Source:http://linkedlifedata.com/resource/pubmed/id/12032173
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
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pubmed:dateCreated |
2002-5-28
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pubmed:abstractText |
In this study we analyzed the signaling pathway triggered by GM3 in lymphoblastoid T-cells. In these cells, GM3 induced cPLA2 activation, arachidonic acid release, and PKC-delta translocation. In order to clarify the upstream molecular signals triggered by GM3, we analyzed the activation of extracellular signal-regulated kinase (ERK)s, a downstream effector of Ras-regulated cytoplasmic kinase cascade. Our results showed that GM3 treatment led to rapid ERK phosphorylation in lymphoblastoid T-cells, as detected by anti-phospho-p44/42 MAP kinase. Similar findings were found in human peripheral blood lymphocytes. Moreover, we showed that GM3 specifically phosphorylated ERK-2, as revealed by anti-phosphotyrosine reactivity on both cell free lysates and ERKs immunoprecipitates. The role of the CD4 cytoplasmic domain in GM3-triggered signaling pathway was investigated using A2.01/CD4-cyt399 cells, which had been transfected with a mutant form of CD4 lacking the bulk of the cytoplasmic domain. In these cells GM3 induced cPLA2 activation, arachidonic acid release, and PKC-delta translocation, but not CD4 endocytosis, indicating that the CD4 cytoplasmic domain plays a key role in GM3-triggered CD4 endocytosis and the GM3-triggered biochemical pathway is upstream of CD4 phosphorylation. These findings strongly suggest that GM3 triggers a novel signaling pathway involved in the regulation of cellular functions.
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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, CD4,
http://linkedlifedata.com/resource/pubmed/chemical/G(M3) Ganglioside,
http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/PRKCD protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Phospholipases A,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C-delta
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0022-2275
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
43
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
971-8
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:12032173-Antigens, CD4,
pubmed-meshheading:12032173-Cell Line,
pubmed-meshheading:12032173-Cells, Cultured,
pubmed-meshheading:12032173-Down-Regulation,
pubmed-meshheading:12032173-G(M3) Ganglioside,
pubmed-meshheading:12032173-Humans,
pubmed-meshheading:12032173-Isoenzymes,
pubmed-meshheading:12032173-Lymphocytes,
pubmed-meshheading:12032173-Mitogen-Activated Protein Kinases,
pubmed-meshheading:12032173-Phospholipases A,
pubmed-meshheading:12032173-Protein Kinase C,
pubmed-meshheading:12032173-Protein Kinase C-delta
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pubmed:year |
2002
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pubmed:articleTitle |
Ganglioside GM3 activates ERKs in human lymphocytic cells.
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pubmed:affiliation |
Dipartimento di Medicina Sperimentale, Università di L'Aquila, Via Vetoio Coppito 2, L'Aquila 67100, Italy.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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