Glomerular angiotensinase A in the rat: Increase of enzyme activity following renal ablation View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

1990-11

AUTHORS

G Wolf, F Thaiss, J E Scherberich, W Schoeppe, R A Stahl

ABSTRACT

Angiotensinase A (aminopeptidase A; ATA) is an angiotensin II splitting exopeptidase, which is localized in endothelial and epithelial cells of the glomerular tuft. In order to investigate the influence of a reduction in renal mass on enzyme activity, ATA activity was measured in isolated rat glomeruli five and 14 weeks after 1-1/3 nephrectomy. Glomerular ATA activity in remnant kidneys increased significantly after five weeks following ablation compared with glomeruli of two kidney control rats (5.34 +/- 4.02 vs. 1.71 +/- 1.96 mU/mg protein, P less than 0.05). After 14 weeks, however, this difference was no longer present. Treatment of rats with enalapril or saralasin inhibited the increase of ATA seen five weeks after renal ablation, whereas indomethacin had no effect on enzyme activity. Furthermore, normal two kidney rats, treated with furosemide, revealed a higher glomerular ATA than two kidney controls (5.5 +/- 2.64 vs. 2.1 +/- 1.7 mU/mg protein, P less than 0.05). In vitro superfusion of isolated glomeruli with enalaprilate or furosemide from rats after renal ablation did not influence enzyme activity, however, superfusion with 0.05 mM angiotensin II or 0.05 mM saralasin significantly reduced ATA. Our results suggest that glomerular ATA might be involved in the early regulation of the intrarenal renin-angiotensin system and could modify glomerular adaptation to reduce renal mass by affecting angiotensin II degradation. More... »

PAGES

862-868

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/ki.1990.283

DOI

http://dx.doi.org/10.1038/ki.1990.283

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1019086706

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/2266670


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56 schema:description Angiotensinase A (aminopeptidase A; ATA) is an angiotensin II splitting exopeptidase, which is localized in endothelial and epithelial cells of the glomerular tuft. In order to investigate the influence of a reduction in renal mass on enzyme activity, ATA activity was measured in isolated rat glomeruli five and 14 weeks after 1-1/3 nephrectomy. Glomerular ATA activity in remnant kidneys increased significantly after five weeks following ablation compared with glomeruli of two kidney control rats (5.34 +/- 4.02 vs. 1.71 +/- 1.96 mU/mg protein, P less than 0.05). After 14 weeks, however, this difference was no longer present. Treatment of rats with enalapril or saralasin inhibited the increase of ATA seen five weeks after renal ablation, whereas indomethacin had no effect on enzyme activity. Furthermore, normal two kidney rats, treated with furosemide, revealed a higher glomerular ATA than two kidney controls (5.5 +/- 2.64 vs. 2.1 +/- 1.7 mU/mg protein, P less than 0.05). In vitro superfusion of isolated glomeruli with enalaprilate or furosemide from rats after renal ablation did not influence enzyme activity, however, superfusion with 0.05 mM angiotensin II or 0.05 mM saralasin significantly reduced ATA. Our results suggest that glomerular ATA might be involved in the early regulation of the intrarenal renin-angiotensin system and could modify glomerular adaptation to reduce renal mass by affecting angiotensin II degradation.
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