| PDGF-BB-mediated activation of p42(MAPK) is independent of PDGF beta-receptor tyrosine phosphorylation. | |
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MedLine Citation:
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PMID: 11557582 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Herein, we investigated the activity of mitogen-activated protein kinase (MAPK), a key component of downstream signaling events, which is activated subsequent to platelet-derived growth factor (PDGF)-BB stimulation. Specifically, p42(MAPK) activity peaked 60 min after addition of PDGF-BB, declined thereafter, and was determined not to be a direct or necessary component of glycosaminoglycan (GAG) synthesis. PDGF-BB also activated MAPK kinase 2 (MAPKK2) but had no effect on MAPKK1 and Raf-1 activity. Chemical inhibition of Janus kinase, phosphatidylinositol 3-kinase, Src kinase, or tyrosine phosphorylation inhibition of the PDGF beta-receptor (PDGFR-beta) did not abrogate PDGF-BB-induced p42(MAPK) activation or its threonine or tyrosine phosphorylation. A dominant negative cytoplasmic receptor for hyaluronan-mediated motility variant 4 (RHAMMv4), a regulator of MAPKK-MAPK interaction and activation, did not inhibit PDGF-BB-induced p42(MAPK) activation nor did a construct expressing PDGFR-beta with cytoplasmic tyrosines mutated to phenylalanine. However, overexpression of a dominant negative PDGFR-beta lacking the cytoplasmic signaling domain abrogated p42(MAPK) activity. These results suggest that PDGF-BB-mediated activation of p42(MAPK) requires the PDGFR-beta but is independent of its tyrosine phosphorylation. |
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Authors:
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N J Cartel; J Liu; J Wang; M Post |
Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: American journal of physiology. Lung cellular and molecular physiology Volume: 281 ISSN: 1040-0605 ISO Abbreviation: Am. J. Physiol. Lung Cell Mol. Physiol. Publication Date: 2001 Oct |
Date Detail:
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Created Date: 2001-09-14 Completed Date: 2001-10-18 Revised Date: 2009-11-19 |
Medline Journal Info:
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Nlm Unique ID: 100901229 Medline TA: Am J Physiol Lung Cell Mol Physiol Country: United States |
Other Details:
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Languages: eng Pagination: L786-98 Citation Subset: IM |
Affiliation:
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Canadian Institutes of Health Research Group in Lung Development, Programme in Lung Biology, Research Institute, Toronto, Ontario, Canada. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Animals Anticoagulants / pharmacology* Benzoquinones Cells, Cultured Enzyme Activation / drug effects Enzyme Inhibitors / pharmacology Female Fibroblasts / cytology, enzymology Lactams, Macrocyclic Lung / cytology, embryology, metabolism MAP Kinase Kinase 2 MAP Kinase Signaling System / drug effects, physiology Male Mitogen-Activated Protein Kinase 1 / metabolism* Mitogen-Activated Protein Kinase Kinases / metabolism Mutagenesis / physiology Phosphorylation Platelet-Derived Growth Factor / pharmacology* Protein-Tyrosine Kinases / metabolism Proto-Oncogene Proteins c-raf / metabolism Quinones / pharmacology Rats Rats, Wistar Receptor, Platelet-Derived Growth Factor beta / genetics, metabolism* Threonine / metabolism Transfection Tyrosine / metabolism Tyrphostins / pharmacology |
| Chemical | |
Reg. No./Substance:
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0/Anticoagulants; 0/Benzoquinones; 0/Enzyme Inhibitors; 0/Lactams, Macrocyclic; 0/Platelet-Derived Growth Factor; 0/Quinones; 0/Tyrphostins; 0/platelet-derived growth factor BB; 55520-40-6/Tyrosine; 70563-58-5/herbimycin; 71308-35-5/tyrphostin AG17; 72-19-5/Threonine; EC 2.7.10.1/Protein-Tyrosine Kinases; EC 2.7.10.1/Receptor, Platelet-Derived Growth Factor beta; EC 2.7.11.1/Proto-Oncogene Proteins c-raf; EC 2.7.11.24/Mitogen-Activated Protein Kinase 1; EC 2.7.12.2/MAP Kinase Kinase 2; EC 2.7.12.2/Mitogen-Activated Protein Kinase Kinases |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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