Topic:Angiotensin-converting enzyme (ACE)
Angiotensin-converting enzyme (ACE) is an important enzyme in horses that plays a role in the regulation of blood pressure and fluid balance. It is part of the renin-angiotensin-aldosterone system (RAAS), which is responsible for maintaining cardiovascular homeostasis. ACE facilitates the conversion of angiotensin I to angiotensin II, a potent vasoconstrictor that increases blood pressure and stimulates aldosterone secretion. In equine health, ACE activity can be indicative of cardiovascular function and is of interest in conditions such as exercise-induced pulmonary hemorrhage (EIPH) and other cardiovascular disorders. This page compiles peer-reviewed research studies and scholarly articles that examine the role, regulation, and clinical significance of angiotensin-converting enzyme in horses, providing insights into its potential as a biomarker for cardiovascular health and its implications in equine veterinary practice.
Morphological, Immunohistochemical, and Ultrastructural Studies of the Donkey’s Eye with Special Reference to the AFGF and ACE Expression. The donkey is mainly used as a working animal for riding and pack transport, as well as for dairy and meat production. Eye afflictions are common in donkeys, thus requiring a detailed study. A few studies had focused on the donkey's eye, and most of them had considered it, merely, a horse's eye. This study aimed to investigate the anatomy, histology, ultrastructure, and immunohistochemical features of the donkey's eye. The results were recorded and compared to those of horses in certain dimensions. Unlike horses, the donkey's eye is more circular in the contour of the cornea, has smaller lenti...
Computational insights into differential interaction of mammalian angiotensin-converting enzyme 2 with the SARS-CoV-2 spike receptor binding domain. The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is the causative agent of the COVID-19 pandemic. Angiotensin-converting enzyme 2 (ACE2) has been identified as the host cell receptor that binds to the receptor-binding domain (RBD) of the SARS-COV-2 spike protein and mediates cell entry. Because the ACE2 proteins are widely available in mammals, it is important to investigate the interactions between the RBD and the ACE2 of other mammals. Here we analyzed the sequences of ACE2 proteins from 16 mammals, predicted the structures of ACE2-RBD complexes by homology modeling, and refi...
Attenuation of the blood pressure response to exogenous angiotensin I after oral administration of benazepril to healthy adult horses. Benazepril has been shown to inhibit circulating angiotensin-converting enzyme (ACE) activity in horses but the optimal dosage is unknown. Objective: To determine the lowest tested dose of benazepril that results in ≥75% attenuation in the response of arterial blood pressure (BP) to exogenous angiotensin I (ANG-I) administration. Methods: Prospective experimental study. Methods: A total of 5 healthy horses were instrumented for the direct measurement of BP. Each horse received 4 intragastric doses of benazepril (0.5, 1, 2 and 4 mg/kg bwt) with a washout period of 7 days between doses. Prior ...
Pharmacokinetics and pharmacodynamics of ramipril and ramiprilat after intravenous and oral doses of ramipril in healthy horses. The pharmacokinetics and pharmacodynamics (PK/PD) of the angiotensin-converting enzyme inhibitor (ACEI) ramiprilat after intravenous (IV) and oral (PO) administration of ramipril have not been evaluated in horses. This study was designed to establish PK profiles for ramipril and ramiprilat as well as to determine the effects of ramiprilat on serum angiotensin converting enzyme (ACE) and to select the most appropriate ramipril dose that suppresses ACE activity. Six healthy horses in a cross-over design received IV ramipril 0.050 mg/kg, PO at a dose of 0 (placebo), and 0.050, 0.10, 0.20, 0.40 ...
