Journal
GLYCOBIOLOGY OF THE IMMUNE RESPONSE
Volume 1253, Issue -, Pages 58-67Publisher
BLACKWELL SCIENCE PUBL
DOI: 10.1111/j.1749-6632.2011.06304.x
Keywords
glycosylation; T cell; CD43; CD45
Funding
- NCI NIH HHS [T32 CA009056:35, R21 CA139368, T32 CA009056] Funding Source: Medline
- NHLBI NIH HHS [HL102989, R21 HL102989] Funding Source: Medline
Ask authors/readers for more resources
Glycosylation affects many essential T cell processes and is intrinsically controlled throughout the lifetime of a T cell. CD43 and CD45 are the two most abundant glycoproteins on the T cell surface and are decorated with O- and N-glycans. Global T cell glycosylation and specific glycosylation of CD43 and CD45 are modulated during thymocyte development and T cell activation; T cells control the type and abundance of glycans decorating CD43 and CD45 by regulating expression of glycosyltransferases and glycosidases. Additionally, T cells regulate glycosylation of CD45 by expressing alternatively spliced isoforms of CD45 that have different glycan attachment sites. The glycophenotype of CD43 and CD45 on T cells influences how T cells interact with the extracellular environment, including how T cells interact with endogenous lectins. This review focuses on changes in glycosylation of CD43 and CD45 occurring throughout T cell development and activation and the role that glycosylation plays in regulating T cell processes, such as migration, T cell receptor signaling, and apoptosis.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available