Please use this identifier to cite or link to this item: http://ahro.austin.org.au/austinjspui/handle/1/9553
Title: Presence of angiotensin converting enzyme in the adventitia of large blood vessels.
Authors: Rogerson, F M;Chai, Syn Y;Schlawe, I;Murray, W K;Marley, P D;Mendelsohn, Frederick AO
Affiliation: University Department of Medicine, Austin Hospital, Heidelberg, Victoria, Australia.
Issue Date: 1-Jul-1992
Citation: Journal of Hypertension; 10(7): 615-20
Abstract: Angiotensin converting enzyme (ACE) is present in the endothelial cells of all vascular beds. There are, however, many reports of converting enzyme activity in blood vessels not associated with the endothelium.ACE was localized in large blood vessels of a number of mammals by in vitro autoradiography using the radioligand 125I-351A. To characterize this binding further, immunohistochemistry was performed on rabbit aorta using polyclonal antisera raised to two different preparations of rabbit lung ACE.In all of the blood vessels studied, which included the rabbit pulmonary artery, rabbit, dog and sheep aorta, human internal mammary artery and human saphenous vein, high levels of radioligand binding were found in endothelial cells, as expected. In addition, a very high density of punctate binding was observed interspersed between diffuse moderate labelling in the adventitia. Immunoreactivity was confined to the endothelium of both the intima and the vasa vasorum of the adventitia. The immunostaining correlated well with the autoradiography. The ACE inhibitors lisinopril and perindoprilat displayed similar high affinities in competing for the binding of 125I-351A to the endothelium and adventitia of the sheep aorta, suggesting that at these two sites the radioligand was binding to ACE.We find that ACE in the adventitia of large blood vessels is confined to the vaso vasorum. The results of this study help to explain the findings of many studies that ACE activity persists in endothelium-denuded blood vessels and also reveals a source of ACE distant from the luminal endothelial surface.
Internal ID Number: 1321187
URI: http://ahro.austin.org.au/austinjspui/handle/1/9553
URL: http://www.ncbi.nlm.nih.gov/pubmed/1321187
Type: Journal Article
Subjects: Angiotensin-Converting Enzyme Inhibitors
Animals
Autoradiography
Blood Vessels.enzymology
Dipeptides
Dogs
Endothelium, Vascular.enzymology
Guinea Pigs
Humans
Immunoenzyme Techniques
Peptidyl-Dipeptidase A.analysis
Rabbits
Radioligand Assay
Sheep
Vasa Vasorum.enzymology
Appears in Collections:Journal articles

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