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From the Department of Biochemical Pharmacology* and the Bone and Joint Research Unit, The William Harvey Research Institute, London, United Kingdom; the Research Center for Glycoscience, National Institute of Advanced Industrial Science and Technology, Ibraki, Japan; the Department of Biological Chemistry, Teikyo University, Sagamiko, Kanagawa, Japan; and the Department of Biology,¶ Instituto de Biociências, Letras e Ciências Exatas-Universidade Estadual Paulista (IBILCE-UNESP), Sao José do Rio Preto, Sao Paulo, Brazil
Galectin-1 (Gal-1), the prototype of a family of ß-galactoside-binding proteins, has been shown to attenuate experimental acute and chronic inflammation. In view of the fact that endothelial cells (ECs), but not human polymorphonuclear leukocytes (PMNs), expressed Gal-1 we tested here the hypothesis that the protein could modulate leukocyte-EC interaction in inflammatory settings. In vitro, human recombinant (hr) Gal-1 inhibited PMN chemotaxis and trans-endothelial migration. These actions were specific as they were absent if Gal-1 was boiled or blocked by neutralizing antiserum. In vivo, hrGal-1 (optimum effect at 0.3 µg equivalent to 20 pmol) inhibited interleukin-1ß-induced PMN recruitment into the mouse peritoneal cavity. Intravital microscopy analysis showed that leukocyte flux, but not their rolling velocity, was decreased by an anti-inflammatory dose of hrGal-1. Binding of biotinylated Gal-1 to resting and postadherent human PMNs occurred at concentrations inhibitory in the chemotaxis and transmigration assays. In addition, the pattern of Gal-1 binding was differentially modulated by PMN or EC activation. In conclusion, these data suggest the existence of a previously unrecognized function of Gal-1, that is inhibition of leukocyte rolling and extravasation in experimental inflammation. It is possible that endogenous Gal-1 may be part of a novel anti-inflammatory loop in which the endothelium is the source of the protein and the migrating PMNs the target for its anti-inflammatory action.
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