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malfunction
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ACE induces angioedema, mainly mediated by bradykinin-induced activation of vascular bradykinin B2 receptors. Icatibant, a bradykinin B2 receptor antagonist, acts as therapeutic drug in treatment of ACE-induced angioedema
malfunction
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ACE inhibitors can induce angioedema, overview. Polymorphism of ACE insertion/deletion and the bradykinin B2 receptor polymorphisms are not involved in the development of ACEi-induced angioedema, overview
malfunction
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ACE is involved in risk of GFR decrease, doubling of serum creatinine or progression to ESRD in renal disease
malfunction
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atherosclerosis-enhancing effects of angiotensin II
malfunction
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both angiotensin-converting enzyme inhibitors and angiotensin receptor blockers can slow the progression of diabetic nephropathy, overview
malfunction
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clinical effects of calcium channel blocker and angiotensin converting enzyme inhibitor on endothelial function and arterial stiffness in patients with angina pectoris, overview
malfunction
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effect of chronic pre-treatment with angiotensin converting enzyme inhibition on skeletal muscle mitochondrial recovery after ischemia/reperfusion. Chronic ACE inhibition reduced blood pressure and might reduce ischemia-induced mitochondrial respiratory chain dysfunction in the frequent setting of hindlimb ischemia-reperfusion, overview
malfunction
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polymorphisms in the neurokinin-2 receptor gene are associated with angiotensin-converting enzyme inhibitor-induced cough, overview
malfunction
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some genetic alleles predispose human individuals to hypertension and cardiac diseases, overview
malfunction
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the enzyme is involved in hypertension, enzyme inhibition by flaxseed, Linum usitatissimum seeds, peptides reduces hypertension
malfunction
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use of ACE inhibitor is associated with a significant decrease in long-term mortality and cardiovascular events in the patients with diastolic heart failure
malfunction
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ACE2 gene transfer to the rostral ventrolateral medulla in spontaneously hypertensive rats attenuates the increased tonically active glutamatergic inputs to the rostral ventrolateral medulla in spontaneously hypertensive rats
malfunction
genetically modified mice carrying three copies of the ACE gene (three-copy mice) show increased angiotensin I-converting enzyme which alters peripheral and renal vascular reactivity to angiotensin II and bradykinin in mice. Mice with three copies of the ACE gene and a moderate genetic increase in ACE synthesis display abnormal systemic and renal hemodynamic responses to ANGII. No ACE genotype effect on the blood pressure response is observed for vasoconstrictor norepinephrine. The increase in endogenous ANG II formation due to increased ACE activity does not result in desensitization to the peptide's effect through downregulation of ANG II type 1 (AT1) receptor synthesis. Regulatory effects of the mutation, overview
malfunction
inhibition of ACE leads to amelioration of endothelial function, vascular remodeling, and reduction in atherosclerosis progression
malfunction
protective and the curative effects of Bacillus subtilis SPB1 crude lipopeptide biosurfactant in alleviating induced obesity complications in rats fed on high-fat-high-fructose diet (HFFD) via inhibition of ACE activity. Administration of SPB1 biosurfactant reduced significantly (34%) the peak of blood glucose concentration 60 min after glucose administration, as compared with untreated rats fed on HFFD. SPB1 lipopeptides treatments improves some of serum electrolytes such as Na+, K+, Ca2+, and Mg2+
malfunction
sAce knockdown through shRNAs impairs proliferation of mouse spermatogonial stem cells in vitro and leads to smaller colony size
malfunction
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genetically modified mice carrying three copies of the ACE gene (three-copy mice) show increased angiotensin I-converting enzyme which alters peripheral and renal vascular reactivity to angiotensin II and bradykinin in mice. Mice with three copies of the ACE gene and a moderate genetic increase in ACE synthesis display abnormal systemic and renal hemodynamic responses to ANGII. No ACE genotype effect on the blood pressure response is observed for vasoconstrictor norepinephrine. The increase in endogenous ANG II formation due to increased ACE activity does not result in desensitization to the peptide's effect through downregulation of ANG II type 1 (AT1) receptor synthesis. Regulatory effects of the mutation, overview
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malfunction
