Oral angiotensin-(1–7) peptide modulates intestinal microbiota improving metabolic profile in obese mice

2021 ◽  
Vol 28 ◽  
Author(s):  
Amanda S Machado ◽  
Janaína R Oliveira ◽  
Deborah de F Lelis ◽  
Victor Hugo D Guimarães ◽  
Alfredo M B de Paula ◽  
...  
Keyword(s):  
Intestinal Microbiota ◽  
Low Density Lipoprotein ◽  
Density Lipoprotein ◽  
Renin Angiotensin System ◽  
Oral Formulation ◽  
Obese Mice ◽  
Angiotensin System ◽  
Neutral Amino Acid Transporter ◽  
First Time ◽  
Tryptophan Uptake

Background: Obesity is a serious health problem which dysregulate Renin-Angiotensin System and intestinal microbiota. Objective: The present study aimed to evaluate the Angiotensin-(1–7) [ANG-(1–7)] oral formulation effects on obese mice intestinal microbiota. Methods: Mice were divided into four groups: obese and non-obese treated with ANG-(1–7) and obese and non-obese without ANG-(1–7) during four weeks. Results: We observed a significant decrease in the fasting plasma glucose, total cholesterol, triglycerides, and Low-density lipoprotein levels and increased High-density lipoprotein in animals treated with ANG-(1–7). The histological analysis showed intestinal villi height reduction in mice treated with ANG-(1–7). Additionally, increased Bacteroidetes and decreased Firmicutes (increased Bacteroidetes/Firmicutes ratio) and Enterobacter cloacae populations were observed in the High-Fat Diet + ANG-(1–7) group. Receptor toll-like 4 (TLR4) intestinal mRNA expression was reduced in the HFD+ ANG-(1–7) group. Finally, the intestinal expression of the neutral amino acid transporter (B0AT1) was increased in animals treated with ANG-(1–7), indicating a possible mechanism associated with tryptophan uptake. Conclusion: The results of the present study suggest for the first time an interaction between oral ANG-(1–7) and intestinal microbiota modulation.

Celecoxib Modulates the Renin-Angiotensin System in the Adipose Tissue of Obese Mice

2018 ◽  
Vol 14 (3) ◽  
pp. 203-209
Author(s):  
Jamille Fernandes Lula ◽  
Toni Ramos Alves de Souza ◽  
Keila Lopes Mendes ◽  
Alanna Fernandes Paraíso ◽  
Deborah de Farias Lelis ◽  
...  
Keyword(s):  
Adipose Tissue ◽  
Renin Angiotensin System ◽  
Obese Mice ◽  
Angiotensin System ◽  
Renin Angiotensin

scholarly journals Low HDL Cholesterol, Smoking and IL-13 R130Q Polymorphism are Associated with Myocardial Infarction in Greek Cypriot Males. A Pilot Study

2008 ◽  
Vol 2 (1) ◽  
pp. 52-59 ◽  
Author(s):  
Stavroulla Xenophontos ◽  
Marilena Hadjivassiliou ◽  
Alexandros Karagrigoriou ◽  
Nafsika Demetriou ◽  
George Miltiadous ◽  
...  
Keyword(s):  
Risk Factors ◽  
Myocardial Infarction ◽  
Low Density Lipoprotein ◽  
Density Lipoprotein ◽  
Hdl Cholesterol ◽  
Lipoprotein Cholesterol ◽  
Greek Cypriot ◽  
Low Hdl ◽  
First Time ◽  
Control Study

This study was carried out in Greek Cypriot males to identify risk factors that predispose to myocardial infarction (MI). Genetic and lipid risk factors were investigated for the first time in a Greek Cypriot male case-control study.Contrary to other studies, mean low density lipoprotein cholesterol did not differ between cases and controls. High density lipoprotein cholesterol on the other hand, although within normal range in cases and controls, was significantly higher in the control population. In agreement with many other studies, smoking was significantly more prevalent in cases compared with controls. In pooled cases and controls, smokers had a significantly lower HDL-C level compared with non-smokers. The frequency of the IL-13 R130Q homozygotes for the mutation (QQ), as well as the mutant allele were significantly higher in cases compared with controls. The IL-13 R130Q variant, or another locus, linked to it, may increase the risk of MI.

