Document Detail


Differential expression of cell-cell adhesion proteins and cyclin D in MEK1-transdifferentiated MDCK cells.
MedLine Citation:
PMID:  11029295     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Overexpression of a constitutively active mutant of the mitogen-activated protein kinase kinase MEK1 (caMEK1) in epithelial Madin-Darby canine kidney (MDCK)-C7 cells disrupts morphogenesis, induces an invasive phenotype, and is associated with a reduced rate of cell proliferation. The role of cell-cell adhesion molecules and cell cycle proteins in these processes, however, has not been investigated. We now report loss of E-cadherin expression as well as a marked reduction of beta- and alpha-catenin expression in transdifferentiated MDCK-C7 cells stably expressing caMEK1 (C7caMEK1) compared with epithelial mock-transfected MDCK-C7 (C7Mock1) cells. At least part of the remaining alpha-catenin was coimmunoprecipitated with beta-catenin, whereas no E-cadherin was detected in beta-catenin immunoprecipitates. In both cell types, the proteasome-specific protease inhibitors N-acetyl-Leu-Leu-norleucinal (ALLN) and lactacystin led to a time-dependent accumulation of beta-catenin, including the appearance of high-molecular-weight beta-catenin species. Quiescent as well as serum-stimulated C7caMEK1 cells showed a higher cyclin D expression than epithelial C7Mock1 cells. The MEK inhibitor U-0126 inhibited extracellular signal-regulated kinase phosphorylation and cyclin D expression in C7caMEK1 cells and almost abolished their already reduced cell proliferation rate. We conclude that the transdifferentiated and invasive phenotype of C7caMEK1 cells is associated with a diminished expression of proteins involved in cell-cell adhesion. Although beta-catenin expression is reduced, C7caMEK1 cells show a higher expression of U-0126-sensitive cyclin D protein.
Authors:
I Marschitz; J Lechner; I Mosser; M Dander; R Montesano; H Schramek
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  American journal of physiology. Cell physiology     Volume:  279     ISSN:  0363-6143     ISO Abbreviation:  Am. J. Physiol., Cell Physiol.     Publication Date:  2000 Nov 
Date Detail:
Created Date:  2000-10-30     Completed Date:  2000-11-16     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  100901225     Medline TA:  Am J Physiol Cell Physiol     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  C1472-82     Citation Subset:  IM    
Affiliation:
Department of Physiology, University of Innsbruck, A-6010 Innsbruck, Austria.
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MeSH Terms
Descriptor/Qualifier:
Animals
Cadherins / metabolism
Cell Adhesion Molecules / metabolism*
Cell Differentiation / physiology
Cell Division / physiology
Cell Line / cytology
Cyclin D
Cyclins / metabolism*
Cysteine Endopeptidases / physiology
Cytoskeletal Proteins / metabolism
Dogs
Kidney / cytology,  metabolism
MAP Kinase Kinase 1
Mitogen-Activated Protein Kinase Kinases / genetics,  physiology*
Multienzyme Complexes / physiology
Peptide Hydrolases / metabolism
Proteasome Endopeptidase Complex
Protein-Serine-Threonine Kinases / genetics,  physiology*
Trans-Activators*
Transfection
alpha Catenin
beta Catenin
Chemical
Reg. No./Substance:
0/Cadherins; 0/Cell Adhesion Molecules; 0/Cyclin D; 0/Cyclins; 0/Cytoskeletal Proteins; 0/Multienzyme Complexes; 0/Trans-Activators; 0/alpha Catenin; 0/beta Catenin; EC 2.7.11.1/Protein-Serine-Threonine Kinases; EC 2.7.12.2/MAP Kinase Kinase 1; EC 2.7.12.2/Mitogen-Activated Protein Kinase Kinases; EC 3.4.-/Peptide Hydrolases; EC 3.4.22.-/Cysteine Endopeptidases; EC 3.4.25.1/Proteasome Endopeptidase Complex

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