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Microdeletions within the hydrophobic core region of cellular prion protein alter its topology and metabolism

Microdeletions within the hydrophobic core region of cellular prion protein alter its topology and metabolism

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LUTZ, Jens, Christine BRABECK, Hartmut H. NIEMANN, Ulrich KLOZ, Carsten KORTH, Vishwanath R. LINGAPPA, Alexander BÜRKLE, 2010. Microdeletions within the hydrophobic core region of cellular prion protein alter its topology and metabolism. In: Biochemical and Biophysical Research Communications. 393(3), pp. 439-444. ISSN 0006-291X. eISSN 1090-2104. Available under: doi: 10.1016/j.bbrc.2010.02.015

@article{Lutz2010Micro-8448, title={Microdeletions within the hydrophobic core region of cellular prion protein alter its topology and metabolism}, year={2010}, doi={10.1016/j.bbrc.2010.02.015}, number={3}, volume={393}, issn={0006-291X}, journal={Biochemical and Biophysical Research Communications}, pages={439--444}, author={Lutz, Jens and Brabeck, Christine and Niemann, Hartmut H. and Kloz, Ulrich and Korth, Carsten and Lingappa, Vishwanath R. and Bürkle, Alexander} }

<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/rdf/resource/123456789/8448"> <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/rdf/resource/123456789/28"/> <dc:creator>Korth, Carsten</dc:creator> <dspace:hasBitstream rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/8448/1/2010_BiochemBiophysResCommun393.pdf"/> <dc:rights>deposit-license</dc:rights> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:43:45Z</dcterms:available> <dc:creator>Brabeck, Christine</dc:creator> <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/rdf/resource/123456789/28"/> <dcterms:issued>2010</dcterms:issued> <dcterms:bibliographicCitation>First publ. in: Biochemical and Biophysical Research Communications 393 (2010), 3, pp. 439-444</dcterms:bibliographicCitation> <foaf:homepage rdf:resource="http://localhost:8080/jspui"/> <dc:contributor>Bürkle, Alexander</dc:contributor> <dc:format>application/pdf</dc:format> <dcterms:title>Microdeletions within the hydrophobic core region of cellular prion protein alter its topology and metabolism</dcterms:title> <dcterms:hasPart rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/8448/1/2010_BiochemBiophysResCommun393.pdf"/> <dc:creator>Kloz, Ulrich</dc:creator> <dcterms:rights rdf:resource="http://nbn-resolving.org/urn:nbn:de:bsz:352-20140905103416863-3868037-7"/> <dc:creator>Bürkle, Alexander</dc:creator> <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/8448"/> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:43:45Z</dc:date> <dc:contributor>Niemann, Hartmut H.</dc:contributor> <dc:creator>Niemann, Hartmut H.</dc:creator> <dc:contributor>Lutz, Jens</dc:contributor> <dc:contributor>Lingappa, Vishwanath R.</dc:contributor> <dc:creator>Lingappa, Vishwanath R.</dc:creator> <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/> <dc:contributor>Korth, Carsten</dc:contributor> <dcterms:abstract xml:lang="eng">The cellular prion protein (PrPC) is a GPI-anchored cell-surface protein. A small subset of PrPC molecules, however, can be integrated into the ER-membrane via a transmembrane domain (TM), which also harbors the most highly conserved regions of PrPC, termed the hydrophobic core (HC). A mutation in HC is associated with prion disease resulting in an enhanced formation of a transmembrane form (CtmPrP), which has thus been postulated to be a neurotoxic molecule besides PrPSc. To elucidate a possible physiological function of the transmembrane domain, we created a set of mutants carrying microdeletions of 2 8 aminoacids within HC between position 114 and 121. Here, we show that these mutations display reduced propensity for transmembrane topology. In addition, the mutants exhibited alterations in the formation of the C1 proteolytic fragment, which is generated by α-cleavage during normal PrPC metabolism, indicating that HC might function as recognition site for the protease(s) responsible for PrPC α-cleavage. Interestingly, the mutant G113V, corresponding to a hereditary form of prion disease in humans, displayed increased CtmPrP topology and decreased α-cleavage in our in vitro assay. In conclusion, HC represents an essential determinant for transmembrane PrP topology, whereas the high evolutionary conservation of this region is rather based upon preservation of PrPC α-cleavage, thus highlighting the biological importance of this cleavage.</dcterms:abstract> <dc:contributor>Brabeck, Christine</dc:contributor> <dc:creator>Lutz, Jens</dc:creator> <dc:contributor>Kloz, Ulrich</dc:contributor> <dc:language>eng</dc:language> </rdf:Description> </rdf:RDF>

Dateiabrufe seit 01.10.2014 (Informationen über die Zugriffsstatistik)

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