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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6278
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pubmed:dateCreated |
1990-8-2
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pubmed:abstractText |
Signalling by membrane immunoglobulin, the B-lymphocyte antigen receptor, regulates B-cell maturation and activation. Crosslinking of membrane immunoglobulin by antigen or by anti-immunoglobulin antibodies inactivates immature B cells, eliminating many of the B cells capable of producing auto-antibodies. By contrast, crosslinking of membrane immunoglobulin promotes activation of mature B cells for clonal expansion and antibody production against foreign antigens. Crosslinking membrane IgM on the immature B-cell line WEHI-231 induces growth arrest. This response may be analogous to the deletion or inactivation of immature B cells that is induced by antigen or anti-IgM antibodies. Membrane immunoglobulin crosslinking stimulates phosphoinositide hydrolysis, which leads to increases in intracellular calcium and activation of protein kinase C. The induced phosphoinositide breakdown is important for inhibiting WEHI-231 growth (ref. 7 and D. Page, M.R.G., K. Fahey, L. Matsuuchi and A.L.D., manuscript submitted for publication), but may not be sufficient, as agents that elevate calcium and activate protein kinase C cause only partial growth arrest. We now show that in both mature splenic B cells and the immature B-cell line WEHI-231 crosslinking membrane immunoglobulin also stimulates phosphorylation of protein tyrosine, a reaction that has been implicated as a key regulator of cell growth. Most of these phosphorylations were not a consequence of the phosphoinositide pathway. Thus, tyrosine phosphorylation is a second mode of transmembrane signalling by membrane immunoglobulin.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin D,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin M,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphotyrosine,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Tyrosine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Antigen, B-Cell,
http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0028-0836
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
28
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pubmed:volume |
345
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
810-3
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:1694265-Animals,
pubmed-meshheading:1694265-B-Lymphocytes,
pubmed-meshheading:1694265-Humans,
pubmed-meshheading:1694265-Immunoglobulin D,
pubmed-meshheading:1694265-Immunoglobulin M,
pubmed-meshheading:1694265-Immunologic Techniques,
pubmed-meshheading:1694265-Mice,
pubmed-meshheading:1694265-Molecular Weight,
pubmed-meshheading:1694265-Phosphoproteins,
pubmed-meshheading:1694265-Phosphotyrosine,
pubmed-meshheading:1694265-Protein-Tyrosine Kinases,
pubmed-meshheading:1694265-Receptor Aggregation,
pubmed-meshheading:1694265-Receptors, Antigen, B-Cell,
pubmed-meshheading:1694265-Signal Transduction,
pubmed-meshheading:1694265-Tyrosine
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pubmed:year |
1990
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pubmed:articleTitle |
Stimulation of protein tyrosine phosphorylation by the B-lymphocyte antigen receptor.
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pubmed:affiliation |
George Williams Hooper Foundation, University of California, San Francisco 94143-0552.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, U.S. Gov't, P.H.S.
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