Cargando…

The human neutrophil serine proteinases, elastase and cathepsin G, can mediate glomerular injury in vivo

We infused microgram quantities of active or inactive PMN elastase and cathepsin G into the renal arteries of rats. Both active and inactive elastase localized to the glomerular capillary wall equally, and in amounts that could be achieved physiologically in GN. However, elastase- perfused rats deve...

Descripción completa

Detalles Bibliográficos
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1988
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2189047/
https://www.ncbi.nlm.nih.gov/pubmed/3049904
_version_ 1782146550735044608
collection PubMed
description We infused microgram quantities of active or inactive PMN elastase and cathepsin G into the renal arteries of rats. Both active and inactive elastase localized to the glomerular capillary wall equally, and in amounts that could be achieved physiologically in GN. However, elastase- perfused rats developed marked proteinuria (196 +/- 32 mg/24 h) compared with control rats receiving inactive elastase (19 +/- 2 mg/24 h, p less than 0.005). Similar results were seen with active and inactive cathepsin G. Neither elastase nor cathepsin G infusion was associated with histologic evidence of glomerular injury. We conclude that the PMN neutral serine proteinases elastase and cathepsin G can mediate marked changes in glomerular permeability in vivo due to their proteolytic activity, and thus, may contribute to the proteinuria observed in PMN-dependent models of GN.
format Text
id pubmed-2189047
institution National Center for Biotechnology Information
language English
publishDate 1988
publisher The Rockefeller University Press
record_format MEDLINE/PubMed
spelling pubmed-21890472008-04-17 The human neutrophil serine proteinases, elastase and cathepsin G, can mediate glomerular injury in vivo J Exp Med Articles We infused microgram quantities of active or inactive PMN elastase and cathepsin G into the renal arteries of rats. Both active and inactive elastase localized to the glomerular capillary wall equally, and in amounts that could be achieved physiologically in GN. However, elastase- perfused rats developed marked proteinuria (196 +/- 32 mg/24 h) compared with control rats receiving inactive elastase (19 +/- 2 mg/24 h, p less than 0.005). Similar results were seen with active and inactive cathepsin G. Neither elastase nor cathepsin G infusion was associated with histologic evidence of glomerular injury. We conclude that the PMN neutral serine proteinases elastase and cathepsin G can mediate marked changes in glomerular permeability in vivo due to their proteolytic activity, and thus, may contribute to the proteinuria observed in PMN-dependent models of GN. The Rockefeller University Press 1988-09-01 /pmc/articles/PMC2189047/ /pubmed/3049904 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Articles
The human neutrophil serine proteinases, elastase and cathepsin G, can mediate glomerular injury in vivo
title The human neutrophil serine proteinases, elastase and cathepsin G, can mediate glomerular injury in vivo
title_full The human neutrophil serine proteinases, elastase and cathepsin G, can mediate glomerular injury in vivo
title_fullStr The human neutrophil serine proteinases, elastase and cathepsin G, can mediate glomerular injury in vivo
title_full_unstemmed The human neutrophil serine proteinases, elastase and cathepsin G, can mediate glomerular injury in vivo
title_short The human neutrophil serine proteinases, elastase and cathepsin G, can mediate glomerular injury in vivo
title_sort human neutrophil serine proteinases, elastase and cathepsin g, can mediate glomerular injury in vivo
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2189047/
https://www.ncbi.nlm.nih.gov/pubmed/3049904