scholarly journals 1049 ANGIOTENSIN-I-CONVERTING ENZYME (ACE) ACTIVITY IN TERM AND PRETERM INFANTS

1978 ◽  
Vol 12 ◽  
pp. 538-538
Author(s):  
John W Bender ◽  
Mary Kate Davitt ◽  
Pedro A Jose
Keyword(s):  
Preterm Infants ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Angiotensin I Converting Enzyme ◽  
Ace Activity

scholarly journals Nandrolone increases angiotensin-I converting enzyme activity in rats tendons

2015 ◽  
Vol 21 (3) ◽  
pp. 173-177 ◽  
Author(s):  
Rita de Cassia Marqueti ◽  
Nara Yumi Hashimoto ◽  
João Luiz Quaglioti Durigan ◽  
Lívia Larissa Batista e Silva ◽  
Jeeser Alves de Almeida ◽  
...  
Keyword(s):  
Training Session ◽  
Renin Angiotensin System ◽  
Tissue Growth ◽  
Control Group ◽  
Activity Levels ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Angiotensin I Converting Enzyme ◽  
Tendon Adaptation ◽  
Ace Activity

INTRODUCTION: The renin-angiotensin system (RAS) has been associated with several biological processes of the human body, regulating, among others blood pressure and water and electrolytes balance. Moreover, RAS also regulates connective tissue growth. Recently, studies have shown that the use of nandrolone modifies the angiotensin-I converting enzyme (ACE) activity and increases collagen deposition in the heart. OBJECTIVE: The aim of study was to evaluate the Angiotensin-I converting enzyme (ACE) activity in the superficial flexor tendon (SFT) and in serum after load exercise in combination with anabolic androgenic steroid (AAS) administration after training session and six weeks of detraining. METHODS: Forty-eight Wistar rats were used into two groups (G1 and G2) subdivided into four subgroups: Sedentary (S); trained (T); AAS-treated (Deca-Durabolin(r), 5mg/kg, twice a week) sedentary rats (AAS) and AAS-treated and trained animals (AAST). Trained groups performed jumps in water: four series of 10 jumps each, followed by a 30 sec interval between the series, for seven weeks. RESULTS: Training increased ACE activity in the SFT compared to the control group (p <0.05). Both AAS and AAST groups presented higher ACE activity levels (p < 0.05). The AAST increased the ACE activity only compared to the trained animals. Only the AAST group presented significant higher levels of ACE in the serum. In the G2 group, all experimental groups presented decreased ACE activity in the serum and in the tendon, as compared to the control group. CONCLUSION: This study indicates that AAS administration and its combination with exercise increased ACE activity of tendons. AAS abuse could compromise tendon adaptation causing maladaptive remodeling.

scholarly journals Aronia melanocarpa ElliotReduces the Activity of Angiotensin I-Converting Enzyme—In VitroandEx VivoStudies

2014 ◽  
Vol 2014 ◽  
pp. 1-7 ◽  
Author(s):  
Joanna Sikora ◽  
Marlena Broncel ◽  
Elżbieta Mikiciuk-Olasik
Keyword(s):  
Ace Inhibition ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Hypotensive Action ◽  
Aronia Melanocarpa ◽  
Clinical Observations ◽  
Angiotensin I Converting Enzyme ◽  
Ace Activity ◽  
Positive Correlations

Purpose. The aim of the study was to analyze the effects of two-month supplementation with chokeberry preparation on the activity of angiotensin I-converting enzyme (ACE) in patients with metabolic syndrome (MS). During thein vitrostage of the study, we determined the concentration of chokeberry extract, which inhibited the activity of ACE by 50% (IC50).Methods. The participants (n=70) were divided into three groups: I—patients with MS who received chokeberry extract supplements, II—healthy controls, and III—patients with MS treated with ACE inhibitors.Results. After one and two months of the experiment, a decrease in ACE activity corresponded to 25% and 30%, respectively. We documented significant positive correlations between the ACE activity and the systolic (r=0.459,P=0.048) and diastolic blood pressure, (r=0.603,P=0.005) and CRP. The IC50of chokeberry extract and captopril amounted to155.4±12.1 μg/mL and0.52±0.18 μg/mL, respectively.Conclusions. Ourin vitrostudy revealed that chokeberry extract is a relatively weak ACE inhibitor. However, the results of clinical observations suggest that the favorable hypotensive action of chokeberry polyphenols may be an outcome of both ACE inhibition and other pleotropic effects, for example, antioxidative effect.

scholarly journals A Study in First-Episode Psychosis Patients: Does Angiotensin I-Converting Enzyme Activity Associated With Genotype Predict Symptom Severity Reductions After Treatment With Atypical Antipsychotic Risperidone?

