scholarly journals Ance, a Drosophila angiotensin-converting enzyme homologue, is expressed in imaginal cells during metamorphosis and is regulated by the steroid, 20-hydroxyecdysone

2002 ◽  
Vol 367 (1) ◽  
pp. 187-193 ◽  
Author(s):  
Richard J. SIVITER ◽  
Christine A.M. TAYLOR ◽  
Deborah M. COTTAM ◽  
Adrian DENTON ◽  
M. Paulina DANI ◽  
...  
Keyword(s):  
Angiotensin Converting Enzyme ◽  
Larval Instar ◽  
Fold Increase ◽  
Peptide Hormone ◽  
Imaginal Discs ◽  
Wing Disc ◽  
Temperature Sensitive ◽  
Converting Enzyme ◽  
Moulting Hormone ◽  
Similar Peptide

Ance is a single domain homologue of mammalian angiotensin-converting enzyme (ACE) and is important for normal development and reproduction in Drosophila melanogaster. Mammalian ACE is responsible for the synthesis of angiotensin II and the inactivation of bradykinin and N-acetyl-Ser-Asp-Lys-Pro, but the absence of similar peptide hormones in insects suggests novel functions for Ance. We now provide evidence in support of a role for Ance during Drosophila metamorphosis. The transition of larva to pupa was accompanied by a 3-fold increase in ACE-like activity, which subsequently dropped to larval levels on adult eclosion. This increase was attributed to the induction of Ance expression during the wandering phase of the last larval instar in the imaginal cells (imaginal discs, abdominal histoblasts, gut imaginal cells and imaginal salivary gland). Ance expression was particularly strong in the presumptive adult midgut formed as a result of massive proliferation of the imaginal midgut cells soon after pupariation. No Ance transcripts were detected in the midgut of the fully differentiated adult intestine. Ance protein and mRNA were not detected in imaginal discs from wandering larvae of flies homozygous for the ecd1 allele, a temperature-sensitive ecdysone-less mutant, suggesting that Ance expression is ecdysteroid-dependent. Physiological levels of 20-hydroxyecdysone induced the synthesis of ACE-like activity and Ance protein by a wing disc cell line (Cl.8+), confirming that Ance is an ecdysteroid-responsive gene. We propose that the expression of Ance in imaginal cells is co-ordinated by exposure to ecdysteroid (moulting hormone) during the last larval instar moult to increase levels of ACE-like activity during metamorphosis. The enzyme activity may be required for the processing of a developmental peptide hormone or may function in concert with other peptidases to provide amino acids for the synthesis of adult proteins.

scholarly journals Lemon Extract Reduces Angiotensin Converting Enzyme (ACE) Expression and Activity and Increases Insulin Sensitivity and Lipolysis in Mouse Adipocytes

Nutrients ◽  
2020 ◽  
Vol 12 (8) ◽  
pp. 2348
Author(s):  
Shilpa Tejpal ◽  
Alan M. Wemyss ◽  
Claire C. Bastie ◽  
Judith Klein-Seetharaman
Keyword(s):  
Gene Expression ◽  
Insulin Sensitivity ◽  
Angiotensin Converting Enzyme ◽  
Protein Expression ◽  
Serum Insulin ◽  
Fold Increase ◽  
Cardiovascular Complications ◽  
Lemon Juice ◽  
Converting Enzyme ◽  
Ace Gene

Obesity is associated with insulin resistance and cardiovascular complications. In this paper, we examine the possible beneficial role of lemon juice in dieting. Lemon extract (LE) has been proposed to improve serum insulin levels and decrease angiotensin converting enzyme (ACE) activity in mouse models. ACE is also a biomarker for sustained weight loss and ACE inhibitors improve insulin sensitivity in humans. Here, we show that LE impacts adipose tissue metabolism directly. In 3T3-L1 differentiated adipocyte cells, LE improved insulin sensitivity as evidenced by a 3.74 ± 0.54-fold increase in both pAKT and GLUT4 levels. LE also induced lipolysis as demonstrated by a 16.6 ± 1.2 fold-change in pHSL protein expression levels. ACE gene expression increased 12.0 ± 0.1 fold during differentiation of 3T3-L1 cells in the absence of LE, and treatment with LE decreased ACE gene expression by 80.1 ± 0.5% and protein expression by 55 ± 0.37%. We conclude that LE’s reduction of ACE expression causes increased insulin sensitivity and breakdown of lipids in adipocytes.

