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The adhesion receptor CD-31 can be primed to rapidly adjust the neutrophil cytoskeleton.

Dimitrijevic, Ivan LU ; Axelsson, Lena LU and Andersson, Tommy LU (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)
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@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},
  keyword      = {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},
  volume       = {292},
  year         = {2002},
}