Immobilisation and activity of human α-amylase in the acquired enamel pellicle

Hannig, Christian; Attin, Thomas; Hannig, Matthias; Henze, Elvira; Brinkmann, Kirsten; Zech, Ronald

doi:10.1016/j.archoralbio.2004.01.005

Cited by 58 publications

(93 citation statements)

References 26 publications

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“…Considering the fold change of 1.5 [Aragão et al, 2012a;Paes Leme et al, 2012], amylase has similar abundance among the samples and it was identified in a notable manner with the highest spectral counts, which means a high abundance of this protein in the acquired enamel pellicle independently of the enamel pretreatment. This result is consistent with earlier findings that indicated that amylase is one of the major components of pellicle [Hannig et al, 2004[Hannig et al, , 2005Siqueira et al, 2012b]. However, the enamel surface modifications showed an effect in the quantity of some proteins, such as histatin-1, a recognized pellicle precursor that was found to be present in low abundance in enamel pellicle from slabs pretreated with APF.…”

Section: Resultssupporting

confidence: 82%

Acidulated Phosphate Fluoride Application Changes the Protein Composition of Human Acquired Enamel Pellicle

et al. 2013

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We evaluated, by proteomic analysis, whether the chemical changes provoked on enamel by acidulated phosphate fluoride (APF) application alter the protein composition of acquired enamel pellicle. Enamel slabs, pretreated with distilled water (negative control), phosphoric acid (active control) or APF solution, were immersed in human saliva for pellicle formation. The adsorbed proteins were extracted and analyzed by liquid chromatography-mass spectrometry/mass spectrometry. Fifty-six proteins were identified, 12 exclusive to APF and 11 to phosphoric acid. APF decreased the concentration of histatin-1, but increased the concentration of S100-A9, which is confirmed by immunoblotting. The findings suggest that APF application changes the acquired enamel pellicle composition.

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Section: Resultssupporting

confidence: 82%

Acidulated Phosphate Fluoride Application Changes the Protein Composition of Human Acquired Enamel Pellicle

et al. 2013

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“…It is known that the action of this enzyme is essential for starch to be metabolized by bacteria present in biofilms, 13 mainly S. mutans, which do not have amylolytic activity. 22 This enzyme is found in acquired pellicle 23 and in biofilm matrix.…”

Section: Discussionmentioning

confidence: 99%

Enamel and dentine demineralization by a combination of starch and sucrose in a biofilm – caries model

et al. 2016

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Sucrose is the most cariogenic dietary carbohydrate and starch is considered non-cariogenic for enamel and moderately cariogenic for dentine. However, the cariogenicity of the combination of starch and sucrose remains unclear. The aim of this study was to evaluate the effect of this combination on Streptococcus mutans biofilm composition and enamel and dentine demineralization. Biofilms of S. mutans UA159 were grown on saliva-coated enamel and dentine slabs in culture medium containing 10% saliva. They were exposed (8 times/day) to one of the following treatments: 0.9% NaCl (negative control), 1% starch, 10% sucrose, or 1% starch and 10% sucrose (starch + sucrose). To simulate the effect of human salivary amylase on the starch metabolization, the biofilms were pretreated with saliva before each treatment and saliva was also added to the culture medium. Acidogenicity of the biofilm was estimated by evaluating (2 times/day) the culture medium pH. After 4 (dentine) or 5 (enamel) days of growth, biofilms (n = 9) were individually collected, and the biomass, viable microorganism count, and polysaccharide content were quantified. Dentine and enamel demineralization was assessed by determining the percentage of surface hardness loss. Biofilms exposed to starch + sucrose were more acidogenic and caused higher demineralization (p < 0.0001) on either enamel or dentine than those exposed to each carbohydrate alone. The findings suggest that starch increases the cariogenic potential of sucrose.

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“…The activities of α-amylase [Morishita et al, 2000;Hannig et al, 2004], GTF [Hannig et al, 2008a], lysozyme [Maeda, 1980;Vray et al, 1980;, and peroxidase [Proctor and Chan, 1994;Hannig et al, 2008b] in the in situ formed pellicles were determined as described previously and were calculated per square centimeter of enamel surface .…”

Section: Enzyme Activities Of the In Situ Formed Pellicle Layermentioning

confidence: 99%

“…Host enzymes with protective properties are lysozyme and peroxidase; α-amylase and glycosyltransferase (GTF) facilitate the binding of microorganisms to the pellicle layer. They can all be found immobilized in the initial in situ pellicle in an active conformation [Deimling et al, 2004;Hannig et al, 2004Hannig et al, , 2008b. The enzyme activity of the pellicle enzymes might be related to the caries activity.…”

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confidence: 99%

Enzymology and Ultrastructure of the in situ Pellicle in Caries-Active and Caries-Inactive Patients

et al. 2017

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Aim: The present study aimed to evaluate the impact of caries activity on the key enzymes and the ultrastructure of the in situ pellicle. Methods: Pellicle formation was performed on bovine enamel slabs. Intraoral exposure (3, 30, and 120 min) was accomplished by 14 caries-active (DMFS: 22.7 ± 12.1) and 13 caries-inactive (DMFS: 1.5 ± 1.8) individuals. The enzyme activities (lysozyme, peroxidase, α-amylase, glycosyltransferase [GTF]) in the in situ pellicle and resting saliva of all participants were analyzed directly after oral exposure. In addition, a simultaneous visualization of these enzymes, extracellular glucans, and adherent bacteria was carried out. Fluorescent patterns were analyzed with fluorescence labeling and 4′,6-diamidino-2-phenylindole/concanavalin A staining. In addition, the distribution of GTF B, C, and D and the ultrastructure of the pellicle were examined by gold immunolabeling and transmission electron microscopy with selected samples. Results: Enzyme activities of amylase, peroxidase, lysozyme, and GTF were detected on all enamel slabs in an active conformation. Neither exposure time nor caries activity had an impact on the enzyme activities. Gold immunolabeling indicated that the pellicle of caries-active subjects tends to more GTF D molecules. The pellicles of caries-inactive and -active individuals revealed a similar ultrastructural pattern. Conclusion: The enzyme activities as well as the pellicle's ultrastructure are of high similarity in caries-active and -inactive subjects. Thereby, oral exposure time has no significant influence. This reflects a high uniformity during the initial phase of bioadhesion (3-120 min) concerning enzymatic functions. However, there is a tendency towards more GTF D in caries-active individuals.

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Immobilisation and activity of human α-amylase in the acquired enamel pellicle

Cited by 58 publications

References 26 publications

Acidulated Phosphate Fluoride Application Changes the Protein Composition of Human Acquired Enamel Pellicle

Acidulated Phosphate Fluoride Application Changes the Protein Composition of Human Acquired Enamel Pellicle

Enamel and dentine demineralization by a combination of starch and sucrose in a biofilm – caries model

Enzymology and Ultrastructure of the in situ Pellicle in Caries-Active and Caries-Inactive Patients

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