scholarly journals Immunonutritional Protease Inhibitors from T. durum and A. sativa Display Metabolic Similarities when Assayed on Human Macrophage-Like Cells

2021 ◽  
Vol 22 (15) ◽  
pp. 8307
Author(s):  
Bartosz Fotschki ◽  
Aurora Garcia Tejedor ◽  
Juan Antonio Nieto Fuentes ◽  
Jose Moisés Laparra Llopis
Keyword(s):  
Protease Inhibitors ◽  
Human Macrophage ◽  
Immune Reactivity ◽  
Molecular Weights ◽  
Protein Levels ◽  
Consumption Rates ◽  
Inflammatory Processes ◽  
Metabolic Protein ◽  
Components Analysis ◽  
Gastrointestinal Enzymes

This study evaluated the immunonutritional effects caused by protease inhibitors from Avena sativa and Triticum durum to human macrophage-like cells. Macrophages were exposed (3 h) to extracts obtained from flours, and mitochondrial-associated oxygen consumption rates and inflammatory, metabolic, and proteome adaptations were quantified. Mass spectrometry ‘m/z’ signals of the extracts obtained from T. durum and A. sativa revealed molecular weights of 18–35 kDa and 16–22 kDa, respectively, for the compounds present at highest concentrations. Extracts from T. durum exhibited lower susceptibility to degradation by gastrointestinal enzymes than those from A. sativa: 9.5% vs. 20.2%. Despite their different botanical origin, both extracts increased TLR4 expression. Metabolic protein levels were indicative of a decreased glycolytic to lactate flux in cell cultures upon stimulation with A. sativa extracts, which improved mitochondrial respiration in relation to those from T. durum. Principal components analysis confirmed relative similarities between immune–metabolic events triggered by immunonutritional ingredients in T. durum and A. sativa. Collectively, immunonutritional effects help to interpret the differences between both crops, worsening or improving, macrophage immune reactivity (tolerogenicity), and better control of inflammatory processes.

Isolation of specific protease inhibitors from Neurospora crassa

1976 ◽  
Vol 54 (8) ◽  
pp. 699-703 ◽  
Author(s):  
Peter H. Yu ◽  
Maria R. Kula ◽  
Hsin Tsai
Keyword(s):  
Neurospora Crassa ◽  
Protease Inhibitors ◽  
Gel Filtration ◽  
Physiological Role ◽  
Exchange Chromatography ◽  
Proteinase K ◽  
Tryptophan Synthase ◽  
Molecular Weights ◽  
Specific Protease

Four natural protease inhibitors have been partially purified by heat treatment, ion-exchange chromatography and gel filtration from Neurospora crassa. The inhibitory activity has been estimated by measuring the inhibition of proteolysis of casein as well as by the protection of Neurospora tryptophan synthase from proteolytic inactivation. The inhibitors are all oligopeptides and possess molecular weights in the range 5000 – 24 000 and appear to be very specific to Neurospora proteases. They may be classified into two types. The first are specific to Neurospora alkaline protease and the second to acidic protease. None of them exhibited any effect on other proteases including trypsin, chymotrypsin, papain, pepsin, thermolysin, subtilisin and proteinase K. The possible physiological role of these inhibitors is discussed.

scholarly journals VOC Profiles of Saliva in Assessment of Halitosis and Submandibular Abscesses Using HS-SPME-GC/MS Technique

Molecules ◽  
2019 ◽  
Vol 24 (16) ◽  
pp. 2977 ◽  
Author(s):  
Fernanda Monedeiro ◽  
Maciej Milanowski ◽  
Ileana-Andreea Ratiu ◽  
Hubert Zmysłowski ◽  
Tomasz Ligor ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Gas Chromatography ◽  
Solid Phase Microextraction ◽  
Solid Phase ◽  
Bacterial Activity ◽  
Statistical Relevance ◽  
Volatile Organic ◽  
Inflammatory Processes ◽  
Components Analysis ◽  
Potential Biomarkers

