MersV1, Istex, Corpus, bibRecord, 002228

Prions and Transmissible Spongiform Encephalopathy (TSE) Chemotherapeutics: A Common Mechanism for Anti-TSE Compounds?

Identifieur interne : 002228 ( Istex/Corpus ); précédent : 002227; suivant : 002229

Prions and Transmissible Spongiform Encephalopathy (TSE) Chemotherapeutics: A Common Mechanism for Anti-TSE Compounds?

Auteurs : B. Caughey ; W. S. Caughey ; D. A. Kocisko ; K. S. Lee ; J. R. Silveira ; J. D. Morrey

Source :

Accounts of Chemical Research [ 0001-4842 ] ; 2006.

RBID : ISTEX:D9570AA45CF61601F20362B4B3A0592330E2FCCE

Abstract

No validated treatments exist for transmissible spongiform encephalopathies (TSEs or prion diseases) in humans or livestock. The search for TSE therapeutics is complicated by persistent uncertainties about the nature of mammalian prions and their pathogenic mechanisms. In pursuit of anti-TSE drugs, we and others have focused primarily on blocking conversion of normal prion protein, PrPC, to the TSE-associated isoform, PrPSc. Recently developed high-throughput screens have hastened the identification of new inhibitors with strong in vivo anti-TSE activities such as porphyrins, phthalocyanines, and phosphorthioated oligonucleotides. New routes of administration have enhanced beneficial effects against established brain infections. Several different classes of TSE inhibitors share structural similarities, compete for the same site(s) on PrPC, and induce the clustering and internalization of PrPC from the cell surface. These activities may represent a common mechanism of action for these anti-TSE compounds.

Url:

