-
Genes Oct 2023The Mediterranean diet (MedD) has been shown to have beneficial effects on health, well-being, and mental status. It potentially modulates gene expressions linked to...
The Mediterranean diet (MedD) has been shown to have beneficial effects on health, well-being, and mental status. It potentially modulates gene expressions linked to oxidative stress, contributing to its beneficial effects on overall health. The aim of this study was to assess the effects of MedD treatment in healthy human volunteers on the expression of ten genes related to oxidative stress and inflammation in women and men. Of 30 enrolled subjects, 17 were eligible, 10 women and 7 men. All of them received the same MedD treatment. Before and after 8 weeks of MedD treatment, an evaluation of body composition, blood tests, and anthropometric and clinical parameters was performed. Furthermore, 10 genes were amplified and analyzed. The study showed significant differences between females and males in body composition and biochemical parameters before and after MedD treatment. Significant differences between females and males in Resistance Force ( < 0.009) and Diastolic Blood Pressure ( < 0.04) before MedD treatment, and in High-Density Lipoprotein ( < 0.02) after MedD treatment, were observed. Moreover, a significant upregulation of and in females has been shown. Sex differences impact MedD treatment response, and influence the genetic expression of genes related to oxidative stress; our findings may help to personalize diet therapy and contribute to overall health and well-being.
Topics: Humans; Male; Female; Diet, Mediterranean; Pilot Projects; Nutrigenomics; Sex Characteristics; Oxidative Stress
PubMed: 38002923
DOI: 10.3390/genes14111980 -
Foods (Basel, Switzerland) Nov 2023Hypertension is a widespread health risk, affecting over a billion people and causing 9 million deaths per year. The Renin-Angiotensin-Aldosterone System (RAAS) is a...
Hypertension is a widespread health risk, affecting over a billion people and causing 9 million deaths per year. The Renin-Angiotensin-Aldosterone System (RAAS) is a primary target for hypertension treatment, and it is primarily treated through drugs that inhibit the Angiotensin I-Converting Enzyme (ACE). In addition to pharmacological treatment, various plants are recommended in traditional medicine for blood pressure regulation. This study aimed to produce high-phenolic-content extracts with and without enzymatic assistance from red grape pomace and evaluate their antioxidant capacity and ACE inhibitory potential. The total phenolic content (TPC) was measured, and phenolic identification was performed using HPLC analysis. In addition, the antioxidant capacity and anti-hypertensive potential were determined via in vitro assays. There was no statistical difference in the TPC antioxidant capacity between the extraction methods. Otherwise, when considering the extraction yield, the enzymatic process recovered around 70% more phenolic compounds from the pomace, and the phenolic profile was changed. Enzymatic assistance also significantly increased the ACE inhibitory potential in the grape pomace extract. This study demonstrates the viability of upcycling grape pomace to obtain bioactive compounds and to reduce their environmental impact, and highlights the influence of the enzymatic extraction on the hypotensive potential of the extract.
PubMed: 38002167
DOI: 10.3390/foods12224109 -
European Journal of Mass Spectrometry... Oct 2023In remembrance of Prof. Dr Przybylski, we are presenting a vision towards his beloved mass spectrometry (MS) and its far-reaching promises outside of the academic...
In remembrance of Prof. Dr Przybylski, we are presenting a vision towards his beloved mass spectrometry (MS) and its far-reaching promises outside of the academic laboratory. Sub-atmospheric pressure (AP) ionization MS is well positioned to make a step-change in direct ionization, a concept that allows ionization and mass analyses of volatile and nonvolatile molecules from clean or dirty samples, directly, accurately, sensitively, and in a straightforward manner that has the potential to expand the field of MS into unchartered application areas. Contrary to ambient ionization MS, ionization commences in the sub-AP region of the mass spectrometer, important for practical and safety reasons, and offers , simplicity, speed, sensitivity, and robustness directly from real-world samples without cleanup. The plate source concept, presented here, provides an easy to use, rapid, and direct sample introduction from AP into the sub-AP of a mass spectrometer. Utilizing sub-AP ionization MS based on the plate source concept, small to large molecules from various environments that would be deemed too dirty for some direct MS methods are demonstrated. The new source concept can be expanded to include multiple ionization methods using the same plate source "front end" without the need to vent the mass spectrometer between the different methods, thus allowing ionization of more compounds on the same mass spectrometer for which any one ionization method may be insufficient. Examples such as fentanyl, gamma-hydroxybutyric acid, clozapine, 1-propionyllysergic acid, hydrocodone angiotensin I and II, myoglobin, and carbonic anhydrase are included.
