Identificador persistente para citar o vincular este elemento: http://hdl.handle.net/10553/44412
Título: Ribonucleases 6 and 7 have antimicrobial function in The human and murine urinary tract
Autores/as: Becknell, Brian
Eichler, Tad E.
Beceiro Casas, Susana 
Li, Birong
Easterling, Robert S.
Carpenter, Ashley R.
James, Cindy L.
McHugh, Kirk M.
Hains, David S.
Partida-Sanchez, Santiago
Spencer, John D.
Clasificación UNESCO: 32 Ciencias médicas
Palabras clave: Antimicrobial peptide
Ribonuclease
Urinary tract infection
Pyelonephritis
Cystitis
Fecha de publicación: 2015
Editor/a: 0085-2538
Publicación seriada: Kidney International 
Resumen: 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.
URI: http://hdl.handle.net/10553/44412
ISSN: 0085-2538
DOI: 10.1038/ki.2014.268
Fuente: Kidney Internationa l[ISSN 0085-2538], v. 87, p. 151-161
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