beta-1,4-galactosyltransferase-I (beta-1,4-GalT-I) has two isoforms that differ only in the length of their cytoplasmic domains. In this study, we found that both the long and short isoforms of beta-1,4-GalT-I were expressed in human CD4(+) T lymphocytes, and localized in the cytoplasm and on the plasma membrane. The expression level of beta-1,4-GalT-I was increased in CD4(+) T cells after stimulation with interleukin (IL)-2, and was further increased after stimulation with IL-2+IL-12, but decreased after stimulation with IL-2+IL-4 when compared to stimulation with IL-2 alone. We also demonstrated that the cellular adhesion of CD4(+) T cells was significantly increased upon cytokine stimulation, and was inhibited by alpha-lactalbumin, indicating that the increase in adhesion was positively correlated with the expression and activity of long beta-1,4-GalT-I. Collectively, the data suggest that beta-1,4-GalT-I plays a role in the cellular adhesion of CD4(+) T cells.
Copyright 2009. Published by Elsevier Inc.