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rdf:type | |
lifeskim:mentions | |
pubmed:dateCreated |
1995-8-18
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pubmed:abstractText |
B lymphocytes must respond to low concentrations of antigen despite having low affinity antigen receptors during the primary immune response. CD19, a B cell-restricted membrane protein of the immunoglobulin superfamily that associates with the antigen receptor complex, may help the B cell meet this requirement. Cross-linking CD19 to membrane immunoglobulin (mIg) lowers, by two orders of magnitude, the number of mIg that must be ligated to activate phospholipase C (PLC) or to induce DNA synthesis. CD19 is coupled, via protein tyrosine kinases (PTKs), to PLC and phosphatidylinositol 3' kinase (PI3' kinase), and it interacts with the Src-type nonreceptor PTK lyn. It also associates with two other membrane proteins, CR2 (complement receptor type 2, CD21), which permits nonimmunologic ligation of CD19, and TAPA-1, a member of the tetraspan family of membrane proteins. CR2 binds fragments of C3 that are covalently attached to glycoconjugates. This indirectly enables CD19 to be cross-linked to mIg after preimmune recognition of an immunogen by the complement system. CR2 also can be ligated by CD23, a lectin-like membrane protein that resides on cells that may present antigen to B cells. TAPA-1 associates with several other membrane proteins on B and T cells, including MHC class II, CD4, and CD8, and it promotes Ca2(+)- and LFA-1-independent homotypic aggregation when ligated directly or indirectly through CD19 or CR2. This may facilitate interaction of the B cell with other cells essential for cellular activation. The formation of this membrane protein complex by representatives of three different protein families helps the B cell resolve its dilemma of combining broad specificity with high sensitivity.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD19,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD81,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Differentiation...,
http://linkedlifedata.com/resource/pubmed/chemical/CD81 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Cd81 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Complement 3d
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pubmed:status |
MEDLINE
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pubmed:issn |
0732-0582
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
13
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
127-49
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:7542009-Amino Acid Sequence,
pubmed-meshheading:7542009-Animals,
pubmed-meshheading:7542009-Antigens, CD,
pubmed-meshheading:7542009-Antigens, CD19,
pubmed-meshheading:7542009-Antigens, CD81,
pubmed-meshheading:7542009-Antigens, Differentiation, B-Lymphocyte,
pubmed-meshheading:7542009-B-Lymphocytes,
pubmed-meshheading:7542009-Humans,
pubmed-meshheading:7542009-Immunity, Innate,
pubmed-meshheading:7542009-Membrane Proteins,
pubmed-meshheading:7542009-Mice,
pubmed-meshheading:7542009-Molecular Sequence Data,
pubmed-meshheading:7542009-Receptors, Complement 3d,
pubmed-meshheading:7542009-Signal Transduction
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pubmed:year |
1995
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pubmed:articleTitle |
The CD19/CR2/TAPA-1 complex of B lymphocytes: linking natural to acquired immunity.
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pubmed:affiliation |
Wellcome Trust Immunology Unit, University of Cambridge School of Clinical Medicine, United Kingdom.
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pubmed:publicationType |
Journal Article,
Review,
Research Support, Non-U.S. Gov't
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