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. 1996 Feb 16;271(5251):981-3.
doi: 10.1126/science.271.5251.981.

Role of Rho in chemoattractant-activated leukocyte adhesion through integrins

C Laudanna  1 , J J Campbell, E C Butcher
Affiliations

Role of Rho in chemoattractant-activated leukocyte adhesion through integrins

C Laudanna et al. Science. .

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 alpha4beta1 adhesion to vascular cell adhesion molecule-1 and neutrophil beta2 integrin adhesion to fibrinogen. These findings suggest that Rho participates in signaling from chemoattractant receptors to trigger rapid adhesion in leukocytes.

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