PubMed: 37999746
DOI: 10.1177/14690667231211486 -
Food Research International (Ottawa,... Dec 2023Dairy-derived angiotensin-I-converting enzyme inhibitory peptides (ANGICon-EIPs) have been regarded as a relatively safe supplementary diet-therapy strategy for... (Review)
Review
Dairy-derived angiotensin-I-converting enzyme inhibitory peptides (ANGICon-EIPs) have been regarded as a relatively safe supplementary diet-therapy strategy for individuals with hypertension, and short-chain peptides may have more relevant antihypertensive benefits due to their direct intestinal absorption. Our previous explorations have confirmed that endogenous goat milk short-chain peptides are also an essential source of ANGICon-EIPs. Nonetheless, there are limited explorations on endogenous ANGICon-EIPs owing to the limitations of the extraction and enrichment of endogenous peptides, currently. This review outlined ameliorated pre-treatment strategies, data acquisition methods, and tools for the prediction of peptide structure and function, aiming to provide creative ideas for discovering novel ANGICon-EIPs. Currently, deep learning-based peptide structure and function prediction algorithms have achieved significant advancements. The convolutional neural network (CNN) and peptide sequence-based multi-label deep learning approach for determining the multi-functionalities of bioactive peptides (MLBP) can predict multiple peptide functions with absolute true value and accuracy of 0.699 and 0.708, respectively. Utilizing peptide sequence input, torsion angles, and inter-residue distance to train neural networks, APPTEST predicted the average backbone root mean square deviation (RMSD) value of peptide (5-40 aa) structures as low as 1.96 Å. Overall, with the exploration of more neural network architectures, deep learning could be considered a critical research tool to reduce the cost and improve the efficiency of identifying novel endogenous ANGICon-EIPs.
Topics: Humans; Deep Learning; Proteins; Neural Networks, Computer; Peptides; Amino Acid Sequence
PubMed: 37986483
DOI: 10.1016/j.foodres.2023.113640 -
Food Research International (Ottawa,... Dec 2023The molecular and biofunctional properties of protein and phenolic fractions in edible truffles remain largely unknown. This study examined the effect of ultrasonication...
Impact of ultrasonication on the contents, profiles and biofunctional properties of free and bound phenolics from white desert truffle (Tirmania nivea) and its protein fractions.
The molecular and biofunctional properties of protein and phenolic fractions in edible truffles remain largely unknown. This study examined the effect of ultrasonication on the contents, profiles, and bioactive properties of free and bound phenolics (FP and BP) from desert truffle (Tirmania nivea) and its protein fractions. Protein fractions from the Osborne extraction scheme were biochemically and structurally characterized. The albumin fraction showed the highest abundance (16.8%) and yield (35.8%). Total phenolic contents were the highest in non-sonicated samples (3.5-34.1 mg/g), particularly in the albumin fraction and in whole truffle. FP extracted at 30 °C (FP-30 °C) accounted for the largest proportion of total phenolics in all protein fractions, whereas BP-30 °C and FP-60 °C were predominant in non-sonicated and sonicated truffle, respectively. The highest antioxidant activity was obtained with FP-30 °C extracts from non-sonicated albumins, globulins and truffle (91.9, 72.7 and 30.0%), followed by BP-30 °C from non-sonicated albumins (25.4%) and FP-60 °C from sonicated glutelins-1 (24.2%). High inhibition of α-amylase was evidenced in several extracts, including FP-30 °C from non-sonicated glutelins-1 (99.2%) and FP-30 °C from sonicated globulins (72.4%). Several extracts also displayed high inhibition of angiotensin I-converting enzyme (ACE), including FP-60 °C from non-sonicated glutelins-1 (65.1%) and sonicated glutelins-1 (71.1%) and globulins (64.7%). Most extracts were rich in epicatechin, gallic acid, chlorogenic acid and catechin. Correlations between phenolic content, antioxidant activity, anti-α-amylase and anti-ACE activities were influenced by sonication. Sonication reduced the particle size of the proteins and modified their structural characteristics. These findings demonstrate that white desert truffle proteins co-occur with bioactive phenolics whose functionalities can be tailored by protein fractionation and sonication.
