Studies into the calmodulin content and activity of tissues from hypertensive and normotensive rats and mice have shown the existence of a factor which potentiates calmodulin's capability to stimulate Ca$ sp{2+}/$CaM-dependent phosphodiesterase (CaM-PDE) and which is detected more in hypertensive animals. This CaM-PDE activator is present in the heart, kidney, erythrocytes, and aortic smooth muscle cells. The augmentation of the CaM-PDE activator is found, as well, in human hypertensives. CaM-PDE activator content is modulated by dietary calcium and sodium. Physicochemical and biochemical characterization of the activator reveal it to be a heat-stable, hydrophobic, protease-sensitive factor with a molecular mass of 4 kDa. Subcellular fractionation studies have revealed that the CaM-PDE activator resides principally in the cytosol although there is a small difference in its subcellular distribution between normotensives and hypertensives. Partial purification of the activator to the step of isocratic, reversed-phase HPLC shows the samples from hypertensive mice to partition into three activity peaks while the normotensives partition into two.
| Identifer | oai:union.ndltd.org:LACETR/oai:collectionscanada.gc.ca:QMM.70248 |
| Date | January 1992 |
| Creators | Chang, Edwin |
| 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 | Doctor of Philosophy (Division of Experimental Medicine.) |
| Rights | All items in eScholarship@McGill are protected by copyright with all rights reserved unless otherwise indicated. |
| Relation | alephsysno: 001265684, proquestno: AAINN74458, Theses scanned by UMI/ProQuest. |
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