Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1991-4-2
pubmed:abstractText
A successful immune response requires intercellular contact between T and B lymphocytes. We recently showed that CD28, a T cell surface protein that regulates an activation pathway, could mediate intercellular adhesion with activated B cells by interaction with the B7 antigen. Here we show that CD28 is the primary receptor for B7 on activated peripheral blood T cells, that CD28 binds to B7 in the absence of other accessory molecules, and that interaction between CD28 and B7 is costimulatory for T cell activation. To characterize the binding of CD28 to B7, we have produced genetic fusions of the extracellular portions of B7 and CD28, and immunoglobulin (Ig) C gamma 1 chains. 125I-labeled B7 Ig bound to CD28-transfected Chinese hamster ovary (CHO) cells, and to immobilized CD28 Ig with a Kd approximately 200 nM. B7 Ig also inhibited CD28-mediated cellular adhesion. The function of CD28-B7 interactions during T cell activation was investigated with soluble fusion proteins and with B7-transfected CHO cells. Immobilized B7 Ig and B7+ CHO cells costimulated T cell proliferation. Stimulation of T cells with B7+ CHO cells also specifically increased levels of interleukin 2 transcripts. These results demonstrate that the CD28 signaling pathway could be activated by B7, resulting in increased T cell cytokine production and T cell proliferation. Cellular interactions mediated by B7 and CD28 may represent an important component of the functional interactions between T and B lymphoid cells.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/1847722-1694723, http://linkedlifedata.com/resource/pubmed/commentcorrection/1847722-1697984, http://linkedlifedata.com/resource/pubmed/commentcorrection/1847722-1971273, http://linkedlifedata.com/resource/pubmed/commentcorrection/1847722-2113314, http://linkedlifedata.com/resource/pubmed/commentcorrection/1847722-2156582, http://linkedlifedata.com/resource/pubmed/commentcorrection/1847722-2162180, http://linkedlifedata.com/resource/pubmed/commentcorrection/1847722-2211998, http://linkedlifedata.com/resource/pubmed/commentcorrection/1847722-2419912, http://linkedlifedata.com/resource/pubmed/commentcorrection/1847722-2437578, http://linkedlifedata.com/resource/pubmed/commentcorrection/1847722-2440339, http://linkedlifedata.com/resource/pubmed/commentcorrection/1847722-2441877, http://linkedlifedata.com/resource/pubmed/commentcorrection/1847722-2442611, http://linkedlifedata.com/resource/pubmed/commentcorrection/1847722-2454644, http://linkedlifedata.com/resource/pubmed/commentcorrection/1847722-2465550, http://linkedlifedata.com/resource/pubmed/commentcorrection/1847722-2477485, http://linkedlifedata.com/resource/pubmed/commentcorrection/1847722-2536900, http://linkedlifedata.com/resource/pubmed/commentcorrection/1847722-2540528, http://linkedlifedata.com/resource/pubmed/commentcorrection/1847722-2543930, http://linkedlifedata.com/resource/pubmed/commentcorrection/1847722-2647304, http://linkedlifedata.com/resource/pubmed/commentcorrection/1847722-2779549, http://linkedlifedata.com/resource/pubmed/commentcorrection/1847722-2794510, http://linkedlifedata.com/resource/pubmed/commentcorrection/1847722-2825196, http://linkedlifedata.com/resource/pubmed/commentcorrection/1847722-3021470, http://linkedlifedata.com/resource/pubmed/commentcorrection/1847722-3289580, http://linkedlifedata.com/resource/pubmed/commentcorrection/1847722-3488815, http://linkedlifedata.com/resource/pubmed/commentcorrection/1847722-4104295, http://linkedlifedata.com/resource/pubmed/commentcorrection/1847722-6274961, http://linkedlifedata.com/resource/pubmed/commentcorrection/1847722-6458039
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0022-1007
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
173
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
721-30
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed-meshheading:1847722-Animals, pubmed-meshheading:1847722-Antigens, CD28, pubmed-meshheading:1847722-Antigens, Differentiation, T-Lymphocyte, pubmed-meshheading:1847722-Base Sequence, pubmed-meshheading:1847722-Cell Line, pubmed-meshheading:1847722-Humans, pubmed-meshheading:1847722-Interleukin-2, pubmed-meshheading:1847722-Interleukin-4, pubmed-meshheading:1847722-Kinetics, pubmed-meshheading:1847722-Lymphocyte Activation, pubmed-meshheading:1847722-Molecular Sequence Data, pubmed-meshheading:1847722-Oligonucleotide Probes, pubmed-meshheading:1847722-Plasmids, pubmed-meshheading:1847722-Polymerase Chain Reaction, pubmed-meshheading:1847722-RNA, Messenger, pubmed-meshheading:1847722-Receptors, Interleukin-4, pubmed-meshheading:1847722-Receptors, Mitogen, pubmed-meshheading:1847722-Recombinant Fusion Proteins, pubmed-meshheading:1847722-T-Lymphocytes, pubmed-meshheading:1847722-Transcription, Genetic, pubmed-meshheading:1847722-Transfection
pubmed:year
1991
pubmed:articleTitle
Binding of the B cell activation antigen B7 to CD28 costimulates T cell proliferation and interleukin 2 mRNA accumulation.
pubmed:affiliation
Oncogen Division, Bristol-Myers-Squibb Pharmaceutical Research Institute, Seattle, Washington 91821.
pubmed:publicationType
Journal Article