https://api.istex.fr/ark:/67375/TPS-M5BVJGWB-R/fulltext.pdf

DOI: 10.1021/ar050068p

Links to Exploration step

ISTEX:D9570AA45CF61601F20362B4B3A0592330E2FCCE

Le document en format XML

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<forename type="first">K. S.</forename>
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<affiliation><orgName type="institution">National Institute of Allergy and Infectious Diseases</orgName>
<orgName type="institution">National Institutes of Health</orgName>
<orgName type="laboratory">Rocky Mountain Laboratories</orgName>
<address><addrLine>Hamilton</addrLine>
<addrLine>Montana</addrLine>
<addrLine>and Institute for Antiviral Research</addrLine>
<addrLine>Animal</addrLine>
<addrLine>Dairy and Veterinary Sciences Department</addrLine>
<addrLine>Utah State University</addrLine>
<addrLine>Logan</addrLine>
<addrLine>Utah</addrLine>
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<note place="foot" n="ar050068pAF2"><ref>†</ref>
<p>
 National Institute of Allergy and Infectious Diseases.</p>
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<author xml:id="author-0004"><persName><surname>Silveira</surname>
<forename type="first">J. R.</forename>
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<affiliation><orgName type="institution">National Institute of Allergy and Infectious Diseases</orgName>
<orgName type="institution">National Institutes of Health</orgName>
<orgName type="laboratory">Rocky Mountain Laboratories</orgName>
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<addrLine>Animal</addrLine>
<addrLine>Dairy and Veterinary Sciences Department</addrLine>
<addrLine>Utah State University</addrLine>
<addrLine>Logan</addrLine>
<addrLine>Utah</addrLine>
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<note place="foot" n="ar050068pAF2"><ref>†</ref>
<p>
 National Institute of Allergy and Infectious Diseases.</p>
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<author xml:id="author-0005"><persName><surname>Morrey</surname>
<forename type="first">J. D.</forename>
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<affiliation><orgName type="institution">National Institute of Allergy and Infectious Diseases</orgName>
<orgName type="institution">National Institutes of Health</orgName>
<orgName type="laboratory">Rocky Mountain Laboratories</orgName>
<address><addrLine>Hamilton</addrLine>
<addrLine>Montana</addrLine>
<addrLine>and Institute for Antiviral Research</addrLine>
<addrLine>Animal</addrLine>
<addrLine>Dairy and Veterinary Sciences Department</addrLine>
<addrLine>Utah State University</addrLine>
<addrLine>Logan</addrLine>
<addrLine>Utah</addrLine>
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<note place="foot" n="ar050068pAF3"><ref>‡</ref>
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 Utah State University.</p>
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<profileDesc><abstract><p>No validated treatments exist for transmissible spongiform encephalopathies (TSEs or prion diseases) in humans or livestock.
The search for TSE therapeutics is complicated by persistent
uncertainties about the nature of mammalian prions and their
pathogenic mechanisms. In pursuit of anti-TSE drugs, we and
others have focused primarily on blocking conversion of normal
prion protein, PrP<hi rend="superscript">C</hi>
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developed high-throughput screens have hastened the identification of new inhibitors with strong in vivo anti-TSE activities such
as porphyrins, phthalocyanines, and phosphorthioated oligonucleotides. New routes of administration have enhanced beneficial
effects against established brain infections. Several different classes
of TSE inhibitors share structural similarities, compete for the same
site(s) on PrP<hi rend="superscript">C</hi>, and induce the clustering and internalization of
PrP<hi rend="superscript">C</hi> from the cell surface. These activities may represent a
common mechanism of action for these anti-TSE compounds.
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<title-group><article-title>Prions and Transmissible
Spongiform Encephalopathy
(TSE) Chemotherapeutics:  A
Common Mechanism for Anti-TSE
Compounds?</article-title>
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<contrib-group><contrib contrib-type="author" corresp="yes"><name><surname>Caughey</surname>
<given-names>B.</given-names>
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<xref rid="ar050068pAF1">*</xref>
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<given-names>W. S.</given-names>
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<contrib contrib-type="author"><name><surname>Lee</surname>
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<xref rid="ar050068pAF2">†</xref>
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<contrib contrib-type="author"><name><surname>Morrey</surname>
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<xref rid="ar050068pAF3">‡</xref>
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<aff>National Institute of Allergy and Infectious Diseases,
National Institutes of Health, Rocky Mountain Laboratories,
Hamilton, Montana, and Institute for Antiviral Research,
Animal, Dairy and Veterinary Sciences Department, Utah
State University, Logan, Utah
</aff>
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<author-notes><corresp id="ar050068pAF1">
 Corresponding author. Mailing address:  Rocky Mountain Labs, 903
S. 4th St., Hamilton, MT 59840. Phone:  (406) 363 9264. Fax:  (406) 363
9286. E-mail:  bcaughey@nih.gov.</corresp>
<fn id="ar050068pAF2"><label>†</label>
<p>
 National Institute of Allergy and Infectious Diseases.</p>
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<fn id="ar050068pAF3"><label>‡</label>
<p>
 Utah State University.</p>
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<abstract><p>No validated treatments exist for transmissible spongiform encephalopathies (TSEs or prion diseases) in humans or livestock.
The search for TSE therapeutics is complicated by persistent
uncertainties about the nature of mammalian prions and their
pathogenic mechanisms. In pursuit of anti-TSE drugs, we and
others have focused primarily on blocking conversion of normal
prion protein, PrP<sup>C</sup>
, to the TSE-associated isoform, PrP<sup>Sc</sup>. Recently
developed high-throughput screens have hastened the identification of new inhibitors with strong in vivo anti-TSE activities such
as porphyrins, phthalocyanines, and phosphorthioated oligonucleotides. New routes of administration have enhanced beneficial
effects against established brain infections. Several different classes
of TSE inhibitors share structural similarities, compete for the same
site(s) on PrP<sup>C</sup>, and induce the clustering and internalization of
PrP<sup>C</sup> from the cell surface. These activities may represent a
common mechanism of action for these anti-TSE compounds.
</p>
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Prions and Transmissible Spongiform Encephalopathy (TSE) Chemotherapeutics: A Common Mechanism for Anti-TSE Compounds?

Prions and Transmissible Spongiform Encephalopathy (TSE) Chemotherapeutics: A Common Mechanism for Anti-TSE Compounds?

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