Hypertension, Vol 3, 198-204, Copyright © 1981 by American Heart Association
P Brecher, A Tercyak and AV Chobanian
Angiotensin-converting enzyme (ACE) was studied in preparations of
microvessels isolated from rabbit cerebral cortex. Activity was determined
by measuring the degradation of hippuryl-histidyl-leucine (Hip-His-Leu) by
the intact microvessels in a physiological salt solution at pH 7.4. ACE
activity was dependent on both substrate and chloride ion concentration and
was inhibited by captopril in a manner similar to that observed previously
with tissue homogenates. Angiotensin I was rapidly degraded by the intact
microvessels, even in the presence of 10(-6)M captopril. An advantage of
the methodology employed was the ability to pretreat the microvessels and
then assess the effect of pretreatment by transfer to a postincubation
assay system. Pretreatment with a hyperosmolar urea solution did not change
ACE activity or cause release of ACE from the microvessels, although lactic
dehydrogenase and lysosomal enzymes were released. Pretreatment with
captopril caused a lag in the subsequent degradation of Hip-His- Leu,
presumably reflecting dissociation of inhibitor from the cell- associated
enzyme. ACE activity was unaffected by hypoxic or anoxic incubation
conditions. The ability to measure ACE activity of the microvessels in
vitro provides a unique opportunity to study the properties of the enzyme
in intact cerebrovascular endothelial cells.
ARTICLES
Properties of angiotensin-converting enzyme in intact cerebral microvessels
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