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protective and the curative effects of Bacillus subtilis SPB1 crude lipopeptide biosurfactant in alleviating induced obesity complications in rats fed on high-fat-high-fructose diet (HFFD) via inhibition of ACE activity. Administration of SPB1 biosurfactant reduced significantly (34%) the peak of blood glucose concentration 60 min after glucose administration, as compared with untreated rats fed on HFFD. SPB1 lipopeptides treatments improves some of serum electrolytes such as Na+, K+, Ca2+, and Mg2+
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malfunction
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inhibition of ACE leads to amelioration of endothelial function, vascular remodeling, and reduction in atherosclerosis progression
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metabolism
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ACE is involved in the renin-angiotensin-aldosterone system, overview
metabolism
angiotensin I-converting enzyme (ACE) plays a critical role in the regulation of the renin-angiotensin system
metabolism
the enzyme is involved in the renin-angiotensin system (RAS), which includes angiotensin I, angiotensin (Ang)II, and peptides angiotensin-(1-9) and angiotensin-(1-7) derived by C-terminal cleavage of their particular antecessors by angiotensin converting enzyme (ACE)1 or ACE2, overview
physiological function
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ACE catalyzes the extracellular formation of angiotensin II, and degradation of bradykinin, thus regulating blood pressure and renal handling of electrolytes. ACE added to smooth muscle cells resultes in transcriptional stimulation of the genes of bradykinin receptors B1 and B2. ACE enhances the activation of platelet-derived growth factor receptor beta signaling pathway
physiological function
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ACE is involved in corneal angiogenesis
physiological function
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ACE is part of the renin-angiotensin system, RAS, that regulates blood pressure and electrolyte homeostasis, and is involved in regulating regeneration, cell growth, apoptosis, inflammation and angiogenesis, expression and function of the key RAS component ACE during fracture healing, overview. ACE is important in bone remodelling
physiological function
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ACE is responsible for degradation of bradykinin which is the most potent stimulus for tissue plasminogen activator secretion. The reaction product from angiotensin I cleavage, angiotensin II, has an important role on fibrinolytic balance causing release of plasminogen activator inhibitor 1 and consequently inhibits fibrinolysis
physiological function
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ACE limits the stimulation of bradykinin receptors by degrading bradykinin, functions of the bradykinin B2 receptor, B2R, signaling, overview. Interaction of B2R and ACE or allosteric transmission occurs on the plasma membrane surface
physiological function
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ACE plays an important role in the renin-angiotensin system
physiological function
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angiotensin I-converting enzyme plays a pivotal role in blood pressure regulation
physiological function
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angiotensin I-converting enzyme, ACE, catalyzes the formation of vasoconstrictor, angiotensin II, and the inactivation of vasodilator, bradykinin
physiological function
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enzyme inhibitors are useful in treatment of hypertension and heart failure, as well as for peritoneal dialysis patients, because inhibit the local tissue renin-angiotensin system, which results in less development of peritoneal fibrosis and a longer life for the peritoneal membrane, overview
physiological function
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key enzyme of the renin-angiotensin system, a circulating endocrine system regulating blood pressure and electrolyte homeostasis. Inhibition of angiotensin-converting enzyme stimulates fracture healing and periosteal callus formation in a murine femur fracture model, overview
physiological function
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peptidases angiotensin-converting enzyme, together with neutral endopeptidase 24.11, mediates most of the kinin catabolism in normal cardiac tissue
physiological function
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ACE activity is higher in the patient group with alopecia areata compared to the control group
physiological function
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ACE identifies embryonic mesodermal precursors responsible for definitive hematopoiesis
physiological function
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ACE2 antagonizes angiotensin II-induced pressor response and NADPH oxidase activation in Wistar-Kyoto rats and spontaneously hypertensive rats
physiological function
