ArticleHypertension (Dallas, Tex. : 1979)2010
Role of prolylcarboxypeptidase in angiotensin II type 2 receptor-mediated bradykinin release in mouse coronary artery endothelial cells.
Article in Hypertension (Dallas, Tex. : 1979), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 44 citations in OpenAlex.
- Aprotinin (I): Understanding the Role of Host Proteases in COVID-19 and the Importance of Pharmacologically Regulating Their Function.International journal of molecular sciences · 2024Review
- Prolylcarboxypeptidase Alleviates Hypertensive Cardiac Remodeling by Regulating Myocardial Tissue Angiotensin II.Journal of the American Heart Association · 2023Article
- A comprehensive review on current understanding of bradykinin in COVID-19 and inflammatory diseases.Molecular biology reports · 2022Review
- COVID-19, vaccines and deficiency of ACEEuropean journal of internal medicine · 2022Review
- A modular map of Bradykinin-mediated inflammatory signaling network.Journal of cell communication and signaling · 2022Article
- Prolylcarboxypeptidase Mitigates Myocardial Ischemia/Reperfusion Injury by Stabilizing Mitophagy.Frontiers in cell and developmental biology · 2020Article
- Understanding the Pathophysiology of COVID-19: Could the Contact System Be the Key?Frontiers in immunology · 2020Article
- Cell-Specific Protective Signaling Induced by the Novel AT2R-Agonist NP-6A4 on Human Endothelial and Smooth Muscle Cells.Frontiers in pharmacology · 2018Article
- Prolyl carboxypeptidase activity in the circulation and its correlation with body weight and adipose tissue in lean and obese subjects.PloS one · 2018Article
- International Union of Basic and Clinical Pharmacology. XCIX. Angiotensin Receptors: Interpreters of Pathophysiological Angiotensinergic Stimuli [corrected].Pharmacological reviews · 2015Review
- Activation of angiotensin II type 2 receptor suppresses TNF-α-induced ICAM-1 via NF-кB: possible role of ACE2.American journal of physiology. Heart and circulatory physiology · 2015Article
- Article
- Prolyl carboxypeptidase activity decline correlates with severity and short-term outcome in acute ischemic stroke.Neurochemical research · 2015Article
- Effects of cardiac overexpression of the angiotensin II type 2 receptor on remodeling and dysfunction in mice post-myocardial infarction.Hypertension (Dallas, Tex. : 1979) · 2014Article
- New insights into insulin action and resistance in the vasculature.Annals of the New York Academy of Sciences · 2014Review
- Prolylcarboxypeptidase independently activates plasma prekallikrein (fletcher factor).Current molecular medicine · 2014Article
- Metabolic actions of angiotensin II and insulin: a microvascular endothelial balancing act.Molecular and cellular endocrinology · 2013Review
- Protective role of AT(2) and B(1) receptors in kinin B(2)-receptor-knockout mice with myocardial infarction.Clinical science (London, England : 1979) · 2013Article
- Angiotensin II type 2 receptor-stimulated activation of plasma prekallikrein and bradykinin release: role of SHP-1.American journal of physiology. Heart and circulatory physiology · 2012Article
- Enzymatic processing of angiotensin peptides by human glomerular endothelial cells.American journal of physiology. Renal physiology · 2012Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Activation of angiotensin II type 2 receptors (AT(2)R) causes the release of kinins, which have beneficial effects on the cardiovascular system. However, it is not clear how AT(2)R interact with the kallikrein-kinin system to generate kinins. Prolylcarboxypeptidase is an endothelial membrane-bound plasma prekallikrein activator that converts plasma prekallikrein to kallikrein, leading to generation of bradykinin from high-molecular-weight kininogen. We hypothesized that AT(2)R-induced bradykinin release is at least in part mediated by activation of prolylcarboxypeptidase. Cultures of mouse coronary artery endothelial cells were transfected with an adenoviral vector containing the AT(2)R gene (Ad-AT(2)R) or green fluorescent protein only (Ad-GFP) as control. We found that overexpression of AT(2)R increased prolylcarboxypeptidase mRNA by 1.7-fold and protein 2.5-fold compared with Ad-GFP controls. AT(2)R overexpression had no effect on angiotensin II type 1 receptor mRNA. Bradykinin release was increased 2.2-fold in AT(2)R-transfected cells. Activation of AT(2)R by CGP42112A, a specific AT(2)R agonist, increased bradykinin further in AT(2)R-transfected cells. These effects were diminished or abolished by AT(2)R blockade or a plasma kallikrein inhibitor. Furthermore, blocking prolylcarboxypeptidase with a small interfering RNA partially but significantly reduced bradykinin release by transfected AT(2)R cells either at the basal condition or when stimulated by the AT(2)R agonist CGP42112A. These findings suggest that overexpression of AT(2)R in mouse coronary artery endothelial cells increases expression of prolylcarboxypeptidase, which may contribute to kinin release.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.