Halitosis and submandibular abscesses are examples of mouth-related diseases with the possible bacterial origin. Salivary volatile organic compounds (VOCs) are potential biomarkers of them, once they can be addressed as metabolites of bacterial activity. Healthy patients (n = 15), subjects with submandibular abscesses located in fascial deep space (n = 10), and subjects with halitosis (n = 5) were enrolled in the study. Saliva samples were subjected to headspace solid-phase microextraction (HS-SPME) and gas chromatography coupled to mass spectrometry (GC/MS) analysis. A total number of 164 VOCs was detected by the developed methodology, 23 specific for halitosis and 41 for abscess. Halitosis’ profiles were characterized by a larger number of sulfur compounds, while for abscess they had a higher variety of alcohols, aldehydes, and hydrocarbons—biomarkers of inflammatory processes. Principal components analysis allowed visualization of clusters formed according to the evaluated conditions. Kruskal-Wallis test indicated that 39 VOCs presented differentiated responses between the studied groups, with statistical relevance (p < 0.05). Random forest was applied, and a prediction model based on eight VOCs (2-butanone, methyl thioacetate, 2-methylbutanoic acid, S-methyl pentanethioate, dimethyl tetrasulfide, indolizine, pentadecane, and octadecanal) provided 100% of sensitivity, 82% of specificity, and 91% of balanced accuracy, indicating the specific presence of submandibular abscess.

scholarly journals Effect of Propofol on the Production of Inflammatory Cytokines by Human Polarized Macrophages

2019 ◽  
Vol 2019 ◽  
pp. 1-13 ◽  
Author(s):  
Tsukasa Kochiyama ◽  
Xiaojia Li ◽  
Hitoshi Nakayama ◽  
Madoka Kage ◽  
Yui Yamane ◽  
...  
Keyword(s):  
Nuclear Translocation ◽  
Inflammatory Responses ◽  
Macrophage Polarization ◽  
Signal Transduction Pathway ◽  
Induce Polarization ◽  
Human Macrophage ◽  
Related Factor ◽  
M2 Macrophages ◽  
M1 Macrophages ◽  
Inflammatory Processes

Macrophages are key immune system cells involved in inflammatory processes. Classically activated (M1) macrophages are characterized by strong antimicrobicidal properties, whereas alternatively activated (M2) macrophages are involved in wound healing. Severe inflammation can induce postoperative complications during the perioperative period. Invasive surgical procedures induce polarization to M1 macrophages and associated complications. As perioperative management, it is an important strategy to regulate polarization and functions of macrophages during inflammatory processes. Although propofol has been found to exhibit anti-inflammatory activities in monocytes and macrophages, it is unclear whether propofol regulates the functions of M1 and M2 macrophages during inflammatory processes. This study therefore investigated the effects of propofol on human macrophage polarization. During M1 polarization, propofol suppressed the production of IL-6 and IL-1β but did not affect TNF-α production. In contrast, propofol did not affect the gene expression of M2 markers, such as IL-10, TGF-β, and CD206, during M2 polarization. Propofol was similar to the GABAA agonist muscimol in inducing nuclear translocation of nuclear factor-E2-related factor 2 (Nrf2) and inhibiting IL-6 and IL-1β, but not TNF-α, production. Knockdown of Nrf2 using siRNA significantly reduced the effect of propofol on IL-6 and IL-1β production. These results suggest that propofol prevents inflammatory responses during polarization of human M1 macrophages by suppressing the expression of IL-6 and IL-1β through the GABAA receptor and the Nrf2-mediated signal transduction pathway.

scholarly journals Extracellular cell stress (heat shock) proteins—immune responses and disease: an overview

2017 ◽  
Vol 373 (1738) ◽  
pp. 20160522 ◽  
Author(s):  
A. Graham Pockley ◽  
Brian Henderson
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Stress Proteins ◽  
Biological Fluids ◽  
Stress Protein ◽  
Cell Stress ◽  
Immune Reactivity ◽  
Protein Levels ◽  
Shock Proteins ◽  
Adaptive Immune Systems

