| http://purl.uniprot.org/citations/14983221 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/14983221 | http://www.w3.org/2000/01/rdf-schema#comment | "We have recently shown that the NH(2)-terminal fragment (PrP23-110) of the human cellular prion protein (PrP(c) ) stimulates t-PA mediated plasminogen activation. PrP23-110 contains an N-terminal lysine cluster (LC1; K(23),K(24), K(27)) and a C-terminal one (LC2; K(101),K(104),K(106),K(110)). To study their biological function we have substituted all lysine residues of each cluster by alanine and generated the recombinant PrP proteins PrP23-110sLC1 and PrP23-110sLC2. The ability of the mutant proteins to stimulate plasminogen activation was assayed. We found that both lysine clusters are essential for t-PA mediated plasminogen activation. We further studied the binding of soluble PrP23-110 to immobilized t-PA or plasminogen using surface plasmon resonance. The recorded binding curves could not be modeled by classical 1:1 binding kinetics suggesting oligomerisation of PrP23-110. Further plasmon resonance studies show that indeed PrP23-110 binds to itself and that glycosaminoglycans modify this interaction. Binding of t-PA or plasminogen to PrP23-110 was no longer influenced by glycosaminoglycans when PrP23-110 was immobilized on the chip surface. Thus a possible role of heparin as a cofactor in the stimulation of plasminogen activation by t-PA could be the generation of a PrP23-110 form with both lysine clusters accessible for binding of t-PA and plasminogen."xsd:string |
| http://purl.uniprot.org/citations/14983221 | http://purl.org/dc/terms/identifier | "doi:10.1160/th03-06-0382"xsd:string |
| http://purl.uniprot.org/citations/14983221 | http://purl.uniprot.org/core/author | "Baier M."xsd:string |
| http://purl.uniprot.org/citations/14983221 | http://purl.uniprot.org/core/author | "Schleuning W.D."xsd:string |
| http://purl.uniprot.org/citations/14983221 | http://purl.uniprot.org/core/author | "Gessner R."xsd:string |
| http://purl.uniprot.org/citations/14983221 | http://purl.uniprot.org/core/author | "Epple G."xsd:string |
| http://purl.uniprot.org/citations/14983221 | http://purl.uniprot.org/core/author | "Praus M."xsd:string |
| http://purl.uniprot.org/citations/14983221 | http://purl.uniprot.org/core/author | "Holzhutter H.G."xsd:string |
| http://purl.uniprot.org/citations/14983221 | http://purl.uniprot.org/core/author | "Kottgen E."xsd:string |
| http://purl.uniprot.org/citations/14983221 | http://purl.uniprot.org/core/author | "Langfeld K."xsd:string |
| http://purl.uniprot.org/citations/14983221 | http://purl.uniprot.org/core/date | "2004"xsd:gYear |
| http://purl.uniprot.org/citations/14983221 | http://purl.uniprot.org/core/name | "Thromb Haemost"xsd:string |
| http://purl.uniprot.org/citations/14983221 | http://purl.uniprot.org/core/pages | "465-472"xsd:string |
| http://purl.uniprot.org/citations/14983221 | http://purl.uniprot.org/core/title | "Both lysine-clusters of the NH2-terminal prion-protein fragment PrP23-110 are essential for t-PA mediated plasminogen activation."xsd:string |
| http://purl.uniprot.org/citations/14983221 | http://purl.uniprot.org/core/volume | "91"xsd:string |
| http://purl.uniprot.org/citations/14983221 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/14983221 |
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