Pharmacological and genetic evidence that cathepsin B is not the physiological activator of rodent prorenin
Identifieur interne : 001683 ( Main/Exploration ); précédent : 001682; suivant : 001684Pharmacological and genetic evidence that cathepsin B is not the physiological activator of rodent prorenin
Auteurs : M. David Percival [Canada] ; Sylvie Toulmond [Canada] ; Nathalie Coulombe [Canada] ; Wanda Cromlish [Canada] ; Sylvie Desmarais [Canada] ; Susana Liu [Canada] ; René St-Jacques [Canada] ; Jacques Yves Gauthier [Canada] ; Jean-Francois Fournier [Canada]Source :
- Biological Chemistry [ 1431-6730 ] ; 2010.
English descriptors
- Teeft :
- Active renin, Aminoacetonitrile class, Angiotensin, Arterial blood pressure, Blood pressure, Cathepsin, Chem, Cysteine, Cysteine cathepsin, Cysteine cathepsins, Desmarais, Gene compensation, Hypertension, Inhibitor, Juxtaglomerular cells, Knockout mice, Lambers heerspink, Lysosomal, Lysosomal proteases, Mature renin, Merck frosst centre, Mouse prorenin, Physiol, Physiological activator, Plasma renin activity, Previous studies, Processing enzyme, Proof cathepsin, Prorenin, Prorenin processing, Prorenin processing enzyme, Protease, Renin, Renin levels, Renin protein levels, Rodent prorenin, Secretory granules, Selective inhibitor, Significant role, Therapeutic research, Whole cells.
Abstract
Renin is the first enzyme in the renin-angiotensin-aldosterone system which is the principal regulator of blood pressure and hydroelectrolyte balance. Previous studies suggest that cathepsin B is the activator of the prorenin zymogen. Here, we show no difference in plasma renin activity, or mean arterial blood pressure between wild-type and cathepsin B knockout mice. To account for potential gene compensation, a potent, selective, reversible cathepsin B inhibitor was developed to determine the role of cathepsin B on prorenin processing in rats. Pharmacological inhibition of cathepsin B in spontaneously hypertensive and double transgenic rats did not result in a reduction in renal mature renin protein levels or plasma renin activity. We conclude that cathepsin B does not play a significant role in this process in rodents.
Url:
DOI: 10.1515/bc.2010.140
Affiliations:
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proteases</term><term>Mature renin</term><term>Merck frosst centre</term><term>Mouse prorenin</term><term>Physiol</term><term>Physiological activator</term><term>Plasma renin activity</term><term>Previous studies</term><term>Processing enzyme</term><term>Proof cathepsin</term><term>Prorenin</term><term>Prorenin processing</term><term>Prorenin processing enzyme</term><term>Protease</term><term>Renin</term><term>Renin levels</term><term>Renin protein levels</term><term>Rodent prorenin</term><term>Secretory granules</term><term>Selective inhibitor</term><term>Significant role</term><term>Therapeutic research</term><term>Whole cells</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Renin is the first enzyme in the renin-angiotensin-aldosterone system which is the principal regulator of blood pressure and hydroelectrolyte balance. Previous studies suggest that cathepsin B is the activator of the prorenin zymogen. Here, we show no difference in plasma renin activity, or mean arterial blood pressure between wild-type and cathepsin B knockout mice. To account for potential gene compensation, a potent, selective, reversible cathepsin B inhibitor was developed to determine the role of cathepsin B on prorenin processing in rats. Pharmacological inhibition of cathepsin B in spontaneously hypertensive and double transgenic rats did not result in a reduction in renal mature renin protein levels or plasma renin activity. We conclude that cathepsin B does not play a significant role in this process in rodents.</div></front></TEI><affiliations><list><country><li>Canada</li></country></list><tree><country name="Canada"><noRegion><name sortKey="Percival, M David" sort="Percival, M David" uniqKey="Percival M" first="M. David" last="Percival">M. David Percival</name></noRegion><name sortKey="Coulombe, Nathalie" sort="Coulombe, Nathalie" uniqKey="Coulombe N" first="Nathalie" last="Coulombe">Nathalie Coulombe</name><name sortKey="Cromlish, Wanda" sort="Cromlish, Wanda" uniqKey="Cromlish W" first="Wanda" last="Cromlish">Wanda Cromlish</name><name sortKey="Desmarais, Sylvie" sort="Desmarais, Sylvie" uniqKey="Desmarais S" first="Sylvie" last="Desmarais">Sylvie Desmarais</name><name sortKey="Fournier, Jean Francois" sort="Fournier, Jean Francois" uniqKey="Fournier J" first="Jean-Francois" last="Fournier">Jean-Francois Fournier</name><name sortKey="Gauthier, Jacques Yves" sort="Gauthier, Jacques Yves" uniqKey="Gauthier J" first="Jacques Yves" last="Gauthier">Jacques Yves Gauthier</name><name sortKey="Liu, Susana" sort="Liu, Susana" uniqKey="Liu S" first="Susana" last="Liu">Susana Liu</name><name sortKey="St Jacques, Rene" sort="St Jacques, Rene" uniqKey="St Jacques R" first="René" last="St-Jacques">René St-Jacques</name><name sortKey="Toulmond, Sylvie" sort="Toulmond, Sylvie" uniqKey="Toulmond S" first="Sylvie" last="Toulmond">Sylvie Toulmond</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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