Source:http://linkedlifedata.com/resource/pubmed/id/12008033
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1-2
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pubmed:dateCreated |
2002-5-14
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pubmed:abstractText |
Ligation of B cell receptors (BCR) on immature B cells may induce apoptosis, while in mature B cells it stimulates cell activation and growth. The signaling pathway regulating the differential functional response, death or survival of the B cell is not fully characterized. We have tested the intracellular signaling requirement of these processes using B cells isolated from the spleen of irradiated auto-reconstituted (transitional immature B cells) and untreated mice (mature B cells), respectively. We compared the BCR induced intracellular [Ca2+] transient, protein tyrosine phosphorylation and ERK phosphorylation, furthermore, the activation of Elk-1 and CREB transcription factors. The BCR induced rise of intracellular [Ca2+] did not significantly differ in the two populations, only a slight difference in the late phase of the response was observed. Immature B cells responded with a maximum tyrosine phosphorylation to a five times lower dose of anti-IgM compared to the mature population. Most importantly, we have found a significant difference in the tyrosine phosphorylation of the Gab family adaptor proteins, Gab1/2. In contrast to mature B cells, crosslinking of BCR on immature B cells did not induce tyrosine phosphorylation of Gab2, thus the Gab2-organized signal amplification complex could not be produced. Furthermore, we detected a significant difference in the kinetics of BCR induced ERK, Elk-1 and CREB phosphorylation. In immature B cells, ERK was transiently phosphorylated, ceasing after 120 min, while in mature cells, ERK phosphorylation was sustained. Elk-1 and CREB activation was also transient in immature B cells, followed the kinetics of ERK phosphorylation. The lack of sustained Erk1/2 activation suppresses the transcription factors necessary for the proliferation signal. Since ERK is regulated by the phosphorylated Gab1/2, these data demonstrate that BCR triggered phosphorylation and signal amplification of Gab1/2 is a critical step in a life or death decision of B cells.
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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/Antigens, Differentiation...,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Gab2 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Antigen, B-Cell,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0165-2478
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
3
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pubmed:volume |
82
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
41-9
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:12008033-Animals,
pubmed-meshheading:12008033-Antigens, Differentiation, B-Lymphocyte,
pubmed-meshheading:12008033-Apoptosis,
pubmed-meshheading:12008033-B-Lymphocyte Subsets,
pubmed-meshheading:12008033-B-Lymphocytes,
pubmed-meshheading:12008033-Calcium,
pubmed-meshheading:12008033-Cell Differentiation,
pubmed-meshheading:12008033-Cells, Cultured,
pubmed-meshheading:12008033-Kinetics,
pubmed-meshheading:12008033-Lymphocyte Activation,
pubmed-meshheading:12008033-Mice,
pubmed-meshheading:12008033-Mice, Inbred BALB C,
pubmed-meshheading:12008033-Mitogen-Activated Protein Kinases,
pubmed-meshheading:12008033-Phosphoproteins,
pubmed-meshheading:12008033-Phosphorylation,
pubmed-meshheading:12008033-Receptors, Antigen, B-Cell,
pubmed-meshheading:12008033-Signal Transduction,
pubmed-meshheading:12008033-Spleen,
pubmed-meshheading:12008033-Stem Cells,
pubmed-meshheading:12008033-Transcription Factors
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pubmed:year |
2002
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pubmed:articleTitle |
BCR mediated signal transduction in immature and mature B cells.
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pubmed:affiliation |
Research Group of the Hungarian Academy of Sciences at the Department of Immunology, L. Eötvös University, Budapest, Hungary.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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