RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/20304780http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20304780http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20304780http://www.w3.org/2000/01/rdf-schema#comment"Mutations in DJ-1 cause recessively transmitted early-onset Parkinson disease (PD), and oxidative damage to DJ-1 has been associated with the pathogenesis of late-onset sporadic PD. The precise biochemical function of DJ-1 remains elusive. Here, we report that DJ-1 is synthesized as a latent protease zymogen with low-intrinsic proteolytic activity. DJ-1 protease zymogen is activated by the removal of a 15-amino acid peptide at its C terminus. The activated DJ-1 functions as a cysteine protease with Cys-106 and His-126 as the catalytic diad. We show that endogenous DJ-1 in dopaminergic cells undergoes C-terminal cleavage in response to mild oxidative stress, suggesting that DJ-1 protease activation occurs in a redox-dependent manner. Moreover, we find that the C-terminally cleaved form of DJ-1 with activated protease function exhibits enhanced cytoprotective action against oxidative stress-induced apoptosis. The cytoprotective action of DJ-1 is abolished by the C106A and H126A mutations. Our findings support a role for DJ-1 protease in cellular defense against oxidative stress and have important implications for understanding and treating PD."xsd:string
http://purl.uniprot.org/citations/20304780http://purl.org/dc/terms/identifier"doi:10.1093/hmg/ddq113"xsd:string
http://purl.uniprot.org/citations/20304780http://purl.org/dc/terms/identifier"doi:10.1093/hmg/ddq113"xsd:string
http://purl.uniprot.org/citations/20304780http://purl.uniprot.org/core/author"Chen J."xsd:string
http://purl.uniprot.org/citations/20304780http://purl.uniprot.org/core/author"Chen J."xsd:string
http://purl.uniprot.org/citations/20304780http://purl.uniprot.org/core/author"Li L."xsd:string
http://purl.uniprot.org/citations/20304780http://purl.uniprot.org/core/author"Li L."xsd:string
http://purl.uniprot.org/citations/20304780http://purl.uniprot.org/core/author"Chin L.S."xsd:string
http://purl.uniprot.org/citations/20304780http://purl.uniprot.org/core/author"Chin L.S."xsd:string
http://purl.uniprot.org/citations/20304780http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20304780http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20304780http://purl.uniprot.org/core/name"Hum. Mol. Genet."xsd:string
http://purl.uniprot.org/citations/20304780http://purl.uniprot.org/core/name"Hum. Mol. Genet."xsd:string
http://purl.uniprot.org/citations/20304780http://purl.uniprot.org/core/pages"2395-2408"xsd:string
http://purl.uniprot.org/citations/20304780http://purl.uniprot.org/core/pages"2395-2408"xsd:string
http://purl.uniprot.org/citations/20304780http://purl.uniprot.org/core/title"Parkinson disease protein DJ-1 converts from a zymogen to a protease by carboxyl-terminal cleavage."xsd:string
http://purl.uniprot.org/citations/20304780http://purl.uniprot.org/core/title"Parkinson disease protein DJ-1 converts from a zymogen to a protease by carboxyl-terminal cleavage."xsd:string
http://purl.uniprot.org/citations/20304780http://purl.uniprot.org/core/volume"19"xsd:string
http://purl.uniprot.org/citations/20304780http://purl.uniprot.org/core/volume"19"xsd:string
http://purl.uniprot.org/citations/20304780http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/20304780
http://purl.uniprot.org/citations/20304780http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/20304780
http://purl.uniprot.org/citations/20304780http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/20304780
http://purl.uniprot.org/citations/20304780http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/20304780