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(Journal of Leukocyte Biology. 2002;71:205-211.)
© 2002 by Society for Leukocyte Biology

Cross-linking of GPI-80, a possible regulatory molecule of cell adhesion, induces up-regulation of CD11b/CD18 expression on neutrophil surfaces and shedding of L-selectin

Department of Immunology and Parasitology, Yamagata University School of Medicine, Yamagata, Japan

Correspondence: Fujiro Sendo, Department of Immunology and Parasitology, Yamagata University School of Medicine, 2-2-2, Iida-Nishi, Yamagata, 990-9585, Japan. E-mail: fsendo{at}med.id.yamagata-u.ac.jp

Previously, we described a novel glycosylphosphatidyl inositol (GPI)-anchored glycoprotein (designated GPI-80) on human neutrophils and monocytes that may regulate ß₂ integrin-dependent neutrophil adherence and migration. However, the mechanism regulating ß₂ integrin remains to be clarified. To study this, we examined changes in ß₂ integrin expression and function caused by cross-linking GPI-80. GPI-80 cross-linking induced up-regulation of CD11b/CD18 (Mac-1) expression on neutrophil surfaces and shedding of L-selectin, which depends on tyrosine phosphorylation and cytoskeleton remodeling. Furthermore, the cross-linking enhanced fMLP-induced human neutrophil adherence. These results suggest that GPI-80 may be a regulator of ß₂ integrin in neutrophils.

Key Words: integrin • adherence • uPAR • DAF

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