|
|
||||||||
1 From the Lilly Laboratory for Clinical Research, Indianapolis General Hospital, Indianapolis, Indiana
By means of a spirally cut strip of rabbit thoracic aorta, it has been shown that angiotonin exists in two forms. One form, angiotonin II, causes a contraction of the strip. The other, angiotonin I, is inactive. They are equally pressor when injected intravenously in animals. An enzyme in plasma converts the inactive form to the active form. The identical pressor activity can be explained by the excess of the converting enzyme in the plasma of the intact animal which rapidly converts angiotonin I to angiotonin II. Some patients with hypertension have a greater content of the converting enzyme in their plasma than is found in plasma of normotensive subjects. In addition to the converting enzyme, other factors in plasma enhance the ability of angiotonin and catechol amines to induce constriction of the strip of aorta. These factors may sensitize the mechanisms in the muscle which set up the process of contraction.
Note:
with the technical assistance of R. M. Sanders
This article has been cited by other articles:
![]() |
T. Stys, W. E. Lawson, G. C. Smaldone, and A. Stys Does Aspirin Attenuate the Beneficial Effects of Angiotensin-Converting Enzyme Inhibition in Heart Failure? Arch Intern Med, May 22, 2000; 160(10): 1409 - 1413. [Abstract] [Full Text] [PDF] |
||||
![]() |
P. Caldwell, B. Seegal, K. Hsu, M Das, and R. Soffer Angiotensin-converting enzyme: vascular endothelial localization Science, March 12, 1976; 191(4231): 1050 - 1051. [Abstract] [PDF] |
||||
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| Visit Other APS Journals Online |