Modulation of acute transient exercise-induced hypertension after oral administration of four angiotensin-converting enzyme inhibitors in normotensive horses. Changes in blood pressure (BP) during acute hypertension in response to angiotensin-converting enzyme inhibitors (ACEIs) have not been investigated in normotensive horses. In this study, six healthy horses were subjected to five trials, consisting in a treadmill exercise workload of 8 m/s for 1 min, 2 h after oral administration (PO) of placebo (0 mg/kg), enalapril (2.0 mg/kg), quinapril (1.0 mg/kg), ramipril (0.2 mg/kg) or benazepril (0.5 mg/kg). Serum angiotensin converting enzyme (ACE) activity was measured and systolic (SBP) and diastolic (DBP) blood pressures were recorded...
Pharmacokinetics and pharmacodynamics of enalapril and its active metabolite, enalaprilat, at four different doses in healthy horses. Pharmacokinetic and pharmacodynamic of IV enalapril at 0.50 mg/kg, PO placebo and PO enalapril at three different doses (0.50, 1.00 and 2.00 mg/kg) were analyzed in 7 healthy horses. Serum concentrations of enalapril and enalaprilat were determined for pharmacokinetic analysis. Angiotensin-converting enzyme (ACE) activity, serum ureic nitrogen (SUN), creatinine and electrolytes were measured, and blood pressure was monitored for pharmacodynamic analysis. The elimination half-lives of enalapril and enalaprilat were 0.67 and 2.76 h respectively after IV enalapril. Enalapril concentrations ...
Effects of quinapril on angiotensin converting enzyme and plasma renin activity as well as pharmacokinetic parameters of quinapril and its active metabolite, quinaprilat, after intravenous and oral administration to mature horses. Angiotensin converting enzyme (ACE) inhibitors improve survival and quality of life in human patients and small animals with cardiovascular and renal disease. There is limited information regarding their effects in horses. Objective: The purpose of this study was to determine the pharmacokinetics of quinapril and its effects on ACE and renin in horses. Methods: Experimental study using healthy mature horses. Methods: Six healthy horses were administered quinapril at 120 mg i.v., 120 mg per os and 240 mg per os in a 3-way crossover design. Blood was collected for measurement of quinapril ...
Effects of the ACE inhibitor quinapril on echocardiographic variables in horses with mitral valve insufficiency. Twenty horses with mitral valve insufficiency, but without signs of congestive heart failure, and five horses without signs of heart disease were examined before and after medication with an angiotensin-converting enzyme (ACE) inhibitor. The examination included echocardiography assessment as well as heart catheterization. The echocardiographic examination included B-mode, M-mode, conventional and colour Doppler techniques. For 8 weeks, all horses were treated with Accupro 20 (active substance: Quinapril) at an oral dose rate of 120 mg/horse/day. A follow-up of the horses with mitral valve ins...
Characterization of the pharmacokinetic and pharmacodynamic properties of the angiotensin-converting enzyme inhibitor, enalapril, in horses. The pharmacokinetics of enalapril (0.5 mg/kg i.v.) and the pharmacodynamics of enalapril (0.5 mg/kg PO) in 5 mares were investigated. After single i.v. dosing, concentrations of enalapril and enalaprilat, its active metabolite, were measured. Two weeks later, enalapril was administered by nasogastric tube. Potassium, creatinine, blood urea nitrogen (BUN), enalapril, and enalaprilat concentrations and angiotensin converting enzyme (ACE) activity were measured in serum. In addition, heart rate, blood pressure, digital venous blood gases, and lactate were measured. Two weeks later, enalapril was ...
A 105- to 94-kilodalton protein in the epididymal fluids of domestic mammals is angiotensin I-converting enzyme (ACE); evidence that sperm are the source of this ACE. SDS-PAGE analysis of luminal fluid from the ram testis and epididymis revealed a protein of about 105 kDa in the fluid in the caput epididymal region. The molecular mass of this fluid protein shifted from 105 kDa to 94 kDa in the distal caput epididymidis and remained at 94 kDa in the lower regions of the epididymis. The possible sperm origin of this protein was suggested by the decrease in intensity of a 105-kDa compound on the sperm plasma membrane extract and by its total disappearance from the fluid of animals with impaired sperm production caused by scrotal heating. The 94-kDa protein was...