TY - JOUR
T1 - ß-glucan affects leukocyte navigation in a complex chemotactic gradient
AU - Tsikitis, Vassiliki L.
AU - Albina, Jorge E.
AU - Reichner, Jonathan S.
N1 - Copyright:
Copyright 2012 Elsevier B.V., All rights reserved.
PY - 2004/8
Y1 - 2004/8
N2 - Background Polymorphonuclear leukocytes (PMNs) must traverse endogenous chemotactic gradients (interleukin 8 [IL-8]) before reaching target chemoattractants (fMLP [N-formylmethionine-leucine-phenylalanine], C5a) produced at a site of bacterial infection. Complement receptor 3 (CR3; CD11b/CD18) contains 2 distinct binding sites, one that mediates adhesion and a lectin-like domain (LLD) that binds polysaccharides of microbial origin. This laboratory previously reported an increase in the chemotactic capacity of PMNs toward fMLP upon ligation of the CR3 LLD with β-glucan, a CR3 agonist. Current studies sought to determine the effect of β-glucan on PMN navigation toward other chemoattractants alone and in a competing chemotactic environment. Methods Migration was assessed by serum agarose overlay with the use of chambered slides containing or not, β-glucan. Migration of human PMNs at 37°C for 2 hours was evaluated toward C5a or IL-8 alone and in competing gradients. Selected groups were treated with anti-CR3-blocking antibodies. The number of chemotactic cells was quantified by microscopy. Results β-glucan significantly enhanced chemotaxis toward C5a and suppressed that toward IL-8 in a CR3-dependent fashion. In the competing chemotactic gradient assays (C5a vs IL-8), β-glucan further enhanced migration toward C5a while not affecting that toward IL-8. Conclusions β-glucan selectively upregulates PMN chemotaxis toward C5a while suppressing chemotaxis toward IL-8.
AB - Background Polymorphonuclear leukocytes (PMNs) must traverse endogenous chemotactic gradients (interleukin 8 [IL-8]) before reaching target chemoattractants (fMLP [N-formylmethionine-leucine-phenylalanine], C5a) produced at a site of bacterial infection. Complement receptor 3 (CR3; CD11b/CD18) contains 2 distinct binding sites, one that mediates adhesion and a lectin-like domain (LLD) that binds polysaccharides of microbial origin. This laboratory previously reported an increase in the chemotactic capacity of PMNs toward fMLP upon ligation of the CR3 LLD with β-glucan, a CR3 agonist. Current studies sought to determine the effect of β-glucan on PMN navigation toward other chemoattractants alone and in a competing chemotactic environment. Methods Migration was assessed by serum agarose overlay with the use of chambered slides containing or not, β-glucan. Migration of human PMNs at 37°C for 2 hours was evaluated toward C5a or IL-8 alone and in competing gradients. Selected groups were treated with anti-CR3-blocking antibodies. The number of chemotactic cells was quantified by microscopy. Results β-glucan significantly enhanced chemotaxis toward C5a and suppressed that toward IL-8 in a CR3-dependent fashion. In the competing chemotactic gradient assays (C5a vs IL-8), β-glucan further enhanced migration toward C5a while not affecting that toward IL-8. Conclusions β-glucan selectively upregulates PMN chemotaxis toward C5a while suppressing chemotaxis toward IL-8.
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U2 - 10.1016/j.surg.2004.05.014
DO - 10.1016/j.surg.2004.05.014
M3 - Article
C2 - 15300205
AN - SCOPUS:3843080856
SN - 0039-6060
VL - 136
SP - 384
EP - 389
JO - Surgery
JF - Surgery
IS - 2
ER -