| Literature DB >> 20202494 |
Yu Han1, Xiaorong Zhou, Yuhong Ji, Aiguo Shen, Xiaolei Sun, Yingqing Hu, Qiong Wu, Xiaoying Wang.
Abstract
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.Entities:
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Year: 2009 PMID: 20202494 DOI: 10.1016/j.cellimm.2009.08.004
Source DB: PubMed Journal: Cell Immunol ISSN: 0008-8749 Impact factor: 4.868