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Restricted tissue distribution of a 37-kD possible adherens junction protein.
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MedLine Citation:
PMID:  1469056     Owner:  NLM     Status:  MEDLINE    
A major polypeptide of M(r) 37,000 was purified from a desmosome-enriched citric acid-insoluble pellet of pig tongue epithelium. The polypeptide was solubilized from the 4-M urea-insoluble pellet with 9 M urea, and extracts were separated by carboxymethyl cellulose and gel filtration chromatography. The 37-kD protein was obtained in milligram quantities as a single band on two-dimensional gels in 30% yield after 21-fold purification from the citric acid-insoluble fraction. The protein is not glycosylated and has a pI of approximately 8.7. Although isolated from a fraction rich in desmosomes, the 37-kD protein is not a desmosomal protein. Indirect immunofluorescence analysis of frozen sections of tongue and other tissues demonstrated that antibodies raised to the 37-kD protein bound only to suprabasal cell layers at punctate regions of the periphery of the cell and was absent from most regions of epidermis, whereas antibodies to desmoplakins I and II, desmosomal proteins, bound similarly but in all epidermal layers. Immunoelectron microscopy localized the 37-kD protein to the cell periphery in regions between, but never in, desmosomes. By immunofluorescence, the 37-kD protein colocalized with actin as well as with vinculin and uvomorulin in oral tissues. Like the 37-kD protein, vinculin and uvomorulin were absent from the basal layer. Based on its appearance, localization, and solubility properties, the 37-kD protein is probably a component of adherens junctions; its restriction to suprabasal cells and exclusion from the epidermis are unique.
M L Chiu; J C Jones; E J O'Keefe
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  The Journal of cell biology     Volume:  119     ISSN:  0021-9525     ISO Abbreviation:  J. Cell Biol.     Publication Date:  1992 Dec 
Date Detail:
Created Date:  1993-01-27     Completed Date:  1993-01-27     Revised Date:  2010-09-07    
Medline Journal Info:
Nlm Unique ID:  0375356     Medline TA:  J Cell Biol     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  1689-700     Citation Subset:  IM    
Department of Dermatology, University of North Carolina, Chapel Hill 27514.
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MeSH Terms
Actins / isolation & purification
Amino Acids / analysis
Antigens, CD
Cadherins / isolation & purification
Cell Adhesion Molecules / isolation & purification*
Desmosomes / chemistry
Epithelial Cells
Epithelium / chemistry,  ultrastructure
Intercellular Junctions / chemistry*
Isoelectric Point
Molecular Weight
Tissue Distribution
Tongue / chemistry*,  cytology,  ultrastructure
Vinculin / isolation & purification
Grant Support
Reg. No./Substance:
0/Actins; 0/Amino Acids; 0/Antigens, CD; 0/CDH2 protein, human; 0/Cadherins; 0/Cell Adhesion Molecules; 125361-02-6/Vinculin

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Journal Information
Journal ID (nlm-ta): J Cell Biol
Journal ID (publisher-id): J. Cell Biol.
ISSN: 0021-9525
ISSN: 1540-8140
Publisher: The Rockefeller University Press
Article Information
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Print publication date: Day: 2 Month: 12 Year: 1992
Volume: 119 Issue: 6
First Page: 1689 Last Page: 1700
ID: 2289738
Publisher Id: 93107168
PubMed Id: 1469056

Restricted tissue distribution of a 37-kD possible adherens junction protein

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