|Delay in serum stimulation of Erk activity caused by oncogenic transformation.|
|PMID: 8622889 Owner: NLM Status: MEDLINE|
|Mitogenic growth factor stimulation activates several signal transduction pathways, including the well-characterized Ras-Erk pathway, resulting in transient activation of Erk1 and Erk2. Oncogenic transformation, however, causes constitutive activation of growth signalling pathways, resulting in an accelerated rate of cell division. We investigated the effects of transformation on serum and growth factor stimulation of Erk1 and Erk2, and show that stimulation of these MAP kinases, as well as the Erk activator Mek, is delayed in oncogene transformed cells. Possible mechanisms of this delay are explored. In addition, our data indicate that prolonged mitogenic stimulation does not necessarily result in constitutive activation of Erk1 and Erk2.|
|H Greulich; C Reichman; H Hanafusa|
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|Type: Comparative Study; Journal Article; Research Support, U.S. Gov't, P.H.S.|
|Title: Oncogene Volume: 12 ISSN: 0950-9232 ISO Abbreviation: Oncogene Publication Date: 1996 Apr|
|Created Date: 1996-06-18 Completed Date: 1996-06-18 Revised Date: 2009-11-19|
Medline Journal Info:
|Nlm Unique ID: 8711562 Medline TA: Oncogene Country: ENGLAND|
|Languages: eng Pagination: 1689-95 Citation Subset: IM|
|Laboratory of Molecular Oncology, Rockefeller University, New York, NY 10021, USA.|
|APA/MLA Format Download EndNote Download BibTex|
Calcium-Calmodulin-Dependent Protein Kinases / drug effects, genetics, metabolism*
Cell Cycle Proteins*
Cell Line, Transformed
Cell Transformation, Neoplastic*
Culture Media, Serum-Free
Dual Specificity Phosphatase 1
Enzyme Activation / drug effects, genetics*
Immediate-Early Proteins / genetics, metabolism
Mitogen-Activated Protein Kinase 1
Mitogen-Activated Protein Kinase 3
Mitogen-Activated Protein Kinase Kinases
Mitogen-Activated Protein Kinases*
Oncogene Protein v-crk
Protein Kinases / metabolism
Protein Phosphatase 1
Protein Tyrosine Phosphatases / genetics, metabolism
Protein-Tyrosine Kinases / drug effects, genetics, metabolism*
Receptor, Epidermal Growth Factor / metabolism
Retroviridae Proteins, Oncogenic / genetics
|CA09673-19/CA/NCI NIH HHS; CA44356/CA/NCI NIH HHS|
|0/Cell Cycle Proteins; 0/Culture Media, Serum-Free; 0/Immediate-Early Proteins; 0/Oncogene Protein v-crk; 0/Retroviridae Proteins, Oncogenic; EC 2.7.-/Protein Kinases; EC 22.214.171.124/Protein-Tyrosine Kinases; EC 126.96.36.199/Receptor, Epidermal Growth Factor; EC 188.8.131.52/Calcium-Calmodulin-Dependent Protein Kinases; EC 184.108.40.206/Mitogen-Activated Protein Kinase 1; EC 220.127.116.11/Mitogen-Activated Protein Kinase 3; EC 18.104.22.168/Mitogen-Activated Protein Kinases; EC 22.214.171.124/Mitogen-Activated Protein Kinase Kinases; EC 126.96.36.199/Phosphoprotein Phosphatases; EC 188.8.131.52/Protein Phosphatase 1; EC 184.108.40.206/Dual Specificity Phosphatase 1; EC 220.127.116.11/Dusp1 protein, rat; EC 18.104.22.168/Protein Tyrosine Phosphatases|
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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