Biochemical and Histological Alterations in Rats after Acute Nitrogen Dioxide Intoxication

1992 ◽  
Vol 11 (3) ◽  
pp. 189-200 ◽  
Author(s):  
J. Meulenbelt ◽  
L. van Bree ◽  
J.A.M.A. Dormans ◽  
A.B.T.J. Boink ◽  
B. Sangster
Keyword(s):  
Enzyme Activity ◽  
Lung Injury ◽  
Angiotensin Converting Enzyme ◽  
Nitrogen Dioxide ◽  
Fold Increase ◽  
Transferase Activity ◽  
Converting Enzyme ◽  
Angiotensin Converting Enzyme Activity ◽  
Glucuronidase Activity ◽  
Glutamyl Transferase

1 In previous studies a rat inhalation model was developed to investigate the treatment of acute nitrogen dioxide (NO2) intoxication. 2 Biochemical parameters, which may be important for the evaluation of lung injury and repair, were reviewed and compared with the histology. 3 After exposure to high NO2 concentrations (75 ppm, 125 ppm or 175 for 10 min) 1 the lung injury observed by light microscope was most pronounced after 24 h and became worse with increasing concentration. 4 The most sensitive indicators for lung injury in the broncho-alveolar lavage fluid (BAL) were protein and albumin concentrations, angiotensin converting enzyme activity, β-glucuronidase activity and the presence of neutrophil leucocytes. The changes observed in these variables were dose-dependent. Following exposure to 175 ppm the protein and albumin concentrations and the angiotensin converting enzyme activity showed a 100-fold increase, while the β-glucuronidase activity showed a 10-fold increase. 5 Glucose-6-phosphate dehydrogenase and glutathione peroxidase in the supernatant of lung homogenate and gamma-glutamyl transferase activity in BAL are likely to be the most practical parameters for monitoring the phase of repair because their activities were maximal at the moment histological changes were reduced in intensity. 6 Repair was almost complete 7 d following exposure.

scholarly journals Angiotensin-Converting Enzyme Gene Insertion/Deletion Polymorphism and Small Vessel Cerebral Stroke in Indian Population

2014 ◽  
Vol 2014 ◽  
pp. 1-4 ◽  
Author(s):  
Puttachandra Prabhakar ◽  
Tanima De ◽  
Dindagur Nagaraja ◽  
Rita Christopher
Keyword(s):  
Blood Pressure ◽  
Angiotensin Converting Enzyme ◽  
Indian Population ◽  
Fold Increase ◽  
Small Vessel ◽  
Cerebral Stroke ◽  
South Indian Population ◽  
Converting Enzyme ◽  
Gene Insertion ◽  
South Indian

Background. Hypertension is an established risk factor for small-vessel cerebral stroke and the renin-angiotensin system plays an important role in the maintenance of blood pressure. We aimed at evaluating the contribution of the angiotensin-converting enzyme (ACE) gene insertion/deletion (I/D) polymorphism to the risk of small-vessel stroke in south Indian population.Materials and Methods. We investigated 128 patients diagnosed with small-vessel stroke and 236 age, and gender-matched healthy controls.ACEI/D polymorphism was detected by polymerase chain reaction.Results. Hypertension was significantly more prevalent in the patient group and was associated with 6-fold increase in risk for stroke.ACEgenotypes were in Hardy-Weinberg equilibrium in both patients and controls. Prevalence of DD, ID, and II genotypes in cases (34.4%, 43.7%, and 28%) did not differ significantly from controls (31.8%, 43.2%, and 25%). The polymorphism was not associated with small-vessel stroke (OR: 1.34; 95% CI: 0.52–1.55). However, diastolic blood pressure was associated with theACEI/D genotypes in the patients. (DD;90.2±14.2>ID;86.2±11.9>II;82.3±7.8 mm Hg,  P=0.047).Conclusion. Our study showed that hypertension, but notACEI/D polymorphism, increased the risk of small-vessel stroke.

