Abstract:
:We have characterized a splice variant (isoform) of the human CD28 T cell costimulatory receptor. The nucleotide sequence of this CD28 isoform was identical to that of CD28 in the signal peptide, the transmembrane domain, and the cytoplasmic tail, but it was missing a large segment of the extracellular ligand-binding domain, which is encoded by the second exon. This isoform (CD28i), whose message level exceeded 25% of CD28, was a transmembrane homodimer. CD28i was found noncovalently associated with CD28 and was tyrosine-phosphorylated/PI3-kinase-complexed following the crosslinking of CD28, and the CD28 costimulatory signal was enhanced in T cells expressing CD28i. These data demonstrate that CD28i, via noncovalent association with CD28, plays a role as a costimulatory signal amplifier in human T cells.
journal_name
Bloodjournal_title
Bloodauthors
Hanawa H,Ma Y,Mikolajczak SA,Charles ML,Yoshida T,Yoshida R,Strathdee CA,Litchfield DW,Ochi Adoi
10.1182/blood.v99.6.2138subject
Has Abstractpub_date
2002-03-15 00:00:00pages
2138-45issue
6eissn
0006-4971issn
1528-0020journal_volume
99pub_type
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