Source:http://linkedlifedata.com/resource/pubmed/id/11164909
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
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| pubmed:dateCreated |
2001-2-22
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| pubmed:abstractText |
Sublines of the lactogen-dependent, rat pre-T Nb2 lymphoma are useful as a model for the investigation of prolactin (PRL) signaling mechanisms, regulation of transcription of target genes, and the immunomodulatory and anti-apoptotic actions of the hormone in T lymphocytes. In the present study, coupling of various tyrosine, serine/threonine, and phospholipid kinase signaling mechanisms to PRL-stimulated Nb2-11 cell proliferation and expression of the protooncogene, pim-1, was investigated utilizing pharmacologic antagonists of a broad spectrum of tyrosine kinases (tyrphostin A25), and the specific enzymes, Jak2 (tyrphostin B42) and ZAP-70 (piceatannol), as well as mitogen-activated protein kinase (MAPK, PD98059), protein kinase C (PKC, calphostin C), and phosphatidylinositol 3-kinase (PI3-kinase, LY294002). Inhibition of each pathway attenuated PRL-stimulated Nb2-11 cell proliferation in a concentration-dependent manner. Blockade of MAPK was the least efficacious; it inhibited proliferation maximally by 60%. Northern blot analysis of pim-1 expression in antagonist-treated cells revealed that MAPK, Jak2 and PI3-kinase appeared to signal to initiation of pim-1 transcription; its expression was attenuated by each of the antagonists. In other experiments, PRL was shown to rapidly activate a downstream effector of PI3-kinase, Akt, and this effect was also blocked by LY294002. It is concluded that PRL-stimulated Nb2 cell proliferation requires participation of each of the signaling pathways investigated. Moreover, hormone-mediated expression of pim-1 appears to reflect signaling by MAPK, Jak2, and PI3-kinase.
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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/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Jak2 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Janus Kinase 2,
http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositol 3-Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphotransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Pim1 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Prolactin,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Tyrosine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-pim-1,
http://linkedlifedata.com/resource/pubmed/chemical/ZAP-70 Protein-Tyrosine Kinase
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| pubmed:status |
MEDLINE
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| pubmed:month |
Feb
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| pubmed:issn |
0165-5728
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| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
15
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| pubmed:volume |
113
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| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
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| pubmed:pagination |
249-59
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| pubmed:dateRevised |
2010-11-18
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| pubmed:meshHeading |
pubmed-meshheading:11164909-Animals,
pubmed-meshheading:11164909-Cell Division,
pubmed-meshheading:11164909-Enzyme Inhibitors,
pubmed-meshheading:11164909-Janus Kinase 2,
pubmed-meshheading:11164909-Mitogen-Activated Protein Kinases,
pubmed-meshheading:11164909-Phosphatidylinositol 3-Kinases,
pubmed-meshheading:11164909-Phosphotransferases,
pubmed-meshheading:11164909-Prolactin,
pubmed-meshheading:11164909-Protein-Serine-Threonine Kinases,
pubmed-meshheading:11164909-Protein-Tyrosine Kinases,
pubmed-meshheading:11164909-Proto-Oncogene Proteins,
pubmed-meshheading:11164909-Proto-Oncogene Proteins c-pim-1,
pubmed-meshheading:11164909-Rats,
pubmed-meshheading:11164909-Signal Transduction,
pubmed-meshheading:11164909-Tumor Cells, Cultured,
pubmed-meshheading:11164909-ZAP-70 Protein-Tyrosine Kinase
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| pubmed:year |
2001
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| pubmed:articleTitle |
Prolactin signaling to pim-1 expression: a role for phosphatidylinositol 3-kinase.
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| pubmed:affiliation |
College of Pharmacy and Department of Molecular and Cellular Physiology, University of Cincinnati Medical Center, 3223 Eden Avenue, P.O. Box 670004, Cincinnati, OH 45267-0004, USA.
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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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