Lipopolysaccharide Induced Upregulation of β-1,4-Galactosyltransferase-I in Schwann cell

β4 Galactosylation of glycoproteins is one of the most important post-translational modifications. Recent studies have demonstrated that aberrant galactosylation associates with some inflammation diseases. β-1,4-galactosyltransferase-I (β-1,4-GalT-I), which transfers galactose to the terminal N-acetylglucosamine of N- and O-linked glycans in a β-1,4- linkage, considered to be the major galactosyltransferse among the seven members of the subfamily responsible for β4 galactosylation. In the present study, we investigated the expression of β-1,4-GalT-I in Schwann cells under Lipopolysaccharide (LPS) treatment. RT-PCR revealed that the β-1,4-GalT-I mRNA was significant increased as early as 2 h after LPS stimulation. Immunofluorescence showed that β-1,4-GalT-I was located in Golgi apparatus and membrane of Schwann cells. With the 1 μg/ml LPS treatment, expression levels of β-1,4-GalT-I was much higher compared with control group. In addition, lectin blot indicated that the β4 galactosylation of glycoproteins such as integrin α5 was enhanced, which may due to the induced β-1,4-GalT-I expression. These results suggested that β-1,4-GalT-I may play an important role in adhesion and migration of Schwann cells during inflammation.