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ACE2 regulates Ang II activity via attenuation of its effects on blood pressure control and oxidative stress
physiological function
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mouse ACE2 (1 mg/kg) obliterates hypertension induced by Ang II infusion by rapidly decreasing plasma Ang II
physiological function
ACE is a well-characterized zinc peptidase that removes C-terminal dipeptides from substrates such as angiotensin I and bradykinin leading to an increase in blood pressure. Angiotensin I-converting enzyme (ACE) plays a critical role in the regulation of the renin-angiotensin system. Somatic ACE, sACE, plays an important role in spermatogonial stem cell (SSC) self-renewal through the regulation of MAPK-dependent cell proliferation. sACE is required for the self-renewal of SSCs through the MAPK signaling pathway
physiological function
ACE is an endothelial ectopeptidase that is also secreted in plasma
physiological function
angiotensin-converting enzyme (ACE) metabolizes many peptides and plays a key role in blood pressure regulation and vascular remodeling, as well as in reproductive functions
physiological function
binding of captopril to angiotensin I-converting enzyme triggers activation of signaling pathways via JNK and ERK1/2 phosphorylation. Captopril leads to gene modulation trough binding to ACE causing a decrease of COX2 expression and an increase of AP2 expression. ACE interacts with beta-arrestin1, and this interaction seems to increase under captopril stimulation in CHO-ACE cells
physiological function
the enzyme is involved in the renin-angiotensin system (RAS), which includes angiotensin I, angiotensin (Ang)II, and peptides angiotensin-(1-9) and angiotensin-(1-7) derived by C-terminal cleavage of their particular antecessors by angiotensin converting enzyme (ACE)1 or ACE2, overview. Because of intensive local formation, the actions of nonclassical angiotensins could be especially important in the paracrine regulation of tissue physiology. RAAS may play a role in the regulation of blood pressure not only in a systemic endocrine manner, but also by local actions of various angiotensins (renin-angiotensin system, RAS) on vessel wall homeostasis
physiological function
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ACE is an endothelial ectopeptidase that is also secreted in plasma
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physiological function
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binding of captopril to angiotensin I-converting enzyme triggers activation of signaling pathways via JNK and ERK1/2 phosphorylation. Captopril leads to gene modulation trough binding to ACE causing a decrease of COX2 expression and an increase of AP2 expression. ACE interacts with beta-arrestin1, and this interaction seems to increase under captopril stimulation in CHO-ACE cells
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additional information
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ACE inhibition during pregnancy and lactation in adult offspring rats induces behavioural changes, e.g. in the open field test, overview
additional information
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angiotensin-converting enzyme inhibitors treatment of myocardial infarction patients bears is asscoiated with increased mortality, the risk is also existent for renal failure patients, overview
additional information
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metabolic effects of low dose angiotensin converting enzyme inhibitor in dietary obesity in the rat
additional information
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renal failure risks of angiotensin-converting-enzyme inhibitors, angiotensin II-receptor blockers, and aspirin for patients with diabetes, overview
additional information
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the enzyme inhibition by angiotensin-converting enzyme inhibitors is inhibited by aspirin, which can cause therapeutic problems during application of both in treatment of heart failure patients. Angiotensin receptor blockers do not interfere with the bradykinin pathway, detailed overview
additional information
ACE colocalizes with beta-arrestin1
additional information
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ACE colocalizes with beta-arrestin1
additional information
conformational fingerprinting of ACE from different tissues/subcellular compartments, i.e. lung and seminal fluid, using anti-catalytic anti-ACE monoclonal antibodies, overview
additional information
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conformational fingerprinting of ACE from different tissues/subcellular compartments, i.e. lung and seminal fluid, using anti-catalytic anti-ACE monoclonal antibodies, overview
additional information
secondary and tertiary structure and activity of ACE is investigated using circular dichroism, fluorescence quenching, and UV-visible spectroscopy, respectively
additional information
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ACE colocalizes with beta-arrestin1
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