2020 ◽  
Vol 23 (11) ◽  
pp. 721-730
Author(s):  
João V Nani ◽  
Caroline Dal Mas ◽  
Camila M Yonamine ◽  
Vanessa K Ota ◽  
Cristiano Noto ◽  
...  
Keyword(s):  
Atypical Antipsychotic ◽  
Symptom Severity ◽  
First Episode Psychosis ◽  
Activity Level ◽  
First Episode ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Angiotensin I Converting Enzyme ◽  
Episode Psychosis ◽  
Ace Activity

Abstract Background Our previous studies showed increased angiotensin I-converting enzyme (ACE) activity in chronic schizophrenia patients compared with healthy control (HC) volunteers, and the relevance of combining ACE genotype and activity for predicting schizophrenia was suggested. Methods ACE activity was measured in plasma of ACE insertion/deletion (I/D) genotyped HC volunteers (n = 53) and antipsychotic-naïve first-episode psychosis (FEP) patients (n = 45) assessed at baseline (FEB-B) and also after 2 months (FEP-2M) of treatment with the atypical antipsychotic risperidone. Results ACE activity measurements showed significant differences among HC, FEP-B, and FEP-2M groups (F = 5.356, df = 2, P = .005) as well as between HC and FEP-2M (post-hoc Tukey’s multiple comparisons test, P = .004). No correlation was observed for ACE activity increases and symptom severity reductions in FEP as assessed by total Positive and Negative Syndrome Scale (r = −0.131, P = .434). FEP subgrouped by ACE I/D genotype showed significant ACE activity increases, mainly in the DD genotype subgroup. No correlation between ACE activity and age was observed in FEP or HC groups separately (r = 0.210, P = .392), but ACE activity level differences observed between these groups were influenced by age. Conclusions The importance of measuring the ACE activity in blood plasma, associated with ACE I/D genotyping to support the follow-up of FEP patients, did not show correlation with general symptom amelioration in the present study. However, new insights into the influence of age and I/D genotype for ACE activity changes in FEP individuals upon treatment was demonstrated.

scholarly journals Plasma concentration, kinetic constants, and gene polymorphism of angiotensin I-converting enzyme in centenarians

1998 ◽  
Vol 44 (10) ◽  
pp. 2083-2087 ◽  
Author(s):  
Laurence Faure-Delanef ◽  
Bruno Baudin ◽  
Bénédicte Bénéteau-Burnat ◽  
Jean-Christophe Beaudoin ◽  
Jacqueline Giboudeau ◽  
...  
Keyword(s):  
Kinetic Constants ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Cardiovascular Pathology ◽  
Angiotensin I Converting Enzyme ◽  
Its Gene ◽  
Causes Of Mortality ◽  
Michaelis Constants ◽  
Ace Activity ◽  
Optimal Ph

Abstract We have determined serum activity and kinetic constants of angiotensin I-converting enzyme (ACE), parallel to an insertion/deletion (I/D) polymorphism in its gene, in French centenarians and controls 20–70 years of age because this enzyme could have an impact on cardiovascular risk, and thus on longevity. Both the ACE D allele and ACE D/D genotype were more frequent in centenarians in comparison with controls, without sex-related differences nor significant correlation with a cardiovascular pathology. In centenarians, I/D polymorphism was correlated with circulating ACE activity (D/D genotype, 89.0 ± 36.8 U/L; I/D genotype, 63.5 ± 26.0 U/L; and I/I genotype, 55.1 ± 39.4 U/L). The Michaelis constants for two substrates were identical whatever the genotype and were not different between centenarians and controls, i.e., 0.30 ± 0.03 mmol/L for furylacryloyl-phenylalanyl-glycyl-glycine and 1.35 ± 0.05 mmol/L for hippuryl-histidyl-leucine; for the latter, the optimal pH and activating concentration of chloride did not depend on I/D polymorphism. The maximal velocities with both substrates reflected the distribution of serum ACE activity as a function of the genotypes, in centenarians and in controls. In conclusion, plasma ACE activity is subject to a similar genotypic influence in centenarians as in adults 20–70 years of age; however, ACE itself appears to be functionally similar for each genotype. Furthermore, the D allele as well as the higher serum ACE activities associated with the D/D genotype cannot discriminate individuals at high risk for cardiovascular diseases, major causes of mortality before the age of 100 years.

