• Journal of Oral Medicine and Pain
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• v.32 no.4
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• pp.365-373
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• 2007

Destruction of oral soft and hard tissues and resulting problems seriously affect the life quality of xerostomic patients. Although artificial saliva is the only regimen for xerostomic patients with totally abolished salivary glands, currently available artificial salivas give restricted satisfaction to patients. The purpose of this study was to contribute to the development of ideal artificial saliva through comparing viscosity and wettability between CMC solutions and human saliva. Commercially-available CMC is dissolved in simulated salivary buffer (SSB) and distilled deionized water (DDW). Various properties of human whole saliva, human glandular saliva, and a CMC-based saliva substitutes known as Salivart and Moi-Stir were compared with those of CMC solutions. Viscosity was measured with a cone-and-plate digital viscometer at six different shear rates, while wettability on acrylic resin and Co-Cr alloy was determined by the contact angle. The obtained results were as follows: 1. The viscosity of CMC solutions was proportional to CMC concentration, with 0.5% CMC solution displaying similar viscosity to stimulated whole saliva. Where as a decrease in contact angle was found with increasing CMC concentration. 2. The viscosity of human saliva was found to be inversely proportional to shear rate, a non-Newtonian (pseudoplastic) trait of biological fluids. The mean viscosity values at various shear rates increased as follows: stimulated parotid saliva, stimulated whole saliva, unstimulated whole saliva, stimulated submandibular-sublingual saliva. 3. Contact angles of human saliva on the tested solid phases were inversely correlated with viscosity, namely decreasing in the order stimulated parotid saliva, stimulated whole saliva, unstimulated whole saliva, stimulated submandibular-sublingual saliva. 4. Boiled CMC dissolved in SSB (CMC-SSB) had a lower viscosity than CMC-SSB (P < 0.01 at shear rate of $90s^{-1}$). 5. For human saliva, contact angles on acrylic resin were significantly lower than those on Co-Cr alloy (P < 0.01). 6. Comparing CMC solutions with human saliva, the contact angles between acrylic resin and human saliva solutions were significantly lower than those between acrylic resin and CMC solutions, including Salivart and Moi-Stir (P <0.01). The effectiveness of CMC solutions in terms of their rheological properties was objectively confirmed, indicating a vital role for CMC in the development of effective salivary substitutes.

• Journal of the korean academy of Pediatric Dentistry
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• v.28 no.3
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• pp.447-463
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• 2001

Dendroaspis natriuretic peptide (DNP), a fourth member of the natriuretic peptide isolated from the venom of the Dendroaspis angusticeps snake, has been reported to be present in human plasma and atrial myocardium and caused vasorelaxation and diuresis in experimental animals. However, it is uncertain whether they are present in peripheral organs other than the heart and its further physiological roles also remains to be clarified. To assess the possible physiological role of DNP in the salivary glands, I investigated the localization of DNP peptide in the rat salivary glands by immunohistochemistry and the binding sites for radiolabelled DNP in the rat salivary glands and oral mucosa using in vitro autoradiography. DNP immunoreactivity was widely distributed in the submandibular, sublingual and parotid glands, particularly in the ducts such as the intercalated and striated ducts, where atrial natriuretic peptide (ANP) was colocalized in consecutive sections, but not in acini. High density $^{125}I-DNP$ binding sites were localized in the epithelia of the tongue and hard palate, while low density binding sites for $^{125}I-DNP$ were also distributed in the submandibular, sublingual, and parotid glands. In the hard palate and tongue, the precise location of this binding was revealed on the basal and parabasal cells of the epithelia by emulsion microautoradiography. These results suggest that DNP may not only have a role in the salivary glands but also play a role in the regulation of growth in the oral epithelium, particularly in the hard palate and tongue.

• Journal of the korean academy of Pediatric Dentistry
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• v.50 no.1
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• pp.1-12
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• 2023

Function of salivary gland and saliva composition can be an indicator of individual's health status. Recently, saliva has been thought to have a high potential for usage in the biomedical field to diagnose, evaluate, and prevent systemic health due to the technological advances in analyzing and detecting small elements such as immunological and metabolic products, viruses, microorganisms, hormones in saliva. As a diagnostic specimen, saliva has some useful advantages compared to serum. Because of simple non-invasive method, saliva sampling is quite comfort for the patient, and it doesn't require specialists to collect samples. The possibility of infection during the collection process is also low. For this reason, proteins, genetic materials, and various biomarkers in saliva are actively being utilized on studying stress, microbiomics, genetics, and epigenetics. For the research on collecting big data related to systemic health, the needs on biobank has been focused. Regeneration of salivary gland based on tissue engineering has been also on advancement. However, there are still many issues to be solved, such as the standardization of sample collection, storage, and usage. This review focuses on the recent trends in the field of saliva research and highlight the future perspectives in biomedical and other applications.

• The korean journal of orthodontics
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• v.32 no.6 s.95
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• pp.443-453
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• 2002

The principal aims of this study were to identify the composition of salivary pellicles formed on various orthodontic brackets and to obtain a detailed information about the protein adsorption profiles from whole saliva and two major glandular salivas. Four different types of orthodontic brackets were used. All were upper bicuspid brackets with a $022{\times}028$ slot Roth prescription; stainless steel metal, monocrystalline sapphire, polycrystalline alumina, and plastic brackets. Bracket pelicles were formed by the incubation of orthodontic brackets with whole saliva, submandibular-sublingual saliva, and parotid saliva for 2 hours. The bracket pellicles were extracted and confirmed by employing sodium dodecyl sulfatepolyacrylamide gel electrophoresis, Western transfer methods, and immunodetection. The results showed that low-molecular weight salivary mucin, ${\alpha}-amylase$, secretory IgA (sIgA), acidic proline-rich proteins, and cystatins were attached to all of these brackets regardless of the bracket types. High-molecular weight mucin, which promotes the adhesion of Streptococcus mutans, did not adhere to uy orthodontic brackets. Though the same components were detected in all bracket pellicles, however, the gel profiles showed qualitatively and quantitatively different pellicles, according to the origins of saliva and the bracket types. In particular, the binding of sIgA was more prominent in the pellicles from parotid saliva and the binding of cystatins was prominent in the pellicles from the form plastic brackets. This study indicates that numerous salivary proteins adhere to the orthodontic brackets and these salivary proteins adhere selectively according to bracket types and the types of the saliva.

• Journal of Oral Medicine and Pain
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• v.30 no.1
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• pp.15-23
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• 2005

Mucin glycoproteins are the primary carriers of the oligosaccharide moieties that constitute the blood group substances in human saliva. The aim of this study was to determine whether or not the conversion of either the A or B blood group antigens to the H antigen can occur during the degradation process of stored saliva samples. Forty subjects (20 subjects in each A and B blood group) identified as secretors were enrolled in this study. Fresh whole saliva samples and their clarified supernatants were stored at room temperature for 1 week. The conversion of the blood group antigens was detected by SDS-PAGE and immunoblotting. Among the subjects showing the conversion in whole saliva, glandular saliva samples were obtained from 8 subjects (4 subjects in each A and B blood group). Submandibular-sublingual saliva (SMSL) and a mixture of SMSL and parotid saliva (PS) were stored at room temperature for 1 week. The conversion of the blood group antigens was detected by the same method. The obtained results were as follows: 1. In the clarified samples of whole saliva, the A antigen was detected as being either intact (5%) or degraded molecules (95%) after the 1 week period. Conversion of the A antigen to the H antigen was detected in 5 subjects (25%). In the unclarified samples, the A antigen was either detected as degraded molecules (90%) or was not detected (10%). Conversion of