Abstract
Galectin-1 belongs to the galectin family of lectins, and is expressed in a variety of tissues including placenta, liver, skeletal and smooth muscle. This protein is thought to be a versatile modulator of cell function, and binds lectin only when it is in a reduced form. Once galectin-1 is oxidized, it shows an axonal regeneration-promoting activity though it loses its ability to bind lectin (Inagaki et al., 2000). Although we have demonstrated that the oxidized galectin-1 promotes axonal regeneration via macrophage after peripheral nerve axotomy (Horie et al., 2004), intracellular signaling pathway remains unknown. Therefore, in order to explore the pathway involved in oxidized galectin-1 via receptor, we have performed proteomic analysis of macrophages stimulated with oxidized galectin-1, galectin-1 mutant in which all six cysteine residues were replaced by serine (CS-Gal), or bovine serum albumin (BSA) using 2-dimensional gel electrophoresis. We found that expression levels of some proteins were changed in macrophages exposed to oxidized galectin-1 as compared with BSA. Those proteins were analyzed and identified with LC/MS/MS and the findings suggest to be related with some kinase pathways. Now we are analyzing relationships between these proteins. [Jpn J Physiol 55 Suppl:S203 (2005)]
