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Published online before print May 2, 2006

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(Journal of Leukocyte Biology. 2006;80:204-211.)
© 2006 by Society for Leukocyte Biology

Induction of human neutrophil chemotaxis by Candida albicans-derived ß-1,6-long glycoside side-chain-branched ß-glucan

Tadashi Sato^*,, Kazuhisa Iwabuchi^*,,1, Isao Nagaoka, Yoshiyuki Adachi^¶, Naohito Ohno^¶, Hiroshi Tamura^||, Kuniaki Seyama, Yoshinosuke Fukuchi, Hitoshi Nakayama^*, Fumiko Yoshizaki^*, Kenji Takamori^* and Hideoki Ogawa^*

^* Institute for Environmental and Gender-Specific Medicine, Departments of
Respiratory Medicine and
Host Defense and Biochemical Research, Juntendo University Graduate School of Medicine, Tokyo, Japan;
Laboratory of Biochemistry, Juntendo University School of Health Care and Nursing, Chiba, Japan;
^¶ Laboratory for Immunopharmacology of Microbial Products, School of Pharmacy, Tokyo University of Pharmacy and Life Science, Japan; and
^|| Seikagaku Corporation, Tokyo, Japan

¹ Correspondence: Institute for Environmental and Gender-Specific Medicine, Juntendo University Graduate School of Medicine, 2-1-1 Tomioka Urayasu-shi, Chiba 279-0021, Japan. E-mail: iwabuchi{at}med.juntendo.ac.jp

Polysaccharide ß-1,3-D-glucans (ß-glucans) are components of the cell wall of various fungi and show immunomodulatory activities. ß-Glucans have been reported to enhance neutrophil accumulation during pathogenic fungi-induced lung inflammation. Therefore, we examined whether ß-glucans themselves possess chemotactic activities for human neutrophils. Among several kinds of ß-glucans, ß-1,6-long glucosyl side-chain-branched ß-glucan, isolated from Candida albicans [Candida soluble ß-D-glucan (CSBG)], dose-dependently induced neutrophil migration in a Boyden chamber system. In contrast, 1,6-monoglucosyl-branched ß-glucans, such as Sparassis crispa-derived ß-glucan (SCG) and grifolan (GRN), which were derived from nonpathogenic fungi, hardly induced neutrophil migration. Moreover, CSBG-induced neutrophil migration was inhibited completely by liposomes containing neutral glycosphingolipid lactosylceramide (LacCer; Galß1-4Glc-ceramide) but not NeuAc2-3Galß1-4Glcß1-1'-Cer ganglioside. Furthermore, binding experiments demonstrated that CSBG bound to glycosphingolipids (such as LacCer) with a terminal galactose residue; however, SCG and GRN (1,6-monoglucosyl-branched ß-glucans) did not bind to LacCer. It is important that a Src kinase inhibitor protein phosphatase 1, a phosphatidylinositol-3 kinase (PI-3K) inhibitor wortmannin, and a G_i/o inhibitor pertussis toxin inhibited neutrophil migration toward CSBG. Taken together, our results suggest that ß-1,6-long glucosyl side-chain-branched ß-glucan CSBG binds to LacCer and induces neutrophil migration through the activation of Src family kinase/PI-3K/heterotrimeric G-protein signal transduction pathways.

Key Words: lactosylceramide • lipid raft • galactose

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