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http://purl.uniprot.org/citations/25075772http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/25075772http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/25075772http://www.w3.org/2000/01/rdf-schema#comment"Recent evidence suggests antimicrobial peptides protect the urinary tract from infection. Ribonuclease 7 (RNase 7), a member of the RNase A superfamily, is a potent epithelial-derived protein that maintains human urinary tract sterility. RNase 7 expression is restricted to primates, limiting evaluation of its antimicrobial activity in vivo. Here we identified ribonuclease 6 (RNase 6) as the RNase A superfamily member present in humans and mice that is most conserved at the amino acid level relative to RNase 7. Like RNase 7, recombinant human and murine RNase 6 has potent antimicrobial activity against uropathogens. Quantitative real-time PCR and immunoblot analysis indicate that RNase 6 mRNA and protein are upregulated in the human and murine urinary tract during infection. Immunostaining located RNase 6 to resident and infiltrating monocytes, macrophages, and neutrophils. Uropathogenic E. coli induces RNase 6 peptide expression in human CD14(+) monocytes and murine bone marrow-derived macrophages. Thus, RNase 6 is an inducible, myeloid-derived protein with markedly different expression from the epithelial-derived RNase 7 but with equally potent antimicrobial activity. Our studies suggest RNase 6 serves as an evolutionarily conserved antimicrobial peptide that participates in the maintenance of urinary tract sterility."xsd:string
http://purl.uniprot.org/citations/25075772http://purl.org/dc/terms/identifier"doi:10.1038/ki.2014.268"xsd:string
http://purl.uniprot.org/citations/25075772http://purl.org/dc/terms/identifier"doi:10.1038/ki.2014.268"xsd:string
http://purl.uniprot.org/citations/25075772http://purl.uniprot.org/core/author"Li B."xsd:string
http://purl.uniprot.org/citations/25075772http://purl.uniprot.org/core/author"Li B."xsd:string
http://purl.uniprot.org/citations/25075772http://purl.uniprot.org/core/author"McHugh K.M."xsd:string
http://purl.uniprot.org/citations/25075772http://purl.uniprot.org/core/author"McHugh K.M."xsd:string
http://purl.uniprot.org/citations/25075772http://purl.uniprot.org/core/author"Becknell B."xsd:string
http://purl.uniprot.org/citations/25075772http://purl.uniprot.org/core/author"Becknell B."xsd:string
http://purl.uniprot.org/citations/25075772http://purl.uniprot.org/core/author"Hains D.S."xsd:string
http://purl.uniprot.org/citations/25075772http://purl.uniprot.org/core/author"Hains D.S."xsd:string
http://purl.uniprot.org/citations/25075772http://purl.uniprot.org/core/author"Spencer J.D."xsd:string
http://purl.uniprot.org/citations/25075772http://purl.uniprot.org/core/author"Spencer J.D."xsd:string
http://purl.uniprot.org/citations/25075772http://purl.uniprot.org/core/author"Partida-Sanchez S."xsd:string
http://purl.uniprot.org/citations/25075772http://purl.uniprot.org/core/author"Partida-Sanchez S."xsd:string
http://purl.uniprot.org/citations/25075772http://purl.uniprot.org/core/author"Beceiro S."xsd:string
http://purl.uniprot.org/citations/25075772http://purl.uniprot.org/core/author"Beceiro S."xsd:string
http://purl.uniprot.org/citations/25075772http://purl.uniprot.org/core/author"Carpenter A.R."xsd:string
http://purl.uniprot.org/citations/25075772http://purl.uniprot.org/core/author"Carpenter A.R."xsd:string
http://purl.uniprot.org/citations/25075772http://purl.uniprot.org/core/author"Easterling R.S."xsd:string
http://purl.uniprot.org/citations/25075772http://purl.uniprot.org/core/author"Easterling R.S."xsd:string
http://purl.uniprot.org/citations/25075772http://purl.uniprot.org/core/author"Eichler T.E."xsd:string
http://purl.uniprot.org/citations/25075772http://purl.uniprot.org/core/author"Eichler T.E."xsd:string