Angiotensin I-converting enzyme (ACE) activity and expression in rat central nervous system after sleep deprivation

2011 ◽  
Vol 392 (6) ◽  
Author(s):  
Bruna Visniauskas ◽  
Vitor Oliveira ◽  
Adriana K. Carmona ◽  
Vânia D’Almeida ◽  
Robson L. de Melo ◽  
...  
Keyword(s):  
Central Nervous System ◽  
Nervous System ◽  
Sleep Deprivation ◽  
Proteolytic Processing ◽  
Male Rats ◽  
Mrna Levels ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Angiotensin I Converting Enzyme ◽  
Ace Activity

Abstract Proteases are essential either for the release of neuropeptides from active or inactive proteins or for their inactivation. Neuropeptides have a fundamental role in sleep-wake cycle regulation and their actions are also likely to be regulated by proteolytic processing. Using fluorescence resonance energy transfer substrates, specific protease inhibitors and real-time PCR we demonstrate changes in angiotensin I-converting enzyme (ACE) expression and proteolytic activity in the central nervous system in an animal model of paradoxical sleep deprivation during 96 h (PSD). Male rats were distributed into five groups (PSD, 24 h, 48 h and 96 h of sleep recovery after PSD and control). ACE activity and mRNA levels were measured in hypothalamus, hippocampus, brainstem, cerebral cortex and striatum tissue extracts. In the hypothalamus, the significant decrease in activity and mRNA levels, after PSD, was only totally reversed after 96 h of sleep recovery. In the brainstem and hippocampus, although significant, changes in mRNA do not parallel changes in ACE specific activity. Changes in ACE activity could affect angiotensin II generation, angiotensin 1–7, bradykinin and opioid peptides metabolism. ACE expression and activity modifications are likely related to some of the physiological changes (cardiovascular, stress, cognition, metabolism function, water and energy balance) observed during and after sleep deprivation.

scholarly journals Functional analysis of the human somatic angiotensin I-converting enzyme gene promoter

1993 ◽  
Vol 293 (3) ◽  
pp. 843-848 ◽  
Author(s):  
P Testut ◽  
F Soubrier ◽  
P Corvol ◽  
C Hubert
Keyword(s):  
Promoter Region ◽  
Promoter Activity ◽  
Regulatory Elements ◽  
Upstream Region ◽  
Start Site ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Angiotensin I Converting Enzyme ◽  
Hepatocarcinoma Cells ◽  
Ace Activity

Angiotensin I-converting enzyme (ACE) is a key enzyme in the regulation of systemic blood pressure and plays a major role in the renin-angiotensin and bradykinin-kinin systems, at the luminal surface of the vascular endothelia. To identify the promoter region, the transcription regulatory elements and the cell specificity of the ACE gene, five successive DNA deletions of the 5′ upstream region (-1214, -754, -472, -343, -132 bp relative to the start site of transcription) were isolated and fused in sense and antisense orientations to the bacterial chloramphenicol acetyltransferase (CAT) reporter gene in the promoterless plasmid pBLCAT3. Promoter activities were measured in transient transfection assays using three different cell lines from rabbit endothelium (RE), human embryocarcinoma (Tera-1) and hepatocarcinoma cells (HepG2). All five fragments of the ACE promoter region directed expression of the CAT gene when transfected into the endothelial and the embryocarcinoma cells, which contain endogenous ACE mRNA and express ACE activity. In contrast only minimal levels of promoter activity were obtained on transfection into hepatocarcinoma cells in which endogenous ACE mRNA and ACE activity were not detected. Transfection of RE and Tera-1 cells demonstrated that promoter activity was defined by the length of the ACE promoter sequence inserted into the construct. The 132 bases located upstream from the transcription start site were sufficient to confer ACE promoter activity, whereas the sequences upstream from -472 bp and between -343 bp and -132 bp were responsible for a decrease of promoter activity. Furthermore, the minimal 132 bp of the ACE promoter contains elements which direct cell-specific CAT expression. In addition, the DNA transfection study in the presence of dexamethasone suggested that the potential glucocorticoid regulatory elements, located in the sequence of the ACE promoter, are not functional.

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