The adhesion receptor CD-31 can be primed to rapidly adjust the neutrophil cytoskeleton.
(2002) In Biochemical and Biophysical Research Communications 292(4). p.1092-1097- Abstract
- The adhesion receptor CD-31 is expressed on neutrophils and endothelial cells and participates in transendothelial migration of neutrophils. Although necessary, information on CD-31-induced signaling and its influence on the shape-forming actin network is scarce. Here, we found that antibody engagement of CD-31 on suspended neutrophils triggered a prompt intracellular Ca(2+) signal, providing the cells had been primed with a chemotactic factor. Inhibition of Src-tyrosine kinases blocked this Ca(2+) signal, but not a fMet-Leu-Phe-induced Ca(2+) signal. Despite the ability of fMet-Leu-Phe to activate Src-tyrosine kinases, it did not per se induce tyrosine phosphorylation of CD-31. However, fMet-Leu-Phe did enable such a phosphorylation... (More)
- The adhesion receptor CD-31 is expressed on neutrophils and endothelial cells and participates in transendothelial migration of neutrophils. Although necessary, information on CD-31-induced signaling and its influence on the shape-forming actin network is scarce. Here, we found that antibody engagement of CD-31 on suspended neutrophils triggered a prompt intracellular Ca(2+) signal, providing the cells had been primed with a chemotactic factor. Inhibition of Src-tyrosine kinases blocked this Ca(2+) signal, but not a fMet-Leu-Phe-induced Ca(2+) signal. Despite the ability of fMet-Leu-Phe to activate Src-tyrosine kinases, it did not per se induce tyrosine phosphorylation of CD-31. However, fMet-Leu-Phe did enable such a phosphorylation following an antibody-induced engagement of CD-31. This clustering also triggered a Ca(2+)-dependent depolymerization of actin and, surprisingly enough, a simultaneous polymerization. The ability of CD-31 to signal dynamic alterations in the cytoskeleton, particularly the Ca(2+)-induced actin depolymerization, further explains how neutrophils can squeeze themselves out between adjacent endothelial cells. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/107589
- author
- Dimitrijevic, Ivan LU ; Axelsson, Lena LU and Andersson, Tommy LU
- organization
- publishing date
- 2002
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- CD31 : drug effects, Antigens, Antibodies : pharmacology, Actins : metabolism, Cytoskeleton : metabolism, Enzyme Inhibitors : pharmacology, Human, Intracellular Fluid : metabolism, N-Formylmethionine Leucyl-Phenylalanine : pharmacology, Neutrophils : cytology, Neutrophils : metabolism, Phosphorylation : drug effects, Signal Transduction : drug effects, Signal Transduction : physiology, Support, Non-U.S. Gov't, src-Family Kinases : antagonists & inhibitors, CD31 : metabolism, Calcium : metabolism, Calcium Signaling : drug effects, Cell Adhesion : physiology, Cell Movement : physiology, Chemotactic Factors : pharmacology
- in
- Biochemical and Biophysical Research Communications
- volume
- 292
- issue
- 4
- pages
- 1092 - 1097
- publisher
- Elsevier
- external identifiers
-
- wos:000175171800047
- pmid:11944928
- scopus:0036298947
- ISSN
- 1090-2104
- DOI
- 10.1006/bbrc.2002.6773
- language
- English
- LU publication?
- yes
- id
- 046354a0-1c08-45b1-ad31-7501821670a4 (old id 107589)
- alternative location
- http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11944928&dopt=Abstract
- date added to LUP
- 2016-04-01 17:06:28
- date last changed
- 2024-01-26 18:20:38
@article{046354a0-1c08-45b1-ad31-7501821670a4,
abstract = {{The adhesion receptor CD-31 is expressed on neutrophils and endothelial cells and participates in transendothelial migration of neutrophils. Although necessary, information on CD-31-induced signaling and its influence on the shape-forming actin network is scarce. Here, we found that antibody engagement of CD-31 on suspended neutrophils triggered a prompt intracellular Ca(2+) signal, providing the cells had been primed with a chemotactic factor. Inhibition of Src-tyrosine kinases blocked this Ca(2+) signal, but not a fMet-Leu-Phe-induced Ca(2+) signal. Despite the ability of fMet-Leu-Phe to activate Src-tyrosine kinases, it did not per se induce tyrosine phosphorylation of CD-31. However, fMet-Leu-Phe did enable such a phosphorylation following an antibody-induced engagement of CD-31. This clustering also triggered a Ca(2+)-dependent depolymerization of actin and, surprisingly enough, a simultaneous polymerization. The ability of CD-31 to signal dynamic alterations in the cytoskeleton, particularly the Ca(2+)-induced actin depolymerization, further explains how neutrophils can squeeze themselves out between adjacent endothelial cells.}},
author = {{Dimitrijevic, Ivan and Axelsson, Lena and Andersson, Tommy}},
issn = {{1090-2104}},
keywords = {{CD31 : drug effects; Antigens; Antibodies : pharmacology; Actins : metabolism; Cytoskeleton : metabolism; Enzyme Inhibitors : pharmacology; Human; Intracellular Fluid : metabolism; N-Formylmethionine Leucyl-Phenylalanine : pharmacology; Neutrophils : cytology; Neutrophils : metabolism; Phosphorylation : drug effects; Signal Transduction : drug effects; Signal Transduction : physiology; Support; Non-U.S. Gov't; src-Family Kinases : antagonists & inhibitors; CD31 : metabolism; Calcium : metabolism; Calcium Signaling : drug effects; Cell Adhesion : physiology; Cell Movement : physiology; Chemotactic Factors : pharmacology}},
language = {{eng}},
number = {{4}},
pages = {{1092--1097}},
publisher = {{Elsevier}},
series = {{Biochemical and Biophysical Research Communications}},
title = {{The adhesion receptor CD-31 can be primed to rapidly adjust the neutrophil cytoskeleton.}},
url = {{http://dx.doi.org/10.1006/bbrc.2002.6773}},
doi = {{10.1006/bbrc.2002.6773}},
volume = {{292}},
year = {{2002}},
}