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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...
Formato: | Texto |
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Lenguaje: | English |
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The Rockefeller University Press
1988
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2189047/ https://www.ncbi.nlm.nih.gov/pubmed/3049904 |
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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 |