Document Detail


Diphtheria toxin receptor. Identification of specific diphtheria toxin-binding proteins on the surface of Vero and BS-C-1 cells.
MedLine Citation:
PMID:  3654609     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The biochemical characteristics of specific receptor molecules for diphtheria toxin on the surface of two toxin-sensitive cell lines (Vero and BS-C-1) were examined. Diphtheria toxin was found to bind to a number of different proteins in Nonidet P-40 solubilized extracts of 125I-labeled cells. In contrast, permitting diphtheria toxin to bind first to labeled intact cells, which were subsequently solubilized and subjected to immunoprecipitation with anti-diphtheria toxin, resulted in a far more restricted profile of diphtheria toxin-binding proteins that possessed Mrs in the range of 10,000-20,000. Direct chemical cross-linking of radioiodinated diphtheria toxin to cell surface proteins resulted in the appearance of several predominant bands possessing Mrs of approximately 80,000. The Mr approximately 80,000 complexes were shown to be composed of radiolabeled diphtheria toxin (Mr 60,000) and unlabeled Mr approximately 20,000 cellular proteins. These complexes were judged to be a result of specific binding in that their appearance could be preferentially inhibited by the addition of a 100-fold excess of unlabeled diphtheria toxin. The formation of the Mr approximately 80,000 complexes was sensitive to prior trypsin treatment of the cells and to known inhibitors of diphtheria toxin binding. Furthermore, prior incubation of the cells with diphtheria toxin at 37 degrees C ("down regulation") markedly and specifically reduced the subsequent formation of the Mr approximately 80,000 cross-linked complexes, and these down-regulated cells were less sensitive to diphtheria toxin in cytotoxicity assays. Further incubation of down-regulated cells at 37 degrees C restored their ability to form Mr approximately 80,000 complexes; this regeneration requires protein synthesis and restores the cells' sensitivity to diphtheria toxin-mediated cytotoxicity. These results strongly suggest that a Mr 10,000-20,000 cell surface protein is, or constitutes a portion of, the functional diphtheria toxin receptor.
Authors:
W Cieplak; H M Gaudin; L Eidels
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  262     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  1987 Sep 
Date Detail:
Created Date:  1987-11-02     Completed Date:  1987-11-02     Revised Date:  2007-11-15    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  13246-53     Citation Subset:  IM    
Affiliation:
Department of Microbiology, University of Texas Health Science Center at Dallas 75235.
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MeSH Terms
Descriptor/Qualifier:
Animals
Cell Line
Cell Membrane / metabolism*
Cell Survival / drug effects
Diphtheria Toxin / metabolism*,  toxicity
Humans
Intercellular Signaling Peptides and Proteins
Kinetics
Molecular Weight
Receptors, Cell Surface*
Receptors, Cholinergic / isolation & purification,  metabolism*
Vero Cells
Grant Support
ID/Acronym/Agency:
AI-16805/AI/NIAID NIH HHS; CA-09082/CA/NCI NIH HHS
Chemical
Reg. No./Substance:
0/Diphtheria Toxin; 0/Intercellular Signaling Peptides and Proteins; 0/Receptors, Cell Surface; 0/Receptors, Cholinergic; 149176-25-0/heparin-binding EGF-like growth factor

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


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