Renin is an aspartyl protease that plays a critical role in the production of angiotensin peptides and therefore in the modulation of blood pressure. Renin participates not only in the circulating renin-angiotensin system (RAS) but may also be taken up by tissues to control the activity of the local RAS. In this study, we provide evidence for the existence of a high affinity, saturable binding site for human renin (estimated k$ sb{ rm d}$ of 125 pM) and prorenin, the inactive precursor of renin, in the human placenta. The interesting finding that prorenin could bind to the same site as renin suggests that its role in vivo may be to act as a natural antagonist that would limit the local levels of angiotensin II production. It is of further interest to identify the protein regions important in this uptake; here we show that the degree of glycosylation in prorenin and the active site of renin are not essential in this process. In the near future, experiments will involve in-depth studies of the regions implicated in the binding process and long term goals will be to identify and characterize this novel renin and prorenin binding site.
| Identifer | oai:union.ndltd.org:LACETR/oai:collectionscanada.gc.ca:QMM.27301 |
| Date | January 1997 |
| Creators | Chiu, Sui Mei Linda. |
| Contributors | Reudelhuber, Timothy L. (advisor) |
| Publisher | McGill University |
| Source Sets | Library and Archives Canada ETDs Repository / Centre d'archives des thèses électroniques de Bibliothèque et Archives Canada |
| Language | English |
| Detected Language | English |
| Type | Electronic Thesis or Dissertation |
| Format | application/pdf |
| Coverage | Master of Science (Division of Experimental Medicine.) |
| Rights | All items in eScholarship@McGill are protected by copyright with all rights reserved unless otherwise indicated. |
| Relation | alephsysno: 001548744, proquestno: MQ29676, Theses scanned by UMI/ProQuest. |
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