Extracellular cell stress proteins are highly conserved phylogenetically and have been shown to act as powerful signalling agonists and receptors for selected ligands in several different settings. They also act as immunostimulatory ‘danger signals’ for the innate and adaptive immune systems. Other studies have shown that cell stress proteins and the induction of immune reactivity to self-cell stress proteins can attenuate disease processes. Some proteins (e.g. Hsp60, Hsp70, gp96) exhibit both inflammatory and anti-inflammatory properties, depending on the context in which they encounter responding immune cells. The burgeoning literature reporting the presence of stress proteins in a range of biological fluids in healthy individuals/non-diseased settings, the association of extracellular stress protein levels with a plethora of clinical and pathological conditions and the selective expression of a membrane form of Hsp70 on cancer cells now supports the concept that extracellular cell stress proteins are involved in maintaining/regulating organismal homeostasis and in disease processes and phenotype. Cell stress proteins, therefore, form a biologically complex extracellular cell stress protein network having diverse biological, homeostatic and immunomodulatory properties, the understanding of which offers exciting opportunities for delivering novel approaches to predict, identify, diagnose, manage and treat disease. This article is part of the theme issue ‘Heat shock proteins as modulators and therapeutic targets of chronic disease: an integrated perspective’.

scholarly journals Biomarkers, Inflammation, and Bipolar Disorder: Association Between the Improvement of Bipolar Disorder Severity and the Improvement in C-Reactive Protein Levels After 7 Days of Inpatient Treatment

2021 ◽  
Vol 12 ◽  
Author(s):  
Alessandro Cuomo ◽  
Despoina Koukouna ◽  
Alessandro Spiti ◽  
Giovanni Barillà ◽  
Arianna Goracci ◽  
...  
Keyword(s):  
Bipolar Disorder ◽  
Inpatient Treatment ◽  
Inflammatory Marker ◽  
C Reactive Protein ◽  
Disease Symptoms ◽  
Mortality And Morbidity ◽  
Protein Levels ◽  
Reactive Protein ◽  
Inflammatory Processes ◽  
The Relationship

Introduction: Compared to the general population, people with severe mental illness (SMI) have a poorer health status and a higher mortality rate, with a 10–20-year reduction in life expectancy. Excess mortality and morbidity in SMI have been explained by intertwined components. Inflammatory processes could increase the morbidity and mortality risk in patients with bipolar disorder (BD) because of a bidirectional interaction between BD and conditions related to inflammation. This pilot study aimed to evaluate the relationship between C-Reactive-Protein (CRP) and bipolar disorder severity.Methods: A retrospective observational study was conducted on 61 hospitalized patients with bipolar disorder. CRP was measured at admission to inpatient treatment (T0) and after seven days from the admission (T1). Clinical Global Impression for Depression, Mania and Overall Bipolar Illness were recorded at T0 and T1. Comparisons among the recorded CRP values were determined through the paired t-test. Correlations between CRP and CGI scores were determined through Spearman's correlation coefficient at T0 and T1.Results: A statistically significant decrease in CRP values was observed after 7 days of hospitalization (p &lt; 0.001) and positive significant correlations emerged between CRP and CGI scores at T0 and T1.Conclusion: Patients admitted to the inpatient unit reported a statistically significant decrease of CRP values during the first 7 days of treatment. Although the direction of the relationship between BP severity and inflammation status continues to remain unclear, this study showed a relationship between the improvement of bipolar disease symptoms and the improvement of the inflammatory marker CRP.

Rat intestinal maltase–glucoamylase. Purification of the detergent-solubilized enzyme in the presence of protease inhibitors: properties and identification of a protease-sensitive subunit

1984 ◽  
Vol 62 (1) ◽  
pp. 36-43 ◽  
Author(s):  
Lilian Lee ◽  
Gordon Forstner
Keyword(s):  
Protease Inhibitors ◽  
Gradient Centrifugation ◽  
Sodium Dodecyl ◽  
Prolonged Storage ◽  
Affinity Column ◽  
Molecular Weights ◽  
Clear Cut ◽  
Maltase Activity ◽  
Continuous Presence ◽  
Monomeric Proteins

