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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1994-10-24
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pubmed:abstractText |
Recent studies of murine and human B lymphocytes have shown that crosslinking of surface IgM (sIgM) and sIgD stimulates tyrosine phosphorylation of a set of proteins involved in signal transduction. We investigated tyrosine phosphorylation of the sIg-associated proteins MB-1 and B29, and p75HS1 (HS1), and the association of HS1 with MB-1/B29 heterodimers in normal human B cells and a human B lymphoma cell line, B104. Using immunoprecipitation with anti-phosphotyrosine antibodies (Abs) followed by immunoblotting with anti-MB-1 Abs, anti-B29 Abs or anti-HS1 Abs, we demonstrated that MB-1, B29 and HS1 were tyrosine-phosphorylated after sIgM or sIgD crosslinking. Immunoprecipitation with anti-B29 Abs followed by anti-HS1 Abs immunoblotting revealed that HS1 was associated with MB-1/B29 heterodimers after sIgM or sIgD crosslinking. The results showed that HS1 may play an important role in signal transduction through sIgM and sIgD on human B cells.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD79,
http://linkedlifedata.com/resource/pubmed/chemical/Blood Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/CD79A protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/CD79B protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Primers,
http://linkedlifedata.com/resource/pubmed/chemical/HCLS1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin D,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin M,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Antigen, B-Cell,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Fc,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, IgG,
http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine,
http://linkedlifedata.com/resource/pubmed/chemical/immunoglobulin M receptor
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0165-2478
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
40
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
65-71
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:7927516-Antigens, CD,
pubmed-meshheading:7927516-Antigens, CD79,
pubmed-meshheading:7927516-B-Lymphocytes,
pubmed-meshheading:7927516-Base Sequence,
pubmed-meshheading:7927516-Blood Proteins,
pubmed-meshheading:7927516-DNA Primers,
pubmed-meshheading:7927516-Humans,
pubmed-meshheading:7927516-Immunoglobulin D,
pubmed-meshheading:7927516-Immunoglobulin M,
pubmed-meshheading:7927516-Membrane Glycoproteins,
pubmed-meshheading:7927516-Molecular Sequence Data,
pubmed-meshheading:7927516-Phosphoproteins,
pubmed-meshheading:7927516-Phosphorylation,
pubmed-meshheading:7927516-Receptors, Antigen, B-Cell,
pubmed-meshheading:7927516-Receptors, Fc,
pubmed-meshheading:7927516-Receptors, IgG,
pubmed-meshheading:7927516-Signal Transduction,
pubmed-meshheading:7927516-Tumor Cells, Cultured,
pubmed-meshheading:7927516-Tyrosine
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pubmed:year |
1994
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pubmed:articleTitle |
Tyrosine phosphorylation of MB-1, B29, and HS1 proteins in human B cells following receptor crosslinking.
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pubmed:affiliation |
Department of Pediatrics, Faculty of Medicine, Kyoto University, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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