-
Clinical Otolaryngology : Official... Jul 2023To investigate the association between laryngopharyngeal reflux (LPR), gastroesophageal reflux disease (GERD) and recalcitrant chronic rhinosinusitis (CRS). (Review)
Review
OBJECTIVE
To investigate the association between laryngopharyngeal reflux (LPR), gastroesophageal reflux disease (GERD) and recalcitrant chronic rhinosinusitis (CRS).
DATA SOURCES
PubMed, Cochrane Library and Scopus.
REVIEW METHODS
Three investigators searched the specified databases for studies investigating the relationship between LPR, GERD and recalcitrant CRS with or without polyposis. The following outcomes were investigated with PRISMA criteria: age; gender; reflux and CRS diagnosis; association outcomes and potential treatment outcomes. The authors performed a bias analysis of papers and provided recommendations for future studies.
RESULTS
A total of 17 studies investigated the association between reflux and recalcitrant CRS. According to pharyngeal pH monitoring, 54% of patients with recalcitrant CRS reported hypo or nasopharyngeal acid reflux events. The number of hypo- and nasopharyngeal acid reflux events was significantly higher in patients compared to healthy individuals in 4 and 2 studies, respectively. Only one study did not report intergroup differences. The proportion of GERD was significantly higher in CRS patients compared to controls, with a prevalence ranging from 32% to 91% of cases. No author considered nonacid reflux events. There was significant heterogeneity in the inclusion criteria; definition of reflux and association outcomes, limiting the ability to draw clear conclusions. Pepsin was found in sinonasal secretions more frequently in CRS patients than controls.
CONCLUSION
Laryngopharyngeal reflux and GERD may be contributing factors of CRS therapeutic resistance, but future studies are needed to confirm the association considering nonacid reflux events.
Topics: Humans; Laryngopharyngeal Reflux; Esophagitis, Peptic; Pepsin A; Sinusitis
PubMed: 36895147
DOI: 10.1111/coa.14047 -
Lin Chuang Er Bi Yan Hou Tou Jing Wai... Feb 2023To analyze the consistency of pepsin assay kit, pepsin IHC, reflux symptom index(RSI) and reflux finding score(RFS) in the diagnosis of laryngopharyngeal reflux...
To analyze the consistency of pepsin assay kit, pepsin IHC, reflux symptom index(RSI) and reflux finding score(RFS) in the diagnosis of laryngopharyngeal reflux disease(LPRD). The clinical data of 61 inpatients with laryngeal diseases who were admitted to the Department of Otolaryngology, the First Affiliated Hospital of Kunming Medical University from May 2020 to December 2021 were retrospectively analyzed. The RSI and RFS scores, the Formwitz score of pepsin immunohistochemistry, and the results of pepsin detection kit were recorded. ICC group correlation coefficient and Kappa consistency analysis was used for three detection methods. Among 61 patients, 30 cases were positive and 31 cases were negative for the pepsin test kit, with a positive rate of 49.18%. The positive rate of pepsin immunohistochemistry was 45.90%(28/61), and the diagnostic agreement rate between the two was 70.49%. The consistency between them was high(=0.409). The positive rate of RSI and RFS in diagnosing LPRD was 62.30%(38/61), and the consistency rate was 73.77% with pepsin detection kit. The consistency between them was high(=0.486). Taking pepsin IHC as the reference standard, the sensitivity, specificity, positive predictive value and negative predictive value of pepsin detection kit were 71.43%(20/28), 69.70%(23/33), 66.67%(20/30) and 74.19%(23/31), respectively. Using RSI and RFS scales as reference criteria, the sensitivity, specificity, positive predictive value and negative predictive value of pepsin detection kit were 89.29%(25/28), 60.61%(20/33), 65.79%(25/38) and 86.96%(20/23), respectively. Analysis of correlation coefficient within ICC group: ICC value was 0.628, 95% confidence interval(0.497-0.741), the three methods have good consistency. The RSI and RFS scale scores were in good agreement with the pepsin test kit, and the pepsin test kit was also in good agreement with pepsin immunohistochemistry. As a non-invasive diagnostic technique, the pepsin test kit can be widely used in the diagnosis of pharyngeal reflux in combination with pepsin immunohistochemistry and RSI and RFS scale.