Failure to develop clear-cut, distinguishing characteristics for hydrophobic and hydrophilic forms of maltase–glucoamylase led us to attempt the purification of the detergent-extracted enzyme in the continuous presence of protease inhibitors (phenylmethylsulfonyl fluoride and N-ethylmaleimide). The enzyme was purified by molecular exclusion, anion-exchange, and affinity column chromatography to a final specific maltase activity of 80 U/mg protein, comparable to previously solubilized enzymes. Both detergent (d-maltase) and proteolytically (p-maltase) solubilized enzymes had identical Km's for maltose and similar glycogenase activity. d-Maltase was clearly amphipathic. Whereas 95% of p-maltase was eluted with aqueous buffer from an octyl-Sepharose CL-4B column, the elution of d-maltase required solutions containing Triton X-100 and ethylene glycol. On density gradient centrifugation and sodium dodecyl sulfate (SDS) – polyacrylamide gels, p-maltase migrated as one high molecular weight species of 500 000. In contrast d-maltase migrated heterogeneously and the smallest maltase-active forms delineated by these two techniques, as well as by high pressure liquid chromatography, had molecular weights which ranged from 120 000 to 150 000. Both p- and d-maltase were dissociated by heat in SDS, forming five prominent species as we have previously described. In contrast to p-maltase, in which the smallest species, band 1, equalled 36.7% of the total mass, band 1 of d-maltase accounted for 66.5%. Band 1 was separable when smaller amounts of enzyme were applied to slab gels and stained with silver, into two proteins of 130 000 and 145 000 daltons. The 145 000 dalton protein was absent in p-maltase and was replaced by a faint band of 140 000 daltons. The 140 000 dalton band, plus a new N-terminal glycine, were also generated from d-maltase during prolonged storage at −20 °C. These data suggest that rat intestinal maltase–glucoamylase contains two monomeric proteins. The largest monomer contains an additional peptide segment at the N-terminus, which is removed by proteolysis and presumably anchors the enzyme to the microvillus membrane. After removal from the membrane, the two monomers of the d-enzyme are apparently partially dissociated to account for maltase activity within the 120 000 to 150 000 dalton range. Conversely, removal of the anchor segment favours a polymeric structure.

scholarly journals Histopathological alterations in bullfrog juveniles fed commercial rations of different crude protein levels

2009 ◽  
Vol 38 (12) ◽  
pp. 2306-2310 ◽  
Author(s):  
José Teixeira de Seixas Filho ◽  
Marcio Hipolito ◽  
Ana Maria Cristina Rabello Pinto da Fonseca Martins ◽  
Eliane Rodrigues ◽  
Airton Antonio Castagna ◽  
...  
Keyword(s):  
Crude Protein ◽  
Renal Tubule ◽  
Histopathological Examination ◽  
Second Phase ◽  
Biological Value ◽  
Protein Levels ◽  
Dietary Crude Protein ◽  
Inflammatory Processes ◽  
The Relationship

The relationship between the quality of dietary crude protein and health of bullfrog juveniles (Lithobates catesbeianus) was evaluated by necropsy and histopathological examination of animals. The histopathology results showed that animals fed different feeds, regardless of CP levels, presented lymphocytary hepatitis, colitis and flattened microvillosities; kidneys with areas of tubulonephrosis and renal tubule calcification; myocarditis and cardiac muscular fiber dissociation. Such injuries suggested a degenerative nutritional process, with development of inflammatory processes spread to all the organs. These findings suggested that the animals had been fed with proteins of low biological value, indicating, apparently, poor feed quality, that harmed the health of the frogs and, consequently, their performance. Complementary studies are necessary to understand the biochemical behavior of the bullfrog in its second phase of life, supplying data for a better understanding of the nutrition of these animals.

scholarly journals Adiponectin Expression Is Modulated by Long-Term Physical Activity in Adult Patients Affected by Cystic Fibrosis

2019 ◽  
Vol 2019 ◽  
pp. 1-7 ◽  
Author(s):  
Rita Polito ◽  
Ersilia Nigro ◽  
Ausilia Elce ◽  
Maria Ludovica Monaco ◽  
Paola Iacotucci ◽  
...  
Keyword(s):  
Physical Activity ◽  
Cystic Fibrosis ◽  
Forced Expiratory Volume ◽  
Total Serum ◽  
C Reactive Protein ◽  
Protein Levels ◽  
Reactive Protein ◽  
Inflammatory Status ◽  
Inflammatory Processes

