Disruption of beta(2)-integrin-cytoskeleton coupling abolishes the signaling capacity of these integrins on granulocytes

Research output: Contribution to journalArticlepeer-review

Standard

Disruption of beta(2)-integrin-cytoskeleton coupling abolishes the signaling capacity of these integrins on granulocytes. / Hellberg, C; Ydrenius, L; Axelsson, L; Andersson, T; Hellberg, Karina.

In: Biochemical and Biophysical Research Communications, Vol. 265, No. 1, 1999, p. 164-9.

Research output: Contribution to journalArticlepeer-review

Harvard

APA

Vancouver

Author

Bibtex

@article{ced3a220f0e14dd1a40168127bc1da92,
title = "Disruption of beta(2)-integrin-cytoskeleton coupling abolishes the signaling capacity of these integrins on granulocytes",
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 Ca(2+) 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.",
author = "C Hellberg and L Ydrenius and L Axelsson and T Andersson and Karina Hellberg",
note = "Copyright 1999 Academic Press.",
year = "1999",
doi = "10.1006/bbrc.1999.1645",
language = "English",
volume = "265",
pages = "164--9",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Elsevier",
number = "1",

}

RIS

TY - JOUR

T1 - Disruption of beta(2)-integrin-cytoskeleton coupling abolishes the signaling capacity of these integrins on granulocytes

AU - Hellberg, C

AU - Ydrenius, L

AU - Axelsson, L

AU - Andersson, T

AU - Hellberg, Karina

N1 - Copyright 1999 Academic Press.

PY - 1999

Y1 - 1999

N2 - 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 Ca(2+) 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.

AB - 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 Ca(2+) 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.

U2 - 10.1006/bbrc.1999.1645

DO - 10.1006/bbrc.1999.1645

M3 - Article

C2 - 10548508

VL - 265

SP - 164

EP - 169

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 1

ER -