Academy of Sciences of the United Statesof America, 90(14), 1993, pp. 6552-6556

Abstract

Previous studies on the mechanism responsible for terminating the generation of second messengers induced by chemotactic factor-receptor complexes have, on one hand, suggested a direct role of a GTP-binding protein(s) (G protein), and, on the other hand, proposed that there is alateral segregation of the ligand-receptor complexes into G protein-depleted domains of the plasma membrane. In the present investigation, which addresses these apparently contradictory findings, we found thata substantial part of the alpha subunits of the G(n) protein (G(nalpha)) in unstimulated neutrophils were associated with a cytoskeletal fraction and that release of these subunits occurred upon stimulation with the chemotactic factor fMet-Leu-Phe. An identical G(nalpha)) release could also be induced by direct activation of G proteins with guanosine 5'-[gamma-thio]triphosphate or AIF4-. In contrast, the alpha subunits of the stimulatory G-protein (G(salpha)) also found associated with the cytoskeletal fraction of unstimulated cells were not released byfMet-Leu-Phe stimulation. However, they were effectively released by direct G-protein activation with guanosine 5'-[gamma-thio]triphosphate. In addition, inhibition of the fMet-Leu-Phe-stimulated modulation ofthe actin network by pertussis toxin did not affect the fMet-Leu-Phe-induced release of G(nalpha) from the cytoskeletal fraction. These observations indicate that fMet-Leu-Phe-induced activation of neutrophilsinvolves a specific dissociation of G(nalpha) from the cytoskeleton and that this release is not a consequence of the well-known effect of fMet-Leu-Phe on the cytoskeleton of neutrophils. The present data contribute ideas concerning the transducing properties of G proteins in cellular signaling and seem to reconcile the apparently contradictory concepts of how the cytoskeleton participates in the termination of the chemotactic-factor-induced generation of second messengers in human neutrophils.

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Documento generato il 16/07/20 alle ore 06:41:28