β-1,4-Galactosyltransferase-involved in lipopolysaccharide-induced adhesion of schwann cells

The carbohydrate moieties of glycoprotein are associated with some inflammatory diseases by affecting a wide range of biological functions of cells. This study aimed to investigate the role of β-1,4-galactosyltransferase-I (β-1,4-GalT-I) in adhesion of Schwann cells during inflammation. A rat Schwann cell line, RSC 96 was used. We used western blotting to detect the expression of β-1,4-GalT-I. Flow cytomety was used to measure the galactosylation of glycoproteins on cell surfaces. Immunofluorescent staining was used to examine the expression of α6 integrin, focal adhesion kinase (FAK) and F-actin. Tyrosine phosphorylation of FAK was detected by immunoprecipitation. An adhesion assay was performed to investigate the adhesion of Schwann cells. One-way ANOVA was used to compare differences between the operated and the control group. Schwann cell adhesion was induced by LPS stimulation and was accompanied by upregulation of β-1,4-GalT-I expression and galactosylation of glycoproteins. There was a change of localization of FAK and cytoskeleton organization in LPS treated cells compared with control cells. The pretreated cells enhanced tyrosine phosphorylation of FAK compared with control cells in the adhesion process. With the increased cell surface expression of α6 integrin and β-1,4-GalT-I, the adhesion of Schwann cells on laminin was increased as well. These results suggested that β-1,4-GalT-I may play an important role in adhesion of Schwann cells during inflammation.