Abstract
Heterotrimeric guanine nucleotide binding protein (G protein)-linked receptors of the chemoattractant subfamily can trigger adhesion through leukocyte integrins, and in this role they are thought to regulate immune cell-cell interactions and trafficking. In lymphoid cells transfected with formyl peptide or interleukin-8 receptors, agonist stimulation activated nucleotide exchange on the small guanosine triphosphate-binding protein RhoA in seconds. Inactivation of Rho by C3 transferase exoenzyme blocked agonist-induced lymphocyte α4β1 adhesion to vascular cell adhesion molecule-1 and neutrophil β2 integrin adhesion to fibrinogen. These findings suggest that Rho participates in signaling from chemoattractant receptors to trigger rapid adhesion in leukocytes.
Keywords
Cell biologyIntegrinCell adhesionCell adhesion moleculeChemistryRHOAHeterotrimeric G proteinChemotaxisReceptorBiologySignal transductionBiochemistryG proteinCell
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Publication Info
- Year
- 1996
- Type
- article
- Volume
- 271
- Issue
- 5251
- Pages
- 981-983
- Citations
- 487
- Access
- Closed
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Cite This
Carlo Laudanna,
James J. Campbell,
Eugene C. Butcher
(1996).
Role of Rho in Chemoattractant-Activated Leukocyte Adhesion Through Integrins.
Science
, 271
(5251)
, 981-983.
https://doi.org/10.1126/science.271.5251.981
Identifiers
- DOI
- 10.1126/science.271.5251.981