Dietary regulation of rat intestinal angiotensin-converting enzyme and dipeptidyl peptidase IV

1993 ◽  
Vol 264 (6) ◽  
pp. G1153-G1159 ◽  
Author(s):  
Y. Suzuki ◽  
R. H. Erickson ◽  
A. Sedlmayer ◽  
S. K. Chang ◽  
Y. Ikehara ◽  
...  
Keyword(s):  
Angiotensin Converting Enzyme ◽  
Brush Border ◽  
Brush Border Membrane ◽  
Fold Increase ◽  
Immunoblot Analysis ◽  
Dipeptidyl Peptidase ◽  
Dipeptidyl Peptidase Iv ◽  
Converting Enzyme ◽  
Brush Border Membranes ◽  
Dpp Iv

The small intestinal brush-border membrane contains several peptidases that are involved in the hydrolysis of dietary peptides containing proline. A high-proline (gelatin) diet was administered to one of several groups of rats to study its possible regulatory effect on levels of two prolyl peptidases, namely angiotensin-converting enzyme (ACE) and dipeptidyl peptidase IV (DPP IV). Groups of rats were maintained on isocaloric diets containing either low (4%), normal (17%), or high (50%) protein (casein) or high (50%) gelatin. After 7 days, brush-border membranes and total RNA were prepared from the small intestine. ACE activity was 3- to 10-fold higher in brush-border membranes from the gelatin group compared with the low-protein group. DPP IV exhibited a three- to sixfold increase. Immunoblot analysis of brush-border membrane-associated ACE protein indicated a six- to eightfold increase in the high-gelatin group. There was also a 1.5- to 3-fold increase in steady-state levels of ACE and DPP IV mRNA. These results suggest that a diet high in proline (gelatin) is particularly effective in increasing intestinal levels of these two enzymes.

Activation of angiotensin-converting enzyme expression in infarct zone following myocardial infarction

1995 ◽  
Vol 269 (4) ◽  
pp. H1268-H1276 ◽  
Author(s):  
R. C. Passier ◽  
J. F. Smits ◽  
M. J. Verluyten ◽  
R. Studer ◽  
H. Drexler ◽  
...  
Keyword(s):  
Myocardial Infarction ◽  
Endothelial Cells ◽  
Angiotensin Converting Enzyme ◽  
Rat Heart ◽  
Fold Increase ◽  
Border Zone ◽  
Sham Operation ◽  
Converting Enzyme ◽  
Infarct Zone ◽  
Protein Density

In the present study we quantified angiotensin-converting enzyme (ACE) mRNA and localized ACE mRNA and protein in the infarcted rat heart. Wistar rats underwent ligation of the left descending coronary artery, resulting in myocardial infarction (MI) or a sham operation. At different times (1-90 days) after surgery (n = 3 each), the heart was removed and divided into the right ventricle (RV), septum (Se) and left ventricle (LV). ACE mRNA was quantified by competitive reverse transcriptase-polymerase chain reaction (RT-PCR). At 4 and 7 days after MI, we found a 2.8-fold increase of ACE mRNA (n = 3; P < or = 0.05) in the infarcted LV compared with the LV of the sham group. No increases of ACE mRNA were found in the noninfarcted hypertrophied compartments. ACE activity increased 2.6- and 3.6-fold in the infarcted LV at 7 and 90 days after MI, respectively. In situ hybridization and immunohistochemistry showed increased ACE mRNA and protein density in the border zone of the infarcted area, predominantly in the endothelial cells lining capillaries. In the noninfarcted myocardium ACE mRNA and protein were confined to endothelial cells of the larger vessels. From these data we conclude that the intracardiac RAS is involved in the healing of the scar after MI in the rat, possibly giving rise to neovascularization. Furthermore, the data suggest that the intracardiac ACE is not necessarily associated with hypertrophy in the rat heart after MI.

