Linked Life Data

18607388

Source:http://linkedlifedata.com/resource/pubmed/id/18607388

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
2008-10-2
pubmed:abstractText
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.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0818-9641
pubmed:author
pubmed:issnType
Print
pubmed:volume
86
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
608-15
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
CD45 glycosylation controls T-cell life and death.
pubmed:affiliation
Department of Pathology and Laboratory Medicine, UCLA School of Medicine, University of California, Los Angeles, CA 90095, USA.
pubmed:publicationType
Journal Article, Review, Research Support, N.I.H., Extramural