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Vascular origin determines angiotensin I-converting enzyme expression in endothelial cells
B Baudin1, M Berard, J L Carrier
1INSERM U. 353, Hôpital Saint-Louis, Paris, France.
Endothelium : Journal of Endothelial Cell Research
|January 1, 1997
Summary
Endothelial cells (EC) from different blood vessels show varying levels of angiotensin I-converting enzyme (ACE). Pulmonary artery EC have the most ACE, while brain capillary EC secrete it faster, impacting hypertension treatments.
Area of Science:
- Cardiovascular Biology
- Enzymology
- Cell Biology
Background:
- Heterogeneous distribution of von Willebrand factor in vascular endothelium noted.
- Angiotensin I-converting enzyme (ACE) is crucial in the renin-angiotensin system.
Purpose of the Study:
- To investigate the expression of ACE in endothelial cells (EC) based on their vascular origin.
- To compare ACE levels and secretion in EC from different pig vascular beds.
Main Methods:
- Culturing EC from pig thoracic aorta, pulmonary artery, inferior vena cava, and brain capillaries.
- Assaying ACE activity using enzymatic radiochemical determination.
- Analyzing ACE protein expression via Western blot and immunofluorescence.
Main Results:
- EC secreted ACE into the culture medium, with cellular presence and plasma membrane localization confirmed.
- Pulmonary artery EC exhibited higher ACE content than other vascular sources, particularly brain capillaries.
- Brain capillary EC showed faster ACE secretion compared to arterial and vena cava EC.
Conclusions:
- Differential ACE expression exists along the vascular tree, with implications for ACE inhibitor pharmacology.
- Endothelial ACE distribution differs from von Willebrand factor.
- EC from von Willebrand disease models normally express ACE, decoupling it from von Willebrand factor expression.