Abstract 381: Upregulation of Tumor Necrosis Factor α-converting Enzyme (TACE) Protein Expression in db/db Mice is Reversed by Rosiglitazone

Hypertension ◽  
2012 ◽  
Vol 60 (suppl_1) ◽  
Author(s):  
Harshita Chodavarapu ◽  
Hari K Somineni ◽  
Esam Salem ◽  
Mariana Morris ◽  
Khalid M Elased
Keyword(s):  
Angiotensin Converting Enzyme ◽  
Protein Expression ◽  
Western Blot ◽  
Fold Increase ◽  
Ectodomain Shedding ◽  
Converting Enzyme ◽  
Glucose Levels ◽  
Pparγ Agonist ◽  
Urinary Parameters ◽  
Factor Α

TACE, also known as ADAM17, is involved in the ectodomain shedding of several membrane bound proteins. Angiotensin converting enzyme 2 (ACE2), homologue of angiotensin converting enzyme (ACE), is known to be renoprotective by increasing the degradation of vasoactive peptide Angiotensin II (Ang II) to vasodilator peptide Ang - (1-7). It has been shown before that TACE mediates regulated ectodomain shedding of ACE2. PPARγ agonist, rosiglitazone, is known to impart renoprotection by attenuating albuminuria. However, the exact mechanism of renoprotection is not clear. Our previous results and others showed that renal ACE2 protein expression is increased during early stages of diabetes in db/db mice. We also demonstrated increased urinary ACE2 excretion in db/db mice. The goal of this study is to test the hypothesis that TACE is upregulated in db/db diabetic mice and treatment with rosiglitazone imparts renoprotection by attenuating the shedding of renal ACE2 via downregulating TACE protein expression. Male 6 week db/db mice were fed rosiglitazone (20mg/kg/day) for 10 weeks. Metabolic and urinary parameters were monitored weekly. Kidney lysate and urine was used to perform western blot and ACE2 activity (pmols/h/μg protein) respectively. db/db mice demonstrated glucose intolerance, hyperglycemia (348.2±29.9 mg/dL), and albuminuria (0.3±0.05 mg/day) at a very early age. Chronic rosiglitazone treatment normalized blood glucose levels (142.0±12.2 mg/dL), improved glucose tolerance and decreased albuminuria (0.17±0.03 mg/day) in treated db/db mice. Western blot showed increased renal TACE protein expression of db/db mice compared to controls (p<0.05). Treatment with rosiglitazone significantly decreased renal TACE protein expression in treated db/db mice compared to untreated mice (p<0.05). In addition, db/db mice demonstrated a 7 fold increase in urinary ACE2 activity (15.1±4.5) compared to controls (1.74±0.9). Treatment with rosiglitazone significantly attenuated and normalized ACE2 activity in treated db/db mice (0.1±0.06). In conclusion, TACE is upregulated in db/db mice and normalizing hyperglycemia with rosiglitazone could impart renoprotection by decreasing renal TACE protein expression and shedding of renal ACE2.

Dietary induction of angiotensin-converting enzyme in proximal and distal rat small intestine

2001 ◽  
Vol 281 (5) ◽  
pp. G1221-G1227 ◽  
Author(s):  
Roger H. Erickson ◽  
Byung-Chul Yoon ◽  
Danielle Y. Koh ◽  
Do Hyong Kim ◽  
Young S. Kim
Keyword(s):  
Small Intestine ◽  
Angiotensin Converting Enzyme ◽  
Fold Increase ◽  
Mrna Levels ◽  
Converting Enzyme ◽  
Distal Intestine ◽  
Distal Small Intestine ◽  
Low Protein ◽  
Intestinal Segments ◽  
Proximal Intestine

Induction of angiotensin-converting enzyme was examined in proximal and distal intestinal segments of rats fed a low-protein (4%) diet and then switched to a high-protein (gelatin) diet. Animals were killed at varying time points, and brush-border membranes and total RNA were prepared from the segments. In the proximal intestine, there was a fivefold increase in angiotensin-converting enzyme levels after 14 days but only a twofold change in mRNA. In the distal intestine, there was no increase in enzyme activity but mRNA increased 2.4-fold. Organ culture was used to measure changes in enzyme biosynthesis. There was a 5- to 6-fold increase in the biosynthesis of angiotensin-converting enzyme in the proximal intestine 24 h after the switch to the gelatin diet and a 1.6-fold increase in mRNA levels. No change in biosynthesis was observed in the distal small intestine despite an increase in mRNA. These results support the conclusion that rapid dietary induction of intestinal angiotensin-converting enzyme is differentially regulated in proximal and distal segments of the small intestine.

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