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The Journal of Immunology, 1999, 162: 4277-4284.
Copyright © 1999 by The American Association of Immunologists

A Novel Glycosylphosphatidyl Inositol-Anchored Protein on Human Leukocytes: A Possible Role for Regulation of Neutrophil Adherence and Migration1

Kichiya Suzuki*, Tadashi Watanabe*, Shin-ichi Sakurai*, Kazuhisa Ohtake*, Taroh Kinoshita{dagger}, Akemi Araki*, Teizo Fujita{ddagger}, Hiroshi Takei*, Yuji Takeda*, Yukiko Sato*, Takao Yamashita*, Yoshihiko Araki* and Fujiro Sendo2,*

* Department of Immunology and Parasitology, Yamagata University School of Medicine, Yamagata, Japan; {dagger} Department of Immunoregulation, Research Institute for Microbial Diseases, Osaka University, Suita, Japan; and {ddagger} Department of Biochemistry, Fukushima Medical College, Fukushima, Japan

We report here a novel glycosylphosphatidyl-inositol (GPI)-anchored glycoprotein on human leukocytes. Treatment of neutrophils with a mAb (3H9) to this molecule sequentially up-regulates and down-regulates ß2 integrin-dependent adhesion of these cells as well as their transendothelial migration in vitro. In addition, this mAb simultaneously modulates the avidity of ß2 integrin for its ligand, iC3b, with kinetics similar to those observed in 3H9 modulation of neutrophil adherence. This mAb also induces ß2 integrin-dependent cytoskeletal remodeling. This novel GPI-anchored protein (GPI-80) is highly homologous with Vanin-1, a recently reported GPI-anchored protein that is expressed on perivascular thymic stromal cells and is involved in thymus homing in mice. The finding that both GPI-80 and Vanin-1 are 40% homologous with human biotinidase suggests the existence of a biotinidase superfamily of molecules that may be involved in the regulation of leukocyte trafficking.




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