scholarly journals Galactose-specific asialoglycoprotein receptor is involved in lipoprotein (a) catabolism

2003 ◽  
Vol 376 (3) ◽  
pp. 765-771 ◽  
Author(s):  
Andelko HRZENJAK ◽  
Sasa FRANK ◽  
Xingde WO ◽  
Yonggang ZHOU ◽  
Theo van BERKEL ◽  
...  
Keyword(s):  
Physiological Function ◽  
Low Density Lipoprotein ◽  
Density Lipoprotein ◽  
Asialoglycoprotein Receptor ◽  
Fractional Catabolic Rate ◽  
Wild Type ◽  
Lipoprotein A ◽  
Apolipoprotein A ◽  
Catabolic Rate ◽  
First Time

Lp(a) [lipoprotein (a)] is a highly atherogenic plasma lipoprotein assembled from low-density lipoprotein and the glycoprotein apolipoprotein (a). The rate of Lp(a) biosynthesis correlates significantly with plasma Lp(a) concentrations, whereas the fractional catabolic rate does not have much influence. So far, little is known about Lp(a) catabolism. To study the site and mode of Lp(a) catabolism, native or sialidase-treated Lp(a) was injected into hedgehogs or ASGPR (asialoglycoprotein receptor)-knockout (ASGPR−) mice or wild-type (ASGPR+) mice, and the decay of the plasma Lp(a) concentration was followed. COS-7 cells were transfected with high- (HL-1) and low-molecular-mass ASGPR subunits (HL-2), and binding and degradation of intact or desialylated Lp(a) were measured. In hedgehogs, one of the few species that synthesize Lp(a), most of the Lp(a) was taken up by the liver, followed by kidney and spleen. Lp(a) and asialo-Lp(a) were catabolized with apparent half-lives of 13.8 and 0.55 h respectively. Asialo-orosomucoide increased both half-lives significantly. In mice, the apparent half-life of Lp(a) was 4–6 h. Catabolism of native Lp(a) by wild-type mice was significantly faster compared with ASGPR− mice and there was a significantly greater accumulation of Lp(a) in the liver of ASGPR+ mice compared with ASGPR− mice. The catabolism of asialo-Lp(a) in ASGPR− mice was 8-fold faster when compared with native Lp(a) in wild-type mice. Transfected COS-7 cells expressing functional ASGPR showed approx. 5-fold greater binding and 2-fold faster degradation of native Lp(a) compared with control cells. Our results for the first time demonstrate a physiological function of ASGPR in the catabolism of Lp(a).

scholarly journals Evaluation of the Hypocholesterolemic Effect and Phytochemical Screening of the Hydroethanolic Extract of Crataegus Aronia from Jordan

2012 ◽  
Vol 7 (1) ◽  
pp. 1934578X1200700 ◽  
Author(s):  
Entisar K. Al-Hallaq ◽  
Fatma U. Afifi ◽  
Shtaywy S. Abdalla
Keyword(s):  
Low Density Lipoprotein ◽  
Density Lipoprotein ◽  
High Cholesterol Diet ◽  
Hypocholesterolemic Effect ◽  
Cholesterol Diet ◽  
Phytochemical Screening ◽  
High Cholesterol ◽  
Chemical Screening ◽  
Hydroethanolic Extract ◽  
First Time

Chemical screening of the leaves and flowers of Crataegus aronia resulted in the isolation of hyperoside, quercetin, rutin and β-sitosterol for the first time from this plant. The effects of the hydroethanolic extract of C. aronia (CAHE) on hypercholesterolemic rats were investigated. The rats, treated orally for four weeks with 400 mg/kg/day CAHE, exhibited significant decreases in serum total cholesterol (TC) and low-density lipoprotein (LDL). The results were compared with those obtained after oral administration of atorvastatin (10 mg/kg/day). Furthermore, 10-week daily co-administration of a high cholesterol diet and CAHE (200 mg/kg/day) prevented the increase in TC and LDL. These observations indicate that CAHE has a hypocholesterolemic effect.

