rdf:type |
|
lifeskim:mentions |
umls-concept:C0037083,
umls-concept:C0051980,
umls-concept:C0079904,
umls-concept:C0086661,
umls-concept:C0205263,
umls-concept:C1332716,
umls-concept:C1332737,
umls-concept:C1516044,
umls-concept:C1704259,
umls-concept:C1705987,
umls-concept:C1710082,
umls-concept:C1948023
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pubmed:issue |
1
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pubmed:dateCreated |
2004-1-21
|
pubmed:abstractText |
Engagement of mIgM induces G1 arrest and apoptosis in immature B cells. The biochemical mechanism(s) regulating the cell death process are poorly understood. Cross-linking of CD72 (a B cell co-receptor) with anti-CD72 antibody was shown to protect B cells from apoptosis. We investigated the molecular mechanism involved in apoptosis preventing signaling mediated by CD72 ligation using a derivative (WEHIdelta) of the WEHI231 cell line which is representative of immature B cells. Apoptotic WEHIdelta cells following cross-linking of mIgM demonstrate a dramatic loss of c-Myc protein after transient up-regulation. In contrast, pre-ligation of CD72 was able to sustain c-Myc expression after transient up-regulation. Cross-linking of mIgM of WEHIdelta cells causes accumulation of the Cdk inhibitor, p27(Kip1). CD72 pre-ligation was shown to inhibit the accumulation of p27(Kip1) protein. Moreover, NF-kappaB activity was not suppressed in WEHIdelta cells after mIgM cross-linking when the cells were pre-treated with anti-CD72 antibody. These results strongly suggest that the apoptosis preventing signal evoked by CD72 ligation is delivered through the pathway of NF-kappaB, c-Myc, p27(Kip1) and cyclin.
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Differentiation...,
http://linkedlifedata.com/resource/pubmed/chemical/Cdkn1b protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Cycle Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclin-Dependent Kinase Inhibitor...,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclins,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin M,
http://linkedlifedata.com/resource/pubmed/chemical/NF-kappa B,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-myc,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Antigen, B-Cell,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Suppressor Proteins
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pubmed:status |
MEDLINE
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pubmed:issn |
0385-5600
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:volume |
48
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
59-66
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:14734859-Animals,
pubmed-meshheading:14734859-Antigens, CD,
pubmed-meshheading:14734859-Antigens, Differentiation, B-Lymphocyte,
pubmed-meshheading:14734859-Apoptosis,
pubmed-meshheading:14734859-B-Lymphocytes,
pubmed-meshheading:14734859-Cell Cycle,
pubmed-meshheading:14734859-Cell Cycle Proteins,
pubmed-meshheading:14734859-Cell Line,
pubmed-meshheading:14734859-Cyclin-Dependent Kinase Inhibitor p27,
pubmed-meshheading:14734859-Cyclins,
pubmed-meshheading:14734859-G1 Phase,
pubmed-meshheading:14734859-Immunoglobulin M,
pubmed-meshheading:14734859-Mice,
pubmed-meshheading:14734859-NF-kappa B,
pubmed-meshheading:14734859-Proto-Oncogene Proteins c-myc,
pubmed-meshheading:14734859-Receptors, Antigen, B-Cell,
pubmed-meshheading:14734859-Signal Transduction,
pubmed-meshheading:14734859-Tumor Suppressor Proteins
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pubmed:year |
2004
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pubmed:articleTitle |
CD72 stimulation modulates anti-IgM induced apoptotic signaling through the pathway of NF-kappaB, c-Myc and p27(Kip1).
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pubmed:affiliation |
Research Institute for Biological Sciences, Tokyo University of Science, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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