Proteínas de prión : de la patogénesis a la función

Lade...
Vorschaubild
Dateien
Mensaje_Bioq06v30p167_184_Edward_Malaga.pdf
Mensaje_Bioq06v30p167_184_Edward_Malaga.pdfGröße: 1.62 MBDownloads: 1322
Datum
2006
Herausgeber:innen
Kontakt
ISSN der Zeitschrift
Electronic ISSN
ISBN
Bibliografische Daten
Verlag
Schriftenreihe
Auflagebezeichnung
DOI (zitierfähiger Link)
ArXiv-ID
Internationale Patentnummer
Angaben zur Forschungsförderung
Projekt
Open Access-Veröffentlichung
Open Access Green
Sammlungen
Core Facility der Universität Konstanz
Gesperrt bis
Titel in einer weiteren Sprache
Forschungsvorhaben
Organisationseinheiten
Zeitschriftenheft
Publikationstyp
Zeitschriftenartikel
Publikationsstatus
Published
Erschienen in
Mensaje Bioquímico. 2006, 30, pp. 167-184. ISSN 0188-137X
Zusammenfassung

The prion protein (PrP) is a membrane-anchored glycoprotein normally present in all vertebrates. Under unusual circumstances, it can undergo structural transformation and become the sole constituent of prions, a unique class of infectious agent devoid of nucleic acid. Prions are the cause of a group of lethal neurodegenerative disorders that include Creutzfeldt-Jakob disease (CJD) in humans and bovine spongiform encephalopathy (BSE) or “mad cow disease”. Much is known about PrP’s pathogenic properties; however, its natural role remains elusive despite extensive characterization of its biochemical and cellular properties. Here we review prion diseases and their molecular basis, as well as the evolution and function of prion proteins. We include work carried out in our laboratory, particularly our analysis of PrP loss-of-function phenotypes in the zebrafish and the heterologous expression of various vertebrate PrPs in zebrafish, mouse and Drosophila cells. Our data show that an evolutionarily conserved function of all vertebtrate PrPs is the establishment of homotypic trans-interactions between neighboring cells, thus mediating cell contact formation and signaling via lipid rafts.

Zusammenfassung in einer weiteren Sprache
Fachgebiet (DDC)
570 Biowissenschaften, Biologie
Schlagwörter
prion proteins, transmissible spongiform encephalopathies, neurodegenerative diseases, species barrier, molecular evolution, zebrafish
Konferenz
Rezension
undefined / . - undefined, undefined
Zitieren
ISO 690MÁLAGA-TRILLO, Edward, Gonzalo SOLIS PADILLA, 2006. Proteínas de prión : de la patogénesis a la función. In: Mensaje Bioquímico. 2006, 30, pp. 167-184. ISSN 0188-137X
BibTex
@article{MalagaTrillo2006Prote-18385,
  year={2006},
  title={Proteínas de prión : de la patogénesis a la función},
  volume={30},
  issn={0188-137X},
  journal={Mensaje Bioquímico},
  pages={167--184},
  author={Málaga-Trillo, Edward and Solis Padilla, Gonzalo}
}
RDF
<rdf:RDF
    xmlns:dcterms="http://purl.org/dc/terms/"
    xmlns:dc="http://purl.org/dc/elements/1.1/"
    xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#"
    xmlns:bibo="http://purl.org/ontology/bibo/"
    xmlns:dspace="http://digital-repositories.org/ontologies/dspace/0.1.0#"
    xmlns:foaf="http://xmlns.com/foaf/0.1/"
    xmlns:void="http://rdfs.org/ns/void#"
    xmlns:xsd="http://www.w3.org/2001/XMLSchema#" > 
  <rdf:Description rdf:about="https://kops.uni-konstanz.de/server/rdf/resource/123456789/18385">
    <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/>
    <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
    <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/18385"/>
    <dc:creator>Solis Padilla, Gonzalo</dc:creator>
    <dc:creator>Málaga-Trillo, Edward</dc:creator>
    <foaf:homepage rdf:resource="http://localhost:8080/"/>
    <dc:rights>terms-of-use</dc:rights>
    <dcterms:rights rdf:resource="https://rightsstatements.org/page/InC/1.0/"/>
    <dcterms:hasPart rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/18385/2/Mensaje_Bioq06v30p167_184_Edward_Malaga.pdf"/>
    <dc:contributor>Málaga-Trillo, Edward</dc:contributor>
    <dcterms:abstract xml:lang="spa">The prion protein (PrP) is a membrane-anchored glycoprotein normally present in all vertebrates. Under unusual circumstances, it can undergo structural transformation and become the sole constituent of prions, a unique class of infectious agent devoid of nucleic acid. Prions are the cause of a group of lethal neurodegenerative disorders that include Creutzfeldt-Jakob disease (CJD) in humans and bovine spongiform encephalopathy (BSE) or “mad cow disease”. Much is known about PrP’s pathogenic properties; however, its natural role remains elusive despite extensive characterization of its biochemical and cellular properties. Here we review prion diseases and their molecular basis, as well as the evolution and function of prion proteins. We include work carried out in our laboratory, particularly our analysis of PrP loss-of-function phenotypes in the zebrafish and the heterologous expression of various vertebrate PrPs in zebrafish, mouse and Drosophila cells. Our data show that an evolutionarily conserved function of all vertebtrate PrPs is the establishment of homotypic trans-interactions between neighboring cells, thus mediating cell contact formation and signaling via lipid rafts.</dcterms:abstract>
    <dc:contributor>Solis Padilla, Gonzalo</dc:contributor>
    <dc:language>spa</dc:language>
    <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2012-02-14T12:32:13Z</dc:date>
    <dcterms:bibliographicCitation>Publ. in:  Mensaje Bioquímico ; 30 (2006). - S. 167-184</dcterms:bibliographicCitation>
    <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
    <dcterms:issued>2006</dcterms:issued>
    <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2012-02-14T12:32:13Z</dcterms:available>
    <dspace:hasBitstream rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/18385/2/Mensaje_Bioq06v30p167_184_Edward_Malaga.pdf"/>
    <dcterms:title>Proteínas de prión : de la patogénesis a la función</dcterms:title>
  </rdf:Description>
</rdf:RDF>
Interner Vermerk
xmlui.Submission.submit.DescribeStep.inputForms.label.kops_note_fromSubmitter
Kontakt
URL der Originalveröffentl.
Prüfdatum der URL
Prüfungsdatum der Dissertation
Finanzierungsart
Kommentar zur Publikation
Allianzlizenz
Corresponding Authors der Uni Konstanz vorhanden
Internationale Co-Autor:innen
Universitätsbibliographie
Ja
Begutachtet
Diese Publikation teilen