Topics: Humans; Laryngopharyngeal Reflux; Pepsin A; Retrospective Studies; Immunohistochemistry; Pharynx
PubMed: 36756822
DOI: 10.13201/j.issn.2096-7993.2023.02.004 -
Indian Journal of Pharmacology 2022The current study aimed to estimate phytochemical screening, in vitro antioxidant activity, and gastroprotective activity of Sesamum indicum Linn ethanolic extract.
OBJECTIVE
The current study aimed to estimate phytochemical screening, in vitro antioxidant activity, and gastroprotective activity of Sesamum indicum Linn ethanolic extract.
MATERIALS AND METHODS
The current study was held out by ulceration induced by pylorus ligation and indomethacin-induced ulcer screening models in Wister albino rats. The screening of antiulcer activity of ethanolic extract of S. indicum leaves (EESIL) at the different amounts (100, 200, and 400 mg/kg; per orally for 7 days) was compared with omeprazole as a usual antiulcer drug. Additional parameters such as gastric content, pH, total acidity, pepsin activity ulcer score, free acidity, ulcer index (UI), % inhibition of ulcers, mean mucin, pepsin content, and total protein content were observed.
RESULTS
In the pylorus ligation model, the pepsin activity free acidity, pepsin content, UI, total acidity, ulcer score, total protein content, and percentage ulcer inhibition were considerably decreased (P < 0.05 and P < 0.01), and mean mucin and gastric content pH extensively elevated (P < 0.05 and P < 0.01) in EESIL tested groups in the comparison of the control group. Doses (100, 200, and 400 mg/kg p.o.) of EESIL showed dose-reliant gastro protective outcomes, a considerable (P < 0.05 and P < 0.01) decrease in gastric parameters as UI and ulcer score and induction in gastric pH and percentage inhibition of ulcer compared with the control group.
CONCLUSION
Antioxidant, anti-Ulcer, EESIL, and EESIL show antioxidant activity at different concentration. The fallout of the study indicated that the EESIL had improved antiulcer potential due to the decrease in offensive factors and increase in defensive factors.
Topics: Rats; Animals; Rats, Wistar; Antioxidants; Pepsin A; Sesamum; Ethanol; Mucins; Plant Extracts
PubMed: 36722554
DOI: 10.4103/ijp.ijp_98_22 -
Scientific Reports Jan 2023Protein hydrolysates from dietary sources possess many physiological and biological properties. Artocarpus altilis is an evergreen multipurpose plant with many benefits....
Protein hydrolysates from dietary sources possess many physiological and biological properties. Artocarpus altilis is an evergreen multipurpose plant with many benefits. Therefore, this study evaluates in vitro antioxidant and anti-inflammatory properties of A. altilis protein hydrolysates. Protein was isolated from A. altilis and hydrolysed with pepsin and trypsin separately using different enzyme: substrate ratios (1:8, 1:16, 1:32). Antioxidant properties investigated included Fe-chelating, 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical and hydrogen peroxide radical scavenging activities. Anti-inflammatory activities were determined using effects on hypotonic solution-induced cell lysis on red blood cell membrane stabilisation and heat-induced protein denaturation. The degree of hydrolysis of trypsin hydrolysate increased with increasing enzyme-substrate ratio, while pepsin hydrolysate decreased as the enzyme-substrate ratio increased. The dominant amino acids in A. altilis protein and hydrolysates were glutamate, aspartate and leucine. Protein hydrolysates obtained from pepsin and trypsin digestion had DPPH scavenging abilities of 43.0 ± 0.01% and 22.2 ± 0.01%, respectively. However, trypsin-hydrolysed protein had a high Fe-chelating ability, while pepsin-hydrolysed protein had high hydrogen peroxide scavenging ability. Trypsin-hydrolysed protein showed good membrane stability and inhibition of protein denaturation. The results indicated that A. altilis protein hydrolysates possess significant antioxidant and anti-inflammatory effects and can further lend support to food industries as functional foods.
Topics: Antioxidants; Artocarpus; Protein Hydrolysates; Fruit; Pepsin A; Trypsin; Hydrogen Peroxide; Parkinson Disease; Fabaceae
PubMed: 36707546
DOI: 10.1038/s41598-023-28684-z -
Nutrients Dec 2022The microstructure of legumes plays a crucial role in regulating starch digestion and postprandial glycemic responses. Starch granules are double encapsulated within the...
The microstructure of legumes plays a crucial role in regulating starch digestion and postprandial glycemic responses. Starch granules are double encapsulated within the outer cell wall and the inner protein matrix of legume cotyledon cells. Despite progress in understanding the role of cell walls in delaying starch digestion, the role of the protein matrix has received little research attention. The aim of this study was to evaluate if the protein matrix and cell wall may present combined physical barriers retarding enzyme hydrolysis of intracellular starch. Intact cotyledon cells were isolated from navy beans and used to assess the barrier effect of the protein matrix on the digestion of starch under conditions simulating the upper gastrointestinal tract. The cells were pretreated with pepsin at 37 °C and pH 2.0 for 1, 4, or 24 h and without pepsin for 24 h (control) to facilitate removal of the intracellular protein matrix prior to cooking and simulated in vitro digestion. A longer pretreatment time resulted in a lower protein content of the cells and a higher initial rate and extent of starch hydrolysis. We suggest that in addition to the primary cell wall barrier, the protein matrix provides a secondary barrier restricting the accessibility of α-amylase to starch. This study provides a new fundamental understanding of the relationship between the structural organization of legume cotyledon cells and starch digestion that could inform the design of novel low glycemic index foods.
Topics: Pepsin A; Starch; Cotyledon; Fabaceae; Cooking; Digestion
PubMed: 36615763
DOI: 10.3390/nu15010105 -
Biometals : An International Journal on... Jun 2023This report describes proteolytic fragmentation and clearance of bovine lactoferrin (bLF) upon intravaginal administration in premenopausal women. Tablet formulations...
This report describes proteolytic fragmentation and clearance of bovine lactoferrin (bLF) upon intravaginal administration in premenopausal women. Tablet formulations (MTbLF) containing 300 mg of bLF progressed through three phases: Pre-Dissolution, Dissolution, and Washout, over a 30-h time course. Tablets dissolved slowly, replenishing intact 80 kDa bLF in vaginal fluid (VF) as proteolysis occurred. bLF was initially cleaved approximately in half between its N- and C-lobes, then degraded into sub-fragments and small peptides. The extent of proteolysis was less than 10-20% across multiple subjects. Concentrations of both intact 80 kDa bLF and smaller fragments decreased in VF with a similar time course suggesting washout not proteolysis was the main clearance mechanism. Concentrations of intact and/or nicked 80 kDa bLF peaked between 4 and 8 h after administration and remained above 5 mg/mL for approximately 24 h. Experiments with protease inhibitors in ex vivo VF digests suggested an aspartyl protease was at least partially responsible for bLF cleavage. However, digestion with commercial pepsin or in vivo in the human stomach, demonstrated distinctly different patterns of fragments compared to vaginal proteolysis. Furthermore, the 3.1 kDa antimicrobial peptide lactoferricin B was not detected in VF. This suggests pepsin-like aspartyl proteases are not responsible for vaginal proteolysis of bLF.
Topics: Female; Humans; Lactoferrin; Pepsin A; Proteolysis; Administration, Intravaginal; Vagina
PubMed: 36580179
DOI: 10.1007/s10534-022-00481-7 -
EFSA Journal. European Food Safety... Dec 2022The food enzyme containing chymosin (EC 3.4.23.4) and pepsin A (EC 3.4.23.1) is prepared from the abomasum of suckling goats, lambs and calves by Laboratoires Abia. The...
The food enzyme containing chymosin (EC 3.4.23.4) and pepsin A (EC 3.4.23.1) is prepared from the abomasum of suckling goats, lambs and calves by Laboratoires Abia. The food enzyme is intended to be used in milk processing for cheese production. As no concerns arise from the animal source of the food enzyme or from its manufacture, and based on the history of safe use and consumption, the Panel considered that toxicological data and the estimation of dietary exposure were not required. On the basis of literature data, the Panel considered that, under the intended conditions of use, the risk of allergic reactions by dietary exposure could not be excluded, but the likelihood for this to occur was considered low. Based on the data provided, the Panel concluded that this food enzyme does not give rise to safety concerns under the intended conditions of use.
PubMed: 36474479
DOI: 10.2903/j.efsa.2022.7649 -
Food Chemistry Apr 2023Wheat is the staple crop for 35% of the world's population, providing a major source of calories, mainly in the form of starch. The digestibility of wheat starch varies...
Wheat is the staple crop for 35% of the world's population, providing a major source of calories, mainly in the form of starch. The digestibility of wheat starch varies between different flours and products. Wheat products that are rapidly digested elicit large post-prandial glucose peaks associated with metabolic disorders. We investigated the impact of protein on starch digestion in three commercial flours with different grain hardness. A soluble extract of wheat proteins reduced starch digestion, even following gastric proteolysis. This extract was enriched in proteinaceous α-amylase inhibitors which were partially degraded during gastric proteolysis. Starch digestion kinetic analysis was carried out for flour samples pre-treated with different pepsin activities. The rate of starch digestion was altered following pepsin pre-digestion, and the extent of starch digestion increased in response to pepsin pre-digestion. We conclude that soluble proteinaceous alpha-amylase inhibitors present in wheat can escape gastric digestion and significantly contribute to reducing starch digestion in the small intestine.
Topics: Starch; Flour; Digestion; Hardness; Pepsin A; Triticum; Kinetics; alpha-Amylases; Plant Extracts
PubMed: 36459801
DOI: 10.1016/j.foodchem.2022.135047 -
Nutrients Nov 2022, a food grade bacterium, is extensively used in the manufacture of fermented products such as yogurt and cheeses. It has been shown that strains exhibited varying...
, a food grade bacterium, is extensively used in the manufacture of fermented products such as yogurt and cheeses. It has been shown that strains exhibited varying anti-inflammatory activities in vitro. Our previous study displayed that this activity could be partially due to peptide(s) generated by trypsin hydrolysis of the surface proteins of LMD-9. Surface protease PrtS could be the source of these peptides during gastrointestinal digestion. Therefore, peptide hydrolysates were obtained by shaving two phenotypically distinct strains of (LMD-9 PrtS and CNRZ-21N PrtS) with pepsin, a gastric protease, followed or not by trypsinolysis. The peptide hydrolysates of both strains exhibited anti-inflammatory action through the modulation of pro-inflammatory mediators in LPS-stimulated THP-1 macrophages (COX-2, Pro-IL-1β, IL-1β, and IL-8) and LPS-stimulated HT-29 cells (IL-8). Therefore, peptides released from either PrtS or PrtS strains in the gastrointestinal tract during digestion of a product containing this bacterium may display anti-inflammatory effects and reduce the risk of inflammation-related chronic diseases.
Topics: Streptococcus thermophilus; Interleukin-8; Lipopolysaccharides; Bacterial Proteins; Peptides; Endopeptidases; Peptide Hydrolases; Anti-Inflammatory Agents
PubMed: 36432464
DOI: 10.3390/nu14224777 -
Biosensors Nov 2022Instead of molecularly imprinting a whole protein molecule, imprinting protein epitopes is gaining popularity due to cost and solubility issues. Belonging to the matrix...
Instead of molecularly imprinting a whole protein molecule, imprinting protein epitopes is gaining popularity due to cost and solubility issues. Belonging to the matrix metalloproteinase protein family, MMP-1 is an interstitial collagenase that degrades collagen and may be involved in cell migration, cell proliferation, the pro-inflammatory effect, and cancer progression. Hence, it can serve as a disease protein biomarker and thus be useful in early diagnosis. Herein, epitopes of MMP-1 were identified by screening its crystal structure. To identify possible epitopes for imprinting, MMP-1 was cleaved in silico with trypsin, pepsin at pH = 1.3, and pepsin at pH > 2.0 using Peptide Cutter, generating peptide fragments containing 8 to 12 amino acids. Five criteria were applied to select the peptides most suitable as potential epitopes for MMP-1. The triphenylamine rhodanine-3-acetic acid (TPARA) functional monomer was synthesized to form a stable pre-polymerization complex with a selected template epitope. The complexed functional monomer was then copolymerized with 3,4-ethoxylenedioxythiophene (EDOT) using potentiodynamic electropolymerization onto indium−tin−oxide (ITO) electrodes. The composition of the molecularly imprinted poly(TPARA-co-EDOT) (MIP) was optimized by maximizing the film’s electrical conductivity. Cyclic voltammetry was used to determine MMP-1 concentration in the presence of the Fe(CN)63−/Fe(CN)64− redox probe actuating the “gate effect.” A calibration curve was constructed and used to determine the usable concentration range and the limit of detection as ca. 0.001 to 10.0 pg/mL and 0.2 fg/mL MMP-1, respectively. Finally, the MMP-1 concentration in the A549 human lung (carcinoma) culture medium was measured, and this determination accuracy was confirmed using an ELISA assay.
Topics: Humans; Molecular Imprinting; Matrix Metalloproteinase 1; Epitopes; Polymers; Pepsin A; Peptides; Poly A
PubMed: 36421137
DOI: 10.3390/bios12111018