The Profound Stimulatory Impact of Gastrin on Gastric Mucus Production in Helicobacter pylori-Negative Asymptomatic Volunteers

2005 ◽  
Vol 100 ◽  
pp. S69
Author(s):  
Tomasz Skoczylas ◽  
Irene Sarosiek ◽  
Katherine Roeser ◽  
Grzegorz Wallner ◽  
Jerzy Sarosiek
Nutrients ◽  
2020 ◽  
Vol 12 (10) ◽  
pp. 2951
Author(s):  
Marcio A. A. de Mendonça ◽  
Ana R. S. Ribeiro ◽  
Adriana K. de Lima ◽  
Gislaine B. Bezerra ◽  
Malone S. Pinheiro ◽  
...  

Propolis has various pharmacological properties of clinical interest, and is also considered a functional food. In particular, hydroalcoholic extracts of red propolis (HERP), together with its isoflavonoid formononetin, have recognized antioxidant and anti-inflammatory properties, with known added value against dyslipidemia. In this study, we report the gastroprotective effects of HERP (50–500 mg/kg, p.o.) and formononetin (10 mg/kg, p.o.) in ethanol and non-steroidal anti-inflammatory drug-induced models of rat ulcer. The volume, pH, and total acidity were the evaluated gastric secretion parameters using the pylorus ligature model, together with the assessment of gastric mucus contents. The anti-Helicobacter pylori activities of HERP were evaluated using the agar-well diffusion method. In our experiments, HERP (250 and 500 mg/kg) and formononetin (10 mg/kg) reduced (p < 0.001) total lesion areas in the ethanol-induced rat ulcer model, and reduced (p < 0.05) ulcer indices in the indomethacin-induced rat ulcer model. Administration of HERP and formononetin to pylorus ligature models significantly decreased (p < 0.01) gastric secretion volumes and increased (p < 0.05) mucus production. We have also shown the antioxidant and anti-Helicobacter pylori activities of HERP. The obtained results indicate that HERP and formononetin are gastroprotective in acute ulcer models, suggesting a prominent role of formononetin in the effects of HERP.


1962 ◽  
Vol 203 (3) ◽  
pp. 553-556 ◽  
Author(s):  
Sherwin Mizell

The production of gastric mucus in vitro by Rana pipiens was studied using histamine stimulation. The frogs were kept at a constant temperature (21 C) both prior to and during experimentation. Quantitative determinations of mucoproteose, mucoprotein, and mucoid of the visible mucus were performed over a 13-month period, utilizing 340 animals in terminal experiments. Mucoproteose constituted one-half of frog gastric mucus, the rest being divided almost equally between mucoprotein and mucoid. No significant differences in this ratio or in the total amount of gastric mucus could be attributed to the change of seasons or to the addition of glucose or inosine triphosphate as substrates. A statistically significant negative correlation exists between both total mucus and mucoproteose and total acid produced. The mucoproteose fraction of gastric mucus may contain the inhibitor found by other investigators in human gastric juice. However, until further information is available on its physiological significance in situ, gastric mucus cannot be considered responsible for the seasonal variation of gastric HCI secretion in Rana pipiens.


Biomaterials ◽  
2017 ◽  
Vol 138 ◽  
pp. 1-12 ◽  
Author(s):  
Rita S. Santos ◽  
George R. Dakwar ◽  
Elisa Zagato ◽  
Toon Brans ◽  
Céu Figueiredo ◽  
...  

1997 ◽  
Vol 25 (2) ◽  
pp. 372S-372S ◽  
Author(s):  
LINDSEY OLIVER ◽  
JULIA L NEWTON ◽  
NICOLA JORDAN ◽  
PAUL GODDARD ◽  
PETER DETTMAR ◽  
...  

Gut ◽  
1998 ◽  
Vol 43 (4) ◽  
pp. 470-475 ◽  
Author(s):  
J L Newton ◽  
N Jordan ◽  
L Oliver ◽  
V Strugala ◽  
J Pearson ◽  
...  

Background—It has been proposed that a pathogenic effect of Helicobacter pylori is a weakening of the protective mucus barrier; however, this remains controversial.Aims—To clarify the effects of H pylori infection on the mucus gel barrier in vivo.Methods—Mucus gel polymeric structure and the thickness of the adherent mucus barrier were measured in endoscopic biopsy samples in subjects with and without H pyloriinfection.Results—There was a significant 18% reduction in the proportion of polymeric gel forming mucin in the adherent mucus layer in H pylori positive compared with negative subjects. There was no change in the adherent mucus thickness betweenH pylori positive and negative subjects without gastric atrophy (mean (SD): 104 (26) μm, 106 (30) μm respectively). There was however a significant reduction in mucus thickness in those H pylori positive subjects with underlying gastric atrophy (84 (13) μm, p=0.03) compared with those without atrophy.Conclusions—A partial breakdown in gel forming structure of the gastric mucus barrier does occur in H pylori infection per se but this is insufficient to cause a collapse of the mucus barrier.


2004 ◽  
Vol 101 (14) ◽  
pp. 5024-5029 ◽  
Author(s):  
S. Schreiber ◽  
M. Konradt ◽  
C. Groll ◽  
P. Scheid ◽  
G. Hanauer ◽  
...  

Gut ◽  
1995 ◽  
Vol 37 (4) ◽  
pp. 589-590
Author(s):  
B L Slomiany ◽  
A Slomiany ◽  
V L Murty ◽  
J Piotrowski

2019 ◽  
Vol 20 (18) ◽  
pp. 4400 ◽  
Author(s):  
Marguerite Clyne ◽  
Felicity E. B. May

Helicobacter pylori colonises the human stomach and has tropism for the gastric mucin, MUC5AC. The majority of organisms live in the adherent mucus layer within their preferred location, close to the epithelial surface where the pH is near neutral. Trefoil factor 1 (TFF1) is a small trefoil protein co-expressed with the gastric mucin MUC5AC in surface foveolar cells and co-secreted with MUC5AC into gastric mucus. Helicobacter pylori binds with greater avidity to TFF1 dimer, which is present in gastric mucus, than to TFF1 monomer. Binding of H. pylori to TFF1 is mediated by the core oligosaccharide subunit of H. pylori lipopolysaccharide at pH 5.0–6.0. Treatment of H. pylori lipopolysaccharide with mannosidase or glucosidase inhibits its interaction with TFF1. Both TFF1 and H. pylori have a propensity for binding to mucins with terminal non-reducing α- or β-linked N-acetyl-d-glucosamine or α-(2,3) linked sialic acid or Gal-3-SO42−. These findings are strong evidence that TFF1 has carbohydrate-binding properties that may involve a conserved patch of aromatic hydrophobic residues on the surface of its trefoil domain. The pH-dependent lectin properties of TFF1 may serve to locate H. pylori deep in the gastric mucus layer close to the epithelium rather than at the epithelial surface. This restricted localisation could limit the interaction of H. pylori with epithelial cells and the subsequent host signalling events that promote inflammation.


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