Renin–angiotensin system inhibitors suppress azoxymethane-induced colonic preneoplastic lesions in C57BL/KsJ-db/db obese mice

2011 ◽  
Vol 410 (1) ◽  
pp. 108-113 ◽  
Author(s):  
Masaya Kubota ◽  
Masahito Shimizu ◽  
Hiroyasu Sakai ◽  
Yoichi Yasuda ◽  
Tomohiko Ohno ◽  
...  
Keyword(s):  
Renin Angiotensin System ◽  
Obese Mice ◽  
Preneoplastic Lesions ◽  
Angiotensin System ◽  
Renin Angiotensin

scholarly journals Peculiaries of interactions between proteins of the macroglobulin family and with the endocytic receptors (a possible mechanism of transmembrane transfer)

2011 ◽  
Vol 57 (1) ◽  
pp. 106-113
Author(s):  
V.N. Zorina ◽  
R.M. Zorina ◽  
N.A. Zorin
Keyword(s):  
Low Density Lipoprotein ◽  
Density Lipoprotein ◽  
Receptor Associated Protein ◽  
Leading Role ◽  
The Family ◽  
Density Lipoprotein Receptor ◽  
A Cell ◽  
Series Of Experiments ◽  
First Time ◽  
Lipoprotein Receptor Related Protein

We have conducted a series of experiments, for specification of mechanisms which proteins of the macroglobulin family deliver regulatory substances inside of a cells. We have shown that all members of the family are not only compete for binding to proteinases, but also can interact with each other. We have confirmed that only a complex of alpha-2-macroglobulin (α2-MG) with proteinase is capable to react with the major endocytic receptor (low-density lipoprotein receptor-related protein, LRP). For the first time we have demonstrated, that interaction of α2-MG firstly with proteinase, and then with LRP provokes a progressive conformational consolidation of the multicomplex, which is accompanied by a paradoxical increase of the electrophoretic mobility in comparison with native α2-MG. We suggest that such stepwise conformational consolidation, together with earlier demonstrated charge neutralization (versus pI of internal environments) after interaction firstly with proteinase, and then with LRP, components of is the key moment of the mechanism of transmembrane transfer. Taking into account, that α2-MG transfers a broad spectrum of protein regulators, and interacts not only with LRP, but also with a signal receptor (grp78), and also can regulate (under certain conditions) both own synthesis, and synthesis of LRP and its blocker (receptor - associated protein, RAP), we suggest that this main member of the macroglobulin family plays a leading role in the regulation of intercellular interactions and in the transmission of signal inside of a cell.

scholarly journals Defective catabolism of low-density lipoprotein by fibroblasts from patients with I-cell disease

1982 ◽  
Vol 202 (1) ◽  
pp. 183-190 ◽  
Author(s):  
J C Williams ◽  
D B Weinstein ◽  
A L Miller ◽  
D Steinberg
Keyword(s):  
Low Density Lipoprotein ◽  
Lipoprotein Metabolism ◽  
Density Lipoprotein ◽  
Acid Proteinase ◽  
Low Density ◽  
Cell Disease ◽  
Mucolipidosis Ii ◽  
First Time ◽  
I Cells

Skin fibroblast cultures from patients with I-cell disease (mucolipidosis II) are characterized by multiple lysosomal enzyme deficiencies The present studies deal with the consequences of these deficiencies with respect to the metabolism of plasma low-density lipoproteins. Degradation of the protein moiety was defective in I-cells compared with control cells, but the binding and internalization of low density lipoprotein were much less affected. Measurements of low-density lipoprotein degradation in homogenates demonstrated directly for the first time a deficiency of acid proteinase activity in I-cell fibroblasts. Comparison of results in 6-h incubations with those in 24-h incubations showed accumulation of intracellular low-density lipoprotein in I-cell fibroblasts and an accelerating rate of degradation, possibly attributable to intracellular accumulation of low-density lipoprotein substrate. The significance of these findings with respect to low-density lipoprotein metabolism in vivo is discussed.

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