Document Detail


P120 catenin is associated with desmogleins when desmosomes are assembled in high-Ca2+ medium but not when disassembled in low-Ca2+ medium in DJM-1 cells.
MedLine Citation:
PMID:  18578707     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
We recently showed that p120 catenin (p120ctn), which is an armadillo family protein member that binds to E-cadherin (E-cad), is also localized to desmosomes by directly or indirectly binding to desmogleins (Dsg). We examined whether p120ctn is associated with Dsg1 and Dsg3, as compared with E-cad and plakoglobin (PG), in keratinocytes grown in high or low Ca2+, using a human squamous cell carcinoma cell line, DJM-1 cells. The cell lysate of DJM-1 cells grown in high- or low-Ca2+ media was immunoprecipitated with anti-Dsg1/2 and Dsg3 antibodies, and we examined whether p120ctn is associated with Dsg1 and Dsg3. Then, we observed the co-localization between Dsg3 and p120ctn in cells grown in high- or low-Ca2+ medium on double-staining immunofluorescence microscopy using anti-p120ctn and anti-Dsg3 antibodies. Immunoprecipitates with anti-Dsg1/2 and Dsg3 antibodies in cells grown in high-Ca2+ medium contained p120ctn. In contrast, in low-Ca2+ medium, p120ctn was co-immunoprecipitated with neither Dsg1 nor Dsg3, but was co-immunoprecipitated with E-cad in cells grown in both high- and low-Ca2+ media. Dsg3 was associated with PG in cells grown in both low- and high-Ca2+ media. On immunofluorescence microscopy, p120ctn and Dsg3 were independently observed in cells grown in low-Ca2+ medium; p120ctn, but not Dsg3, was observed in a linear pattern at the cell-cell boundary. However, they were co-localized at cell-cell contacts in cells grown in high-Ca2+ medium. Thus, these proteins are not co-localized in low Ca2+ medium. These results suggest that p120ctn plays an important role in Ca2+-induced desmosome formation.
Authors:
Miho Kanno; Yumi Aoyama; Yasuka Isa; Yukari Yamamoto; Yasuo Kitajima
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  The Journal of dermatology     Volume:  35     ISSN:  0385-2407     ISO Abbreviation:  J. Dermatol.     Publication Date:  2008 Jun 
Date Detail:
Created Date:  2008-06-26     Completed Date:  2008-09-19     Revised Date:  2010-01-29    
Medline Journal Info:
Nlm Unique ID:  7600545     Medline TA:  J Dermatol     Country:  Japan    
Other Details:
Languages:  eng     Pagination:  317-24     Citation Subset:  IM    
Affiliation:
Department of Dermatology, Gifu University School of Medicine, Gifu City, Japan.
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MeSH Terms
Descriptor/Qualifier:
Antibodies, Monoclonal
Blotting, Western
Cadherins / metabolism*
Calcium / metabolism*
Cell Adhesion Molecules / chemistry,  metabolism*,  physiology
Cell Line, Tumor
Cells, Cultured
Culture Media / chemistry
Desmoglein 1 / metabolism*
Desmoglein 3 / metabolism*
Desmosomes / metabolism*
Humans
Immunoprecipitation
Keratinocytes / metabolism*,  physiology
Microscopy, Fluorescence
Phosphoproteins / chemistry,  metabolism*,  physiology
Protein Isoforms / metabolism
gamma Catenin / metabolism
Chemical
Reg. No./Substance:
0/Antibodies, Monoclonal; 0/Cadherins; 0/Cell Adhesion Molecules; 0/Culture Media; 0/Desmoglein 1; 0/Desmoglein 3; 0/Phosphoproteins; 0/Protein Isoforms; 0/delta catenin; 0/gamma Catenin; 7440-70-2/Calcium

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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