muramidase and Tooth-Erosion

To assess the effect of protein-containing toothpastes on the progression of dental erosion in situ (with pellicle) and in vitro (without pellicle).. A combined split-mouth (extraoral water or toothpaste brushing) and crossover (type of toothpaste) setup was used. Two protein-containing (high/low concentrations of colostrum) and one nonprotein (placebo) toothpaste were investigated. Sixteen volunteers wore intraoral appliances containing 2 human enamel samples on 3 afternoons for pellicle growth during 90 min. One enamel sample was brushed for 5 s with one of the three toothpastes and subsequently exposed to a slurry of the corresponding toothpaste for 2 min. The other sample was exposed to water. Both samples were subsequently exposed to citric acid (extraorally). Loss of calcium and inorganic phosphate were determined. The same sequence of exposures was applied to 16 enamel samples in an in vitro setup without pellicle.. With the in situ-formed pellicle, all toothpastes significantly reduced calcium loss compared to water brushing, although no significant differences were found among toothpastes (p = 0.073). For the loss of phosphate, a significant reduction could be found with the use of the high-protein toothpaste compared to the nonprotein toothpaste. Overall there were only slight differences between the toothpastes. Toothpaste effects were less clear in the in vitro experiment.. The addition of proteins to toothpaste shows some promise for the prevention of erosion. Further research is needed to investigate the performance of the protein-containing toothpastes in longer in situ studies with regard to erosive wear.

Topics: Calcium; Caseins; Citric Acid; Cross-Over Studies; Dental Enamel; Dental Pellicle; Disease Progression; Double-Blind Method; Glucan 1,4-alpha-Glucosidase; Glucose Oxidase; Humans; Hydrogen-Ion Concentration; Immunoglobulin G; Lactoferrin; Lactoperoxidase; Muramidase; Phosphates; Placebos; Proteins; Tooth Erosion; Toothpastes; Water

This electron microscopic study aimed at investigating effects of oral astringent stimuli on the enamel pellicle's morphology.. Pellicles were formed in situ within 30min on bovine enamel slabs, fixed to individuals' upper jaw splints. The pellicle-coated specimens were immersed in vitro in seven diverse astringent solutions and subsequently analyzed by scanning electron microscopy (SEM), energy dispersive X-ray (EDX) spectroscopy, as well as transmission electron microscopy (TEM). Four biocompatible astringents, namely the polyphenol epigallocatechin gallate, the metal salt iron(III) sulfate, the basic protein lysozyme, and the aminopolysaccharide chitosan, were additionally applied in situ. After rinsing the oral cavity with these compounds, the pellicle's ultrastructure was imaged by SEM and TEM, respectively. Untreated pellicle samples served as controls.. Exposure to polyphenols and lysozyme induced particularly thicker and electron-denser pellicles in comparison to the control pellicle with similar characteristics in vitro and in situ. In contrast, acidic chitosan and metal salt solutions, respectively, revealed minor pellicle alterations. The incorporation of Fe and Al into the pellicles treated with the corresponding inorganic salts was verified by EDX analysis.. Astringent-induced pellicle modifications were for the first time visualized by TEM. The ultrastructural alterations of the dental pellicle may partly explain the tooth-roughening effect caused by oral astringent stimuli.. Astringents might modify the pellicle's protective properties against dental erosion, attrition, as well as bacterial adhesion, and by this means may influence tooth health. The findings may thus be particularly relevant for preventive dentistry.

Topics: Adult; Aluminum Chloride; Aluminum Compounds; Animals; Astringents; Bacterial Adhesion; Catechin; Cattle; Chitosan; Chlorides; Dental Enamel; Dental Pellicle; Ferric Compounds; Humans; Materials Testing; Microscopy, Electron, Scanning; Microscopy, Electron, Transmission; Mouth; Muramidase; Polyphenols; Preventive Dentistry; Salivary Proteins and Peptides; Spectrometry, X-Ray Emission; Surface Properties; Time Factors; Tooth Attrition; Tooth Erosion

To investigate the effect of saliva substitutes on enamel erosion in vitro.. A total of 204 bovine enamel samples were embedded in acrylic resin and allocated to 17 groups (n=12). The specimens were eroded in an artificial mouth (3 days; 6×30 s/days, flow rate: 2 ml/min) using citric acid (pH: 2.5). Immediately after the erosive attacks, saliva substitutes (12 sprays, 3 gels) were applied. Between the erosive cycles the specimens were rinsed with artificial saliva (flowrate: 0.5 ml/min). A SnCl2/AmF/NaF-containing mouthrinse was used as positive control, water spray served as negative control. Enamel loss was measured profilometrically and the data were analyzed using one-way ANOVA followed by Scheffé's post hoc tests (p<0.05).. Four saliva substitutes increased enamel erosion, probably due to the low pH or the content of citric acid. Several saliva substitutes were able to reduce enamel erosion significantly by 60-90% (in the range of the positive control). The protective potential of these products was in the range of the positive control (reduction of enamel loss to 30% of negative control). The erosion-protective potential of these high-viscous products is probably related to their film-forming properties, leading to a mechanical protection of the surface.. Saliva substitutes containing a very low pH exhibit a distinct erosive potential, while most high-viscous products present an erosion-protective effect. It can be recommended that patients suffering from xerostomia and at high risk for dental erosion should use high-viscous saliva substitutes, but should avoid saliva substitutes with low pH or containing citric acid.. It can be recommended that patients suffering from xerostomia and at high risk for dental erosion should use high-viscous saliva substitutes, but should avoid saliva substitutes with low pH or containing citric acid.

Topics: Aerosols; Animals; Cattle; Cellulose; Citric Acid; Dental Enamel; Diamines; Drug Combinations; Fluorides; Gels; Glucose Oxidase; Hydrogen-Ion Concentration; Lactoperoxidase; Materials Testing; Mouthwashes; Muramidase; Protective Agents; Saliva, Artificial; Sodium Fluoride; Tin Compounds; Tooth Demineralization; Tooth Erosion; Tooth Remineralization; Viscosity

Patients with bulimia nervosa are at high risk for dental erosion. However, not all bulimic patients suffer from erosion, irrespective of the severity of their eating disorder. It is often speculated that differences in the saliva are important, however, little is known about salivary parameters in bulimic patients, particularly directly after vomiting. The aim of the clinical trial was to compare different salivary parameters of subjects suffering from bulimia with those of healthy controls. Twenty-eight subjects participated (14 patients with bulimia nervosa, 7 of them with erosion; 14 matched healthy controls). Resting and stimulated saliva of all participants was analysed as well as saliva collected from bulimic patients directly and 30 min after vomiting. Parameters under investigation were flow rate, pH, buffering capacity and the enzyme activities of proteases in general, collagenase, pepsin, trypsin, amylase, peroxidase, and lysozyme. Regarding flow rate, pH and buffering capacity only small differences were found between groups; buffering capacity directly after vomiting was significantly lower in bulimic subjects with erosion than in subjects without erosion. Differences in enzymatic activities were more pronounced. Activities of proteases, collagenase and pepsin in resting and proteases in stimulated saliva were significantly higher in bulimic participants with erosion than in controls. Peroxidase activity was significantly decreased by regular vomiting. Proteolytic enzymes seem to be relevant for the initiation and progression of dental erosion directly after vomiting, maybe by both hydrolysis of demineralized dentine structures as well as modulation of the pellicle layer.

Topics: Adult; Amylases; Analysis of Variance; Buffers; Bulimia Nervosa; Case-Control Studies; Collagenases; Female; Humans; Hydrogen-Ion Concentration; Male; Muramidase; Pepsin A; Peptide Hydrolases; Peroxidase; Proteolysis; Saliva; Secretory Rate; Statistics, Nonparametric; Tooth Erosion; Trypsin; Vomiting

The aim of this study was to quantify the buffer attributes (value, power, range and optimum) of two model systems for whole human resting saliva, the purified proteins from whole human resting saliva and single proteins. Two model systems, the first containing amyloglucosidase and lysozyme, and the second containing amyloglucosidase and alpha-amylase, were shown to provide, in combination with hydrogencarbonate and di-hydrogenphosphate, almost identical buffer attributes as whole human resting saliva. It was further demonstrated that changes in the protein concentration as small as 0.1% may change the buffer value of a buffer solution up to 15 times. Additionally, it was shown that there was a protein concentration change in the same range (0.16%) between saliva samples collected at the time periods of 13:00 and others collected at 9:00 am and 17:00. The mode of the protein expression changed between these samples corresponded to the change in basic buffer power and the change of the buffer value at pH 6.7. Finally, SDS Page and Ruthenium II tris (bathophenantroline disulfonate) staining unveiled a constant protein expression in all samples except for one 50 kDa protein band. As the change in the expression pattern of that 50 kDa protein band corresponded to the change in basic buffer power and the buffer value at pH 6.7, it was reasonable to conclude that this 50 kDa protein band may contain the protein(s) belonging to the protein buffer system of human saliva.

Topics: Adult; Animals; Aspergillus niger; Bicarbonates; Buffers; Chickens; Circadian Rhythm; Electrophoresis, Polyacrylamide Gel; Fungal Proteins; Glucan 1,4-alpha-Glucosidase; Humans; Hydrogen-Ion Concentration; Male; Middle Aged; Muramidase; Phosphoric Acids; Saliva; Salivary alpha-Amylases; Salivary Proteins and Peptides; Species Specificity; Swine; Tooth Erosion