Twists and turns in the search for the elusive renin processing enzyme: focus on “Cathepsin B is not the processing enzyme for mouse prorenin”
Author:
Affiliation:
1. Molecular and Cellular Biology, Roswell Park Cancer Institute, Buffalo, New York;
2. University of Virginia School of Medicine, Charlottesville, Virginia; and
3. University of Iowa, Iowa City, Iowa
Publisher
American Physiological Society
Subject
Physiology (medical),Physiology
Link
https://www.physiology.org/doi/pdf/10.1152/ajpregu.00188.2010
Reference26 articles.
1. Hydrolysis by Cathepsin B of Fluorescent Peptides Derived From Human Prorenin
2. Proprotein conversion is determined by a multiplicity of factors including convertase processing, substrate specificity, and intracellular environment. Cell type-specific processing of human prorenin by the convertase PC1.
3. Renin-1 Is Essential for Normal Renal Juxtaglomerular Cell Granulation and Macula Densa Morphology
4. Characterization of pure human renal renin. Evidence for a subunit structure.
5. Renin, a secretory glycoprotein, acquires phosphomannosyl residues.
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2. Behind every smile there's teeth: Cathepsin B's function in health and disease with a kidney view;Biochimica et Biophysica Acta (BBA) - Molecular Cell Research;2022-04
3. Transgenic Mice Overexpressing Human Alpha-1 Antitrypsin Exhibit Low Blood Pressure and Altered Epithelial Transport Mechanisms in the Inactive and Active Cycles;Frontiers in Physiology;2021-09-22
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5. Classical Renin‐Angiotensin System in Kidney Physiology;Comprehensive Physiology;2014-06-12
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