期刊
IMMUNOLOGY AND CELL BIOLOGY
卷 86, 期 7, 页码 608-615出版社
WILEY
DOI: 10.1038/icb.2008.46
关键词
CD45; lectin; galectin; glycan; phosphatase; T-cell
资金
- NIH [R01 GM63281, T32 A152031]
- NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES [T32AI052031] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM063281] Funding Source: NIH RePORTER
CD45, an abundant and highly glycosylated cell-surface protein, is a critical regulator of T-cell development. CD45 is differentially glycosylated throughout the life of a T cell, and the glycosylation state of CD45 controls recognition by various binding partners, affects intracellular signaling by the cytoplasmic tyrosine phosphatase domain and modulates the response of the T cell to antigen. Although the importance of CD45 during T-cell development has been established, it is becoming increasingly clear that glycosylation of CD45 is a dynamic process that modifies T-cell survival, activation and immune function. In this review, we address changes that occur in CD45 glycosylation during T-cell development and differentiation, describe carbohydrate-binding proteins that recognize differentially glycosylated forms of CD45, and discuss how differential glycosylation alters the T-cell response to a variety of signals involved in selection, activation and apoptosis.
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