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International Immunology, Vol. 12, No. 4, 487-492, April 2000
© 2000 Japanese Society for Immunology

Redistribution of selectin counter-ligands induced by cytokines

Kisaburo Nagata1,4, Tsutomu Tsuji1,5, Kouji Matsushima2, Nobuo Hanai3 and Tatsuro Irimura1

1 Laboratory of Cancer Biology and Molecular Immunology, Graduate School of Pharmaceutical Sciences, and
2 Department of Molecular Preventive Medicine, School of Medicine, University of Tokyo, 7-3-1- Hongo, Bunkyo-ku, Tokyo 113-0033, Japan
3 Tokyo Research Laboratories, Kyowa Hakko Kogyo Co. Ltd, Machida, Tokyo 194-0023, Japan

Correspondence to: T. Irimura

Soluble recombinant (r) P-selectin and rP-selectin immobilized on plastic surfaces were tested for their capacity to activate neutrophils to produce superoxide anion. Soluble rP-selectin was incapable of activating leukocytes, whereas immobilized rP-selectin was able to induce leukocyte activation. When neutrophils were pretreated with a low dose of IL-8, granulocyte colony stimulating factor or granulocyte macrophage colony stimulating factor, soluble rP-selectin was no longer inert. These cytokine-primed leukocytes produced superoxide anion in the presence of soluble rP-selectin. During this priming period, sialyl Lewis X (sLeX) epitopes redistributed to one end of the leukocytes. Similar polarization of sLeX epitopes was observed at the attachment site of cells that adhered to immobilized rP-selectin. Cap formation and superoxide anion production induced by solid-phase P-selectin or by IL-8 and soluble rP-selectin treatment were inhibited by treatment of the leukocytes with cytochalasin B. These observations suggest that the redistribution of the carbohydrate ligands and the polarization of the leukocyte surface through an active process is a prerequisite but not sufficient to leukocyte superoxide production through P-selectin.

Keywords: neutrophils, selectin ligand, sialyl Lewis X, superoxide anion

4 Present address: Department of Immunology, Tokyo Metropolitan Institute of Medical Science, 3-18-22 Honkomagome, Bunkyo-ku, Tokyo 113-8613, Japan

5 Present address: Department of Microbiology, Hoshi University, 2-4-41 Ebara, Shinagawa-ku, Tokyo 142-8501, Japan

Transmitting editor: K. Okumura


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