Signaling to localized degranulation in neutrophils adherent to immune complexes.
(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:
https://lup.lub.lu.se/record/107336
- author
- Nauclér, Claes LU ; Grinstein, Sergio ; Sundler, Roger LU and Tapper, Hans LU
- organization
- publishing date
- 2002
- 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
- John Wiley & Sons Inc.
- external identifiers
-
- wos:000174807800019
- pmid:11927658
- scopus:0036554394
- ISSN
- 1938-3673
- language
- English
- LU publication?
- yes
- additional info
- The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Division of Infection Medicine (BMC) (013024020), Macrophage Signalling (013212039)
- 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
- 2016-04-01 11:56:22
- date last changed
- 2022-01-26 20:27:17
@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}},
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}},
language = {{eng}},
number = {{4}},
pages = {{701--710}},
publisher = {{John Wiley & Sons Inc.}},
series = {{Journal of Leukocyte Biology}},
title = {{Signaling to localized degranulation in neutrophils adherent to immune complexes.}},
url = {{http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11927658&dopt=Abstract}},
volume = {{71}},
year = {{2002}},
}