- Authors
- Jasmin Kirsch Technische Universität Dresden, Clinic of Operative and Pediatric Dentistry, Medical Faculty Carl Gustav Carus, Dresden
- Sandra PötschkeTechnische Universität Dresden, Clinic of Operative and Pediatric Dentistry, Medical Faculty Carl Gustav Carus, Dresden
- Sabine BascheTechnische Universität Dresden, Clinic of Operative and Pediatric Dentistry, Medical Faculty Carl Gustav Carus, Dresden
- Christian Hannig
- William H. Bowen
- Matthias Hannig
- Stefan Rupf
- Simone Trautmann
- Natalia Umanskaya
- title
- Enzymology and Ultrastructure of the in situ Pellicle in Caries-Active and Caries-Inactive Patients
- Please use the following URL when quoting:
- https://nbn-resolving.org/urn:nbn:de:bsz:14-qucosa2-706118
- original0000000000000
- Caries Research
Erscheinungsjahr: 2017
Jahrgang: 51
Heft: 2
Seiten: 109-118
ISSN: 0008-6568
E-ISSN: 1421-976X - publication_date
- 2017
- Abstract (EN)
- 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 cariesactive 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.
- otherVersion00000
- Link zum Artikel der zuerst in der Zeitschrift 'Caries research' erschienen ist
DOI: 10.1159/000452226 - Keywords (DE)
- Amylase, Kariesaktivität, Glykosyltransferase, Lysozym, Peroxidase, Speichelhäutchen, Transmissionselektronenmikroskopie
- Keywords (EN)
- Amylase, Caries activity, Glycosyltransferase, Lysozyme, Peroxidase, Salivary pellicle, Transmission electron microscopy
- Classification (DDC)
- 610
- Publishing house
- Karger, Basel
- Project sponsoring
- Deutsche Forschungsgemeinschaft (DFG)
SFB 1027: Physikalische Modellierung von Nichtgleichgewichtsprozessen in biologischen Systemen
ID: 200049484
Deutsche Forschungsgemeinschaft (DFG)
ID: HA 5192/7-1
Deutsche Forschungsgemeinschaft (DFG)
ID: HA 2718/11-1
Deutsche Forschungsgemeinschaft (DFG)
ID: RU 866/2-1 - version
- publizierte Version / Verlagsversion
- URN Qucosa
- urn:nbn:de:bsz:14-qucosa2-706118
- Qucosa date of publication
- 22.05.2020
- Document type
- article
- Document language
- English
- licence