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Cardiovascular Research 1998 40(1):206-210; doi:10.1016/S0008-6363(98)00103-5
© 1998 by European Society of Cardiology
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Copyright © 1998, European Society of Cardiology

Upregulation of angiotensin converting enzyme by atrial natriuretic peptide and cyclic GMP in human endothelial cells

Outi Saijonmaa* and Frej Fyhrquist

Minerva Institute for Medical Research and Department of Internal Medicine, Helsinki University Central Hospital, Helsinki, Finland

* Corresponding author. Address for correspondence: Minerva Institute for Medical Research, Tukholmankatu 2, SF-00250 Helsinki, Finland. Tel.: +358 (0) 477 1004; Fax: +358 (0) 477 1025; E-mail: outi.saijonmaa@kruuna.helsinki.fi

Objective: To examine the role of atrial natriuretic peptide (ANP) and cyclic GMP in the regulation of angiotensin converting enzyme (ACE) in cultured human endothelial cells. Methods: Cultured endothelial cells from human umbilical veins (HUVEC) were treated with ANP (0.3–30 nM), 8-Br-cGMP (1–100 µM), Rp-8-Br-PET-cGMPS (1 µM), or the phosphodiesterase inhibitors, zaprinast (10–100 µM), dipyridamole (1–10 µM), or isobutyl methyl xanthine (IBMX, 0.1–0.5 mM). ACE amounts were measured by inhibitor binding assay and cellular cGMP levels by radioimmunoassay. Results: ANP caused a dose dependent increase in ACE measured in intact endothelial cell culture. The stimulatory effect of ANP was blocked by Rp-8-Br-PET-cGMPS, a protein kinase G inhibitor. The cyclic GMP analog, 8-Br-cGMP and the cyclic GMP specific phosphodiesterase inhibitor, zaprinast, both increased ACE. Increase of ACE was also caused by nonspecific phosphodiesterase inhibitors, dipyridamole and IBMX. Intracellular cGMP levels were shown to increase by ANP, and phosphodiesterase inhibitors. Conclusions: These data suggest that cGMP is an intracellular mediator regulating ACE and that ANP induced increase of ACE is mediated via a cGMP dependent mechanism.

KEYWORDS Angiotensin converting enzyme; Atrial natriuretic peptide; Cyclic GMP; Phosphodiesterase inhibitors; HUVEC


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