Cystic fibrosis (CF) is a genetic disease characterized by progressive decline of lung function and chronic airway inflammation. Adipose tissue, through adiponectin and leptin, exerts several effects on energy metabolism and inflammatory processes. This study evaluated the levels of adiponectin and leptin in adult healthy subjects, in patients with CF and their correlation with long-term physical activity. CF patients were divided into two groups (sedentary versus active) based on their regular physical activity over 3 years. Anthropometric and serum biochemical profiles of CF patients and controls were evaluated and compared. Total serum adiponectin and leptin levels were measured by ELISA; adiponectin oligomeric profiles were analysed by western blot. Adiponectin levels were significantly higher while leptin levels were lower in patients with CF than in healthy controls. Furthermore, adiponectin was significantly lower in active compared to sedentary CF (p=0.047), while leptin was slightly increased in active compared to sedentary CF. In addition, C-reactive protein levels were significantly lower in active than in sedentary CF patients (p=0.048). Interestingly, only in the active group adiponectin levels were inversely correlated with forced expiratory volume (FEV) 1% decrease/year and FEV1% decrease. Moreover, adiponectin levels negatively correlated with lipid profiles. Our findings indicated that regular, long-term physical activity in CF improves respiratory function, metabolism, and inflammation status. These improvements in patients’ conditions are associated with immunometabolic processes involving adiponectin, leptin, and C-reactive protein. Therefore, we propose that both adipokines may be a useful biomarker in the evaluation of metabolic and inflammatory status in patients with CF.

scholarly journals Ubiquitin-Specific Protease 2 Modulates the Lipopolysaccharide-Elicited Expression of Proinflammatory Cytokines in Macrophage-like HL-60 Cells

2017 ◽  
Vol 2017 ◽  
pp. 1-15 ◽  
Author(s):  
Hiroshi Kitamura ◽  
Takeshi Ishino ◽  
Yoshinori Shimamoto ◽  
Jun Okabe ◽  
Tomomi Miyamoto ◽  
...  
Keyword(s):  
Proinflammatory Cytokines ◽  
Peritoneal Macrophages ◽  
Human Macrophage ◽  
Mrna Levels ◽  
Mrna Accumulation ◽  
Protein Levels ◽  
Protein Ubiquitination ◽  
Specific Protease ◽  
Tlr4 Activation ◽  
Mouse Peritoneal Macrophages

We investigated the regulatory roles of USP2 in mRNA accumulation of proinflammatory cytokines in macrophage-like cells after stimulation with a toll-like receptor (TLR) 4 ligand, lipopolysaccharide (LPS). Human macrophage-like HL-60 cells, mouse macrophage-like J774.1 cells, and mouse peritoneal macrophages demonstrated negative feedback to USP2 mRNA levels after LPS stimulation, suggesting that USP2 plays a significant role in LPS-stimulated macrophages.USP2knockdown (KD) by short hairpin RNA in HL-60 cells promoted the accumulation of transcripts for 25 of 104 cytokines after LPS stimulation. In contrast, limited induction of cytokines was observed in cells forcibly expressing the longer splice variant of USP2 (USP2A), or in peritoneal macrophages isolated fromUsp2atransgenic mice. An ubiquitin isopeptidase-deficient USP2A mutant failed to suppress LPS-induced cytokine expression, suggesting that protein ubiquitination contributes to USP2-mediated cytokine repression. Although USP2 deficiency did not accelerate TNF receptor-associated factor (TRAF) 6-nuclear factor-κB (NF-κB) signaling, it increased the DNA binding ratio of the octamer binding transcription factor (Oct)-1 to Oct-2 inTNF,CXCL8,CCL4, andIL6promoters. USP2 decreased nuclear Oct-2 protein levels in addition to decreasing the polyubiquitination of Oct-1. In summary, USP2 modulates proinflammatory cytokine induction, possibly through modification of Oct proteins, in macrophages following TLR4 activation.

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