Document Detail


Binding of the protease-sensitive form of PrP (prion protein) to sulfated glycosaminoglycan and congo red [corrected]
MedLine Citation:
PMID:  7511169     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Congo red and certain sulfated glycans are potent inhibitors of protease-resistant PrP accumulation in scrapie-infected cells. One hypothesis is that these inhibitors act by blocking the association between protease-resistant PrP and sulfated glycosaminoglycans or proteoglycans (e.g., heparan sulfate proteoglycan) that is observed in amyloid plaques of scrapie-infected brain tissue. Accordingly, we have investigated whether the apparent precursor of protease-resistant PrP, protease-sensitive PrP, binds to Congo red and heparin, a highly sulfated glycosaminoglycan with an inhibitory potency like that of heparan sulfate. Protease-sensitive PrP released from the surface of mouse neuroblastoma cells bound to heparin-agarose and Congo red-glass beads. Sucrose density gradient fractionation provided evidence that at least some of the PrP capable of binding heparin-agarose was monomeric. Free Congo red blocked PrP binding to heparin and vice versa, suggesting that these ligands share a common binding site. The relative efficacies of pentosan polysulfate, Congo red, heparin, and chondroitin sulfate in blocking PrP binding to heparin-agarose corresponded with their previously demonstrated potencies in inhibiting protease-resistant PrP accumulation. These results are consistent with the idea that sulfated glycans and Congo red inhibit protease-resistant PrP accumulation by interfering with the interaction of PrP with an endogenous glycosaminoglycan or proteoglycan.
Authors:
B Caughey; K Brown; G J Raymond; G E Katzenstein; W Thresher
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Journal of virology     Volume:  68     ISSN:  0022-538X     ISO Abbreviation:  J. Virol.     Publication Date:  1994 Apr 
Date Detail:
Created Date:  1994-04-25     Completed Date:  1994-04-25     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  0113724     Medline TA:  J Virol     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  2135-41     Citation Subset:  IM    
Affiliation:
Laboratory of Persistent Viral Diseases, Rocky Mountain Laboratories, National Institute for Allergy and Infectious Diseases, Hamilton, Montana 59840.
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MeSH Terms
Descriptor/Qualifier:
Animals
Congo Red / metabolism*
Endopeptidases / metabolism
Glass
Heparan Sulfate Proteoglycans
Heparitin Sulfate / metabolism*
Mice
Nerve Tissue / metabolism
Nerve Tissue Proteins / immunology,  isolation & purification,  metabolism*
Pentosan Sulfuric Polyester / pharmacology
PrPSc Proteins
Precipitin Tests
Prions / immunology,  isolation & purification,  metabolism*
Protein Binding / drug effects
Protein Precursors / immunology,  isolation & purification,  metabolism*
Proteoglycans / metabolism*
Tumor Cells, Cultured
Chemical
Reg. No./Substance:
0/Heparan Sulfate Proteoglycans; 0/Nerve Tissue Proteins; 0/PrPSc Proteins; 0/Prions; 0/Protein Precursors; 0/Proteoglycans; 37300-21-3/Pentosan Sulfuric Polyester; 573-58-0/Congo Red; 9050-30-0/Heparitin Sulfate; EC 3.4.-/Endopeptidases
Comments/Corrections
Erratum In:
J Virol 1994 Jun;68(6):4107

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


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