beta4 Galactosylation of glycoproteins is one of the most important post-translational modifications. Recent studies have demonstrated that aberrant galactosylation associates with some inflammation diseases. beta-1,4-galactosyltransferase-I (beta-1,4-GalT-I), which transfers galactose to the terminal N-acetylglucosamine of N- and O-linked glycans in a beta-1,4- linkage, considered to be the major galactosyltransferse among the seven members of the subfamily responsible for beta4 galactosylation. In the present study, we investigated the expression of beta-1,4-GalT-I in Schwann cells under Lipopolysaccharide (LPS) treatment. RT-PCR revealed that the beta-1,4-GalT-I mRNA was significant increased as early as 2 h after LPS stimulation. Immunofluorescence showed that beta-1,4-GalT-I was located in Golgi apparatus and membrane of Schwann cells. With the 1 microg/ml LPS treatment, expression levels of beta-1,4-GalT-I was much higher compared with control group. In addition, lectin blot indicated that the beta4 galactosylation of glycoproteins such as integrin alpha5 was enhanced, which may due to the induced beta-1,4-GalT-I expression. These results suggested that beta-1,4-GalT-I may play an important role in adhesion and migration of Schwann cells during inflammation.