Source:http://linkedlifedata.com/resource/pubmed/id/11164895
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
11
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pubmed:dateCreated |
2001-2-22
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pubmed:abstractText |
We previously demonstrated that stimulation of human T-lymphocytes with calcium ionophores induced the phosphorylation and enzymatic activation of ERK2. We now report on the mechanism by which calcium-ionophore-induced activation of ERK1 and 2 occurs in these cells. The activation of ERK1 and 2 by increases in intracellular calcium was inhibited by calmidazolium suggesting the involvement of calmodulin in this response. To further elucidate the mechanism by which calcium-induced ERK activation occurs, we used the CaM-kinase inhibitor KN-93 and an inactive analog of KN-93 (KN-92). KN-93, but not KN-92, blocked ionomycin-induced activation of ERK1 and 2 in human T lymphocytes. We previously demonstrated that stimulation of T lymphocytes with ionomycin or A23187 resulted in a CaM-kinase-dependent shift in the mobility of p56(Lck). To determine if p56(Lck) was involved in calcium-induced ERK activation, we stimulated the p56(Lck) negative Jurkat cell derivatives, J.CaM1.6 and J.CaM1/Rep3, with ionomycin. In these p56(Lck) negative cell lines, activation of ERK1 and 2 in response to ionomycin was only minimally detected. When J.CaM1 cells were reconstituted with p56(Lck), ionomycin induced ERK1 and 2 activation. Treatment of Jurkat cells with PP2, an inhibitor of p56(Lck), inhibited calcium-induced, but not PMA-induced, ERK1 and 2 activation. Treatment of Jurkat cells with the MEK inhibitor PD98059 blocked ionomycin-induced ERK activation, but not the shift in the mobility of p56(Lck). Our data suggests that increases in intracellular calcium induce the activation of ERK1 and 2 in human T lymphocytes via sequential activation of CaM-kinase and phosphorylation of p56(Lck).
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/CAMK4 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Calmodulin-Dependent...,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Calmodulin-Dependent...,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Calmodulin-Dependent...,
http://linkedlifedata.com/resource/pubmed/chemical/Lymphocyte Specific Protein...,
http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinase 1,
http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinase 3,
http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinases
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0161-5890
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
37
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
675-83
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:11164895-Calcium,
pubmed-meshheading:11164895-Calcium-Calmodulin-Dependent Protein Kinase Type 2,
pubmed-meshheading:11164895-Calcium-Calmodulin-Dependent Protein Kinase Type 4,
pubmed-meshheading:11164895-Calcium-Calmodulin-Dependent Protein Kinases,
pubmed-meshheading:11164895-Cell Line,
pubmed-meshheading:11164895-Enzyme Activation,
pubmed-meshheading:11164895-Humans,
pubmed-meshheading:11164895-Lymphocyte Specific Protein Tyrosine Kinase p56(lck),
pubmed-meshheading:11164895-Mitogen-Activated Protein Kinase 1,
pubmed-meshheading:11164895-Mitogen-Activated Protein Kinase 3,
pubmed-meshheading:11164895-Mitogen-Activated Protein Kinases,
pubmed-meshheading:11164895-T-Lymphocytes
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pubmed:year |
2000
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pubmed:articleTitle |
Calcium-induced ERK activation in human T lymphocytes occurs via p56(Lck) and CaM-kinase.
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pubmed:affiliation |
Department of Microbiology and Immunology, East Carolina University School of Medicine, Brody Building, Greenville, NC 27858, USA. franklinr@mail.ecu.edu
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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