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(Journal of Leukocyte Biology. 2000;68:65-72.)
© 2000 by Society for Leukocyte Biology

Sulfatide binding and activation of leukocytes through an L-selectin-independent pathway

Ziqiang Ding, Hiroto Kawashima and Masayuki Miyasaka

Department of Bioregulation, Biomedical Research Center, Osaka University Medical School, Japan

Correspondence: Dr. Ziqiang Ding, Department of Pediatrics, IWK Grace Health Center, 5850 University Avenue, Halifax, NS, B3J 3G9, Canada. E-mail: zding{at}is.dal.ca

Sulfatide has been reported to activate leukocytes through L-selectin. Here we provide evidence that sulfatide binds to and activates leukocytes through both L-selectin-dependent and -independent pathways. Rat leukocytes of various sources shed surface L-selectin after phorbol myristate acetate (PMA) treatment, however, these cells retained the ability to bind sulfatide. In addition, sulfatide also bound to an L-selectin-negative cell line EL-4, and the binding was up-regulated by PMA. Sulfatide induced aggregation of L-selectin-positive lymphocytes, which was highly dependent on divalent cations, protein tyrosine kinases (PTK), and protein kinase C (PKC), but was independent of ß1 and ß2 integrins. In contrast, sulfatide-induced EL-4 cell aggregation required an LFA-1/ICAM-1 adhesion pathway but not PTK and PKC. A sulfatide receptor of 65 kDa was isolated from EL-4 cells. Taken together, this study suggests that sulfatide can bind to and activate leukocytes through an L-selectin-independent molecule and triggers signal transduction pathways different from those induced by L-selectin activation.

Key Words: adhesion molecules • lymphocytes • signal transduction • phorbol ester




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