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Signaling to localized degranulation in neutrophils adherent to immune complexes.

Nauclér, Claes LU ; Grinstein, Sergio; Sundler, Roger LU and Tapper, Hans LU (2002) In Journal of Leukocyte Biology 71(4). p.701-710
Abstract
The present study demonstrates that the secretion of azurophilic granules occurring during Fc receptor-mediated attachment and spreading of neutrophils is highly localized to the adhering region of the cell. In contrast, the secretion of specific granules occurs in a nonpolarized way. This implies that unique signals are involved in the regulation of azurophilic degranulation. Assembly of actin filaments, as visualized by staining with rhodamine phalloidin, neither hindered nor facilitated degranulation. Further, the azurophilic secretory response remained localized in the presence of cytochalasin B. Release of azurophilic-granule content was inhibited by genistein and erbstatin, inhibitors of tyrosine kinases, and by GF109203X, a protein... (More)
The present study demonstrates that the secretion of azurophilic granules occurring during Fc receptor-mediated attachment and spreading of neutrophils is highly localized to the adhering region of the cell. In contrast, the secretion of specific granules occurs in a nonpolarized way. This implies that unique signals are involved in the regulation of azurophilic degranulation. Assembly of actin filaments, as visualized by staining with rhodamine phalloidin, neither hindered nor facilitated degranulation. Further, the azurophilic secretory response remained localized in the presence of cytochalasin B. Release of azurophilic-granule content was inhibited by genistein and erbstatin, inhibitors of tyrosine kinases, and by GF109203X, a protein kinase C (PKC) inhibitor. We could also demonstrate a relative enrichment of syk tyrosine kinase and the PKC isoforms alpha and beta1 in adherent plasma membranes. (Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Cell Adhesion, Cell Degranulation, Cytochalasin B : pharmacology, Enzyme Precursors : analysis, Human, Isoenzymes : analysis, Protein Kinase C : analysis, Neutrophils : physiology, Protein Kinase C : physiology, Protein-Tyrosine Kinase : analysis, Protein-Tyrosine Kinase : physiology, Antigen-Antibody Complex : physiology, Actins : metabolism
in
Journal of Leukocyte Biology
volume
71
issue
4
pages
701 - 710
publisher
Society for Leukocyte Biology
external identifiers
  • wos:000174807800019
  • pmid:11927658
  • scopus:0036554394
ISSN
1938-3673
language
English
LU publication?
yes
id
2d5d1878-93b5-4244-8107-c0760415caa9 (old id 107336)
alternative location
http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11927658&dopt=Abstract
date added to LUP
2007-07-05 08:45:37
date last changed
2017-01-01 04:41:06
@article{2d5d1878-93b5-4244-8107-c0760415caa9,
  abstract     = {The present study demonstrates that the secretion of azurophilic granules occurring during Fc receptor-mediated attachment and spreading of neutrophils is highly localized to the adhering region of the cell. In contrast, the secretion of specific granules occurs in a nonpolarized way. This implies that unique signals are involved in the regulation of azurophilic degranulation. Assembly of actin filaments, as visualized by staining with rhodamine phalloidin, neither hindered nor facilitated degranulation. Further, the azurophilic secretory response remained localized in the presence of cytochalasin B. Release of azurophilic-granule content was inhibited by genistein and erbstatin, inhibitors of tyrosine kinases, and by GF109203X, a protein kinase C (PKC) inhibitor. We could also demonstrate a relative enrichment of syk tyrosine kinase and the PKC isoforms alpha and beta1 in adherent plasma membranes.},
  author       = {Nauclér, Claes and Grinstein, Sergio and Sundler, Roger and Tapper, Hans},
  issn         = {1938-3673},
  keyword      = {Cell Adhesion,Cell Degranulation,Cytochalasin B : pharmacology,Enzyme Precursors : analysis,Human,Isoenzymes : analysis,Protein Kinase C : analysis,Neutrophils : physiology,Protein Kinase C : physiology,Protein-Tyrosine Kinase : analysis,Protein-Tyrosine Kinase : physiology,Antigen-Antibody Complex : physiology,Actins : metabolism},
  language     = {eng},
  number       = {4},
  pages        = {701--710},
  publisher    = {Society for Leukocyte Biology},
  series       = {Journal of Leukocyte Biology},
  title        = {Signaling to localized degranulation in neutrophils adherent to immune complexes.},
  volume       = {71},
  year         = {2002},
}