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Disruption of β2-integrin-cytoskeleton coupling abolishes the signaling capacity of these integrins on granulocytes

Hellberg, Carina; Ydrenius, Liselotte; Axelsson, Lena LU and Andersson, Tommy LU (1999) In Biochemical and Biophysical Research Communications 265(1). p.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 β2-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 β2-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 β2-integrin, nor to inhibition of protein kinases. Instead, association of... (More)

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 β2-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 β2-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 β2-integrin, nor to inhibition of protein kinases. Instead, association of β2-integrins with the cortical cytoskeleton, which was observed in untreated cells, was abolished after exposure to staurosporine, indicating that β2-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 β2-integrin signalling during granulocyte locomotion.

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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Biochemical and Biophysical Research Communications
volume
265
issue
1
pages
6 pages
publisher
Elsevier
external identifiers
  • Scopus:0033547461
ISSN
0006-291X
DOI
10.1006/bbrc.1999.1645
language
English
LU publication?
yes
id
ef4d0691-8ebc-4663-885a-7fac1172727c
date added to LUP
2017-03-10 13:02:18
date last changed
2017-03-10 13:02:18
@article{ef4d0691-8ebc-4663-885a-7fac1172727c,
  abstract     = {<p>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 β<sub>2</sub>-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 β<sub>2</sub>-integrin-induced Ca<sup>2+</sup> signal and also its ability to trigger actin polymerisation. This inhibition was not related to phosphorylation of the CD18-chain of the β<sub>2</sub>-integrin, nor to inhibition of protein kinases. Instead, association of β<sub>2</sub>-integrins with the cortical cytoskeleton, which was observed in untreated cells, was abolished after exposure to staurosporine, indicating that β<sub>2</sub>-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 β<sub>2</sub>-integrin signalling during granulocyte locomotion.</p>},
  author       = {Hellberg, Carina and Ydrenius, Liselotte and Axelsson, Lena and Andersson, Tommy},
  issn         = {0006-291X},
  language     = {eng},
  number       = {1},
  pages        = {164--169},
  publisher    = {Elsevier},
  series       = {Biochemical and Biophysical Research Communications},
  title        = {Disruption of β<sub>2</sub>-integrin-cytoskeleton coupling abolishes the signaling capacity of these integrins on granulocytes},
  url          = {http://dx.doi.org/10.1006/bbrc.1999.1645},
  volume       = {265},
  year         = {1999},
}