Topics: Antioxidants; Phenols; Catechin; alpha-Amylases; Albumins; Globulins; Glutens
PubMed: 37986408
DOI: 10.1016/j.foodres.2023.113453 -
Critical Care (London, England) Nov 2023The renin-angiotensin system (RAS) plays a crucial role in regulating blood pressure and the cardio-renal system. The classical RAS, mainly mediated by angiotensin I,... (Review)
Review
The renin-angiotensin system (RAS) plays a crucial role in regulating blood pressure and the cardio-renal system. The classical RAS, mainly mediated by angiotensin I, angiotensin-converting enzyme, and angiotensin II, has been reported to be altered in critically ill patients, such as those in vasodilatory shock. However, recent research has highlighted the role of some components of the counterregulatory axis of the classical RAS, termed the alternative RAS, such as angiotensin-converting Enzyme 2 (ACE2) and angiotensin-(1-7), or peptidases which can modulate the RAS like dipeptidyl-peptidase 3, in many critical situations. In cases of shock, dipeptidyl-peptidase 3, an enzyme involved in the degradation of angiotensin and opioid peptides, has been associated with acute kidney injury and mortality and preclinical studies have tested its neutralization. Angiotensin-(1-7) has been shown to prevent septic shock development and improve outcomes in experimental models of sepsis. In the context of experimental acute lung injury, ACE2 activity has demonstrated a protective role, and its inactivation has been associated with worsened lung function, leading to the use of active recombinant human ACE2, in preclinical and human studies. Angiotensin-(1-7) has been tested in experimental models of acute lung injury and in a recent randomized controlled trial for patients with COVID-19 related hypoxemia. Overall, the alternative RAS appears to have a role in the pathogenesis of disease in critically ill patients, and modulation of the alternative RAS may improve outcomes. Here, we review the available evidence regarding the methods of analysis of the RAS, pathophysiological disturbances of this system, and discuss how therapeutic manipulation may improve outcomes in the critically ill.
Topics: Humans; Renin-Angiotensin System; Angiotensin-Converting Enzyme 2; Critical Illness; Angiotensin II; Acute Lung Injury
PubMed: 37986086
DOI: 10.1186/s13054-023-04739-5 -
Plant Foods For Human Nutrition... Mar 2024Angiotensin I-converting enzyme (ACE)-inhibiting peptides were isolated from walnut protein isolate (WPI) using ultrasound-assisted extraction. This study aimed to...
Screening and Constructing of Novel Angiotensin I-Converting Enzyme Inhibiting Peptides from Walnut Protein Isolate and Their Mechanisms of Action: A Merged In Silico and In Vitro Study.
Angiotensin I-converting enzyme (ACE)-inhibiting peptides were isolated from walnut protein isolate (WPI) using ultrasound-assisted extraction. This study aimed to assess the impact of ultrasonic pretreatment on the physicochemical properties of WPI. The optimal extraction conditions for WPI were determined as a 15-min ultrasonic treatment at 400 W. Subsequently, the hydrolysate exhibiting the highest in vitro ACE-inhibiting activity underwent further processing and separation steps, including ultrafiltration, ion exchange chromatography, liquid chromatography-tandem mass spectrometry, ADMET screening, and molecular docking. As a result of this comprehensive process, two previously unidentified ACE-inhibiting peptides, namely Tyr-Ile-Gln (YIQ) and Ile-Tyr-Gln (IYQ), were identified. In addition, a novel peptide, Ile-Lys-Gln (IKQ), was synthesized, demonstrating superior ACE-inhibiting activity and temperature stability. In silico analysis estimated an in vivo utilization rate of 21.7% for IKQ. These peptides were observed to inhibit ACE through an anti-competitive mechanism, with molecular docking simulations suggesting an interaction mechanism involving hydrogen bonding. Notably, both IYQ and IKQ peptides exhibited no discernible toxicity to HUVECs cells and promoted nitric oxide (NO) generation. These findings underscore the potential of ultrasonicated WPI in the separation of ACE-inhibiting peptides and their utility in the development of novel ACE inhibitors for functional food applications.
Topics: Juglans; Peptidyl-Dipeptidase A; Molecular Docking Simulation; Peptides; Angiotensin-Converting Enzyme Inhibitors; Protein Hydrolysates
PubMed: 37962805
DOI: 10.1007/s11130-023-01122-1 -
Protein and Peptide Letters 2023Islet β-cell dedifferentiation may be the main cause of reduced insulin secretion. Angiotensin-(1-7) [Ang-(1-7)] can attenuate high glucose-induced apoptosis and...
BACKGROUND
Islet β-cell dedifferentiation may be the main cause of reduced insulin secretion. Angiotensin-(1-7) [Ang-(1-7)] can attenuate high glucose-induced apoptosis and dedifferentiation of pancreatic β-cell, but the specific signal transduction pathway and mechanism are not yet clear.
OBJECTIVES
This study aimed to investigate the effects of Ang-(1-7) on high glucose-induced islet β-cell dedifferentiation by activating the phosphatidylinositol-3-kinase/Protein kinase B/ Forkhead box transcription factor O1 (PI3K/Akt/FoxO1) signaling pathway.
METHODS
The mouse islet β-cell line MIN6 cells were passaged and cultured and randomly divided into five groups: control (Con) group, high glucose (HG) group, HG with Ang-(1-7) group, HG with Ang-(1-7) and specific MasR antagonist A-779 group, and HG with Ang-(1-7) and PI3K inhibitor LY294002 group. After 48 hours, glucose-stimulated insulin secretion (GSIS) was detected by Enzyme-Linked Immunosorbent Assay (ELISA). The mRNA and protein expression levels of β-cell-specific factors (Pancreatic duodenal homeobox-1 (Pdx1), v-maf musculoaponeurotic fibrosarcoma oncogene homolog A(MafA)) and endocrine progenitor cell-specific factors (Octamer binding transcription factor 4(Oct4), Nanog) were measured by Real Time-PCR and Western blot. The factors of protein expression levels of PI3K/Akt/FoxO1 signaling pathway (Akt, p-Akt, Fox- O1, p-FoxO1) were determined by Western blot.
RESULTS
We observed for the first time that high glucotoxicity can induce dedifferentiation of pancreatic islet β-cell, causing a decrease in insulin secretion levels and expression of Pdx1, MafA, p-- FoxO1, and p-Akt and an increase in expression of Oct4 and Nanog. After Ang-(1-7) intervention, insulin secretion levels and expression of Pdx1, MafA, p-FoxO1 and p-Akt were increased, and the levels of Oct4 and Nanog were reduced. However, A-779 and LY294002 could reverse this effect. During these processes, the total Akt and total FoxO1 expression did not change significantly.
CONCLUSION
Ang-(1-7) may prevent high glucose-induced pathological dedifferentiation of pancreatic β-cell by activating the PI3K/Akt/FoxO1 signaling pathway.
Topics: Mice; Animals; Proto-Oncogene Proteins c-akt; Phosphatidylinositol 3-Kinases; Cell Dedifferentiation; Trans-Activators; Islets of Langerhans; Glucose
PubMed: 37953618
DOI: 10.2174/0109298665257646231020054036 -
Bioscience Reports Nov 2023Abdominal aortic aneurysm (AAA) represents a debilitating vascular disease characterized by aortic dilatation and wall rupture if it remains untreated. We aimed to...
Abdominal aortic aneurysm (AAA) represents a debilitating vascular disease characterized by aortic dilatation and wall rupture if it remains untreated. We aimed to determine the effects of Ang 1-7 in a murine model of AAA and to investigate the molecular mechanisms involved. Eight- to 10-week-old apolipoprotein E-deficient mice (ApoEKO) were infused with Ang II (1.44 mg/kg/day, s.c.) and treated with Ang 1-7 (0.576 mg/kg/day, i.p.). Echocardiographic and histological analyses showed abdominal aortic dilatation and extracellular matrix remodeling in Ang II-infused mice. Treatment with Ang 1-7 led to suppression of Ang II-induced aortic dilatation in the abdominal aorta. The immunofluorescence imaging exhibited reduced smooth muscle cell (SMC) density in the abdominal aorta. The abdominal aortic SMCs from ApoEKO mice exhibited markedly increased apoptosis in response to Ang II. Ang 1-7 attenuated cell death, as evident by increased SMC density in the aorta and reduced annexin V/propidium iodide-positive cells in flow cytometric analysis. Gene expression analysis for contractile and synthetic phenotypes of abdominal SMCs showed preservation of contractile phenotype by Ang 1-7 treatment. Molecular analyses identified increased mitochondrial fission, elevated cellular and mitochondrial reactive oxygen species (ROS) levels, and apoptosis-associated proteins, including cytochrome c, in Ang II-treated aortic SMCs. Ang 1-7 mitigated Ang II-induced mitochondrial fission, ROS generation, and levels of pro-apoptotic proteins, resulting in decreased cell death of aortic SMCs. These results highlight a critical vasculo-protective role of Ang 1-7 in a degenerative aortic disease; increased Ang 1-7 activity may provide a promising therapeutic strategy against the progression of AAA.
Topics: Animals; Mice; Reactive Oxygen Species; Angiotensin II; Aortic Aneurysm, Abdominal; Aorta, Abdominal; Apoptosis Regulatory Proteins; Myocytes, Smooth Muscle; Disease Models, Animal; Mice, Inbred C57BL
PubMed: 37947205
DOI: 10.1042/BSR20230718 -
Food Chemistry Mar 2024In this study, black sesame seeds were fermented by Lactobacillus Plantarum NCU116 and then hydrolyzed using acid protease to improve Angiotensin-I-converting enzyme...
In this study, black sesame seeds were fermented by Lactobacillus Plantarum NCU116 and then hydrolyzed using acid protease to improve Angiotensin-I-converting enzyme (ACE) inhibitory activity. The random forest-particle swarm optimization (RF-PSO) model was applied to predict the ACE inhibitory activity during the hydrolysis process based on the experimental data. After separating by adsorption chromatography, gel filtration chromatography, and reversed phased-high performance liquid chromatography and then screening in silico method, eight peptides were identified from fermented black sesame seed hydrolysates as ITAPHW, SLPNYHPSPR, QYLPR, IRPNGL, YHNAPIL, LSYPR, GFAGDDAPRA, and LDPNPRSF with IC values of 51.69 μM, 146.67 μM, 655.02 μM, 752.60 μM, 1.02 mM, 2.01 mM, 1.97 mM, and 3.43 mM, respectively. ITAPHW and SLPNYHPSPR exhibited high antioxidant activity and inhibited the ACE activity in a non-competitive pattern. Molecular docking revealed that the strong ACE inhibition of ITAPHW and SLPNYHPSPR is probably attributed to the interaction with Zn of ACE.
Topics: Molecular Docking Simulation; Sesamum; Angiotensin-Converting Enzyme Inhibitors; Random Forest; Peptides; Hydrolysis; Peptidyl-Dipeptidase A; Protein Hydrolysates
PubMed: 37944395
DOI: 10.1016/j.foodchem.2023.137921