کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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2167667 | 1092346 | 2010 | 7 صفحه PDF | دانلود رایگان |

β-1,4-galactosyltransferase-I (β-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 β-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 β-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 α-lactalbumin, indicating that the increase in adhesion was positively correlated with the expression and activity of long β-1,4-GalT-I. Collectively, the data suggest that β-1,4-GalT-I plays a role in the cellular adhesion of CD4+ T cells.
Journal: Cellular Immunology - Volume 262, Issue 1, 2010, Pages 11–17