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Rapid activation of Mac‐1(CD11b/CD18) molecules on macrophages by a new chemotactic factor ‘Gasserokine’ produced by Lactobacillus gasseri JCM1131 T
Author(s) -
KITAZAWA Haruki,
INO Tomohiko,
KAWAI Yasushi,
ITOH Takatoshi,
SAITO Tadao
Publication year - 2002
Publication title -
animal science journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.606
H-Index - 38
eISSN - 1740-0929
pISSN - 1344-3941
DOI - 10.1046/j.1344-3941.2002.00055.x
Subject(s) - phosphorylation , chemotaxis , tyrosine phosphorylation , lactobacillus gasseri , cd18 , microbiology and biotechnology , integrin alpha m , biology , macrophage , biochemistry , chemistry , cell , lactobacillus , receptor , in vitro , fermentation
The chemoattractant activity of a new chemotactic factor, ‘Gasserokine’ produced by Lactobacillus gasseri JCM1131 T , has been proposed as a novel immunological function of probiotic lactic acid bacteria. The focus of the present study was to understand the mechanism of the chemotaxis induced by Gasserokine, using activation of an adhesion molecule, Mac‐1 (CD11b/CD18) on macrophages. The macrophage chemotaxis to Gasserokine was abolished by preincubation of macrophages with the anti‐Mac‐1 mAb. Gasserokine induced rapid serine phosphorylation of CD18 molecules within 1 min of stimulation, but the effect was short‐lived. Substantial tyrosine phosphorylation was observed in CD18‐associated protein of macrophages stimulated by Gasserokine. The tyrosine phosphorylation was confirmed in macrophages stimulated with Gasserokine and also serine/threonine phosphorylation was detected on CD18 molecules by laser microscopy using a double immunostaining method. These results suggest that selective activation of intracellular signaling cascades, such as the mitogen‐activated protein kinase pathway, are related to the macrophage chemotaxis induced by Gasserokine.