6th World Congress on Inflammation August 2-6, 2003 Vancouver, Canada

Vassiliki Tsikitis, Nicole Morin, Elizabeth Harrington, Jonathan Reichner. Rhode Island Hospital Dept. of Surgery, Brown University Medical School,
Providence, R.I

CR3 (CD11b/CD18) is unique among the leukocyte beta2 integrins because, apart from the ligand-binding I-domain, it contains a lectin-like domain.

Glucans are beta (1-3)-linked glucose polymers, which can bind to the CR3 lectin-like domain. Co-occupancy of the lectin-like domain with beta-glucan and the I-domain with fibronectin promotes neutrophil (PMN) chemotaxis.

The current study was undertaken to determine whether treatment of activated neutrophils with beta-glucan would alter PMN:endothelial cell interactions by a CR3-dependent mechanism. Electric Cell Substrate Impedance Sensing (ECIS) was used to evaluate the barrier function of an intact pulmonary capillary endothelial monolayer. Human PMNs were activated, or not, with formyl-met-leu-phe (fMLP), added to a confluent endothelial monolayer and barrier function was measured over time. Although activated PMNs induced a 60±5% (SEM) decrease in normalized monolayer resistance, addition of beta-glucan maintained optimal barrier function. Therefore, beta-glucan may protect endothelial barrier function in the presence of activated PMNs concerning inflammation.

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