RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/8546712http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8546712http://www.w3.org/2000/01/rdf-schema#comment"The low-density-lipoprotein receptor-related protein (LRP) is a multifunctional receptor involved in the clearance of a large number of diverse ligands, including proteases, protease-inhibitor complexes and lipoproteins. The mature receptor is composed of a 515 kDa and a 85 kDa subunit generated by proteolytic cleavage from a 600 kDa precursor polypeptide in a trans-Golgi compartment. Proteolytic processing occurs C-terminal to the tetrabasic amino acid sequence RHRR, a consensus recognition site for precursor processing endoproteases or convertases. In this study we have identified furin, a subtilisin-type protease, to be necessary for efficient processing of LRP in cells. Furin-deficient RPE.40 cells exhibited an impaired processing of endogenous LRP and of a recombinant soluble form of the receptor containing the processing site. The processing defect in RPE.40 cells could be complemented by expression of furin from a transfected cDNA in cultured cells and by purified furin in vitro. The impaired maturation of LRP in RPE.40 cells did not affect its intracellular transport, and correlated with a slight but consistent reduction in the endocytosis of LRP-specific ligands. These data suggest that proteolytic processing of LRP by furin is not necessary for intracellular trafficking but might be required for normal receptor activity."xsd:string
http://purl.uniprot.org/citations/8546712http://purl.org/dc/terms/identifier"doi:10.1042/bj3130071"xsd:string
http://purl.uniprot.org/citations/8546712http://purl.uniprot.org/core/author"Herz J."xsd:string
http://purl.uniprot.org/citations/8546712http://purl.uniprot.org/core/author"Willnow T.E."xsd:string
http://purl.uniprot.org/citations/8546712http://purl.uniprot.org/core/author"Inocencio N.M."xsd:string
http://purl.uniprot.org/citations/8546712http://purl.uniprot.org/core/author"Moehring J.M."xsd:string
http://purl.uniprot.org/citations/8546712http://purl.uniprot.org/core/author"Moehring T.J."xsd:string
http://purl.uniprot.org/citations/8546712http://purl.uniprot.org/core/date"1996"xsd:gYear
http://purl.uniprot.org/citations/8546712http://purl.uniprot.org/core/name"Biochem J"xsd:string
http://purl.uniprot.org/citations/8546712http://purl.uniprot.org/core/pages"71-76"xsd:string
http://purl.uniprot.org/citations/8546712http://purl.uniprot.org/core/title"The low-density-lipoprotein receptor-related protein (LRP) is processed by furin in vivo and in vitro."xsd:string
http://purl.uniprot.org/citations/8546712http://purl.uniprot.org/core/volume"313"xsd:string
http://purl.uniprot.org/citations/8546712http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8546712
http://purl.uniprot.org/citations/8546712http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/8546712
http://purl.uniprot.org/uniprot/#_P09958-mappedCitation-8546712http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/8546712
http://purl.uniprot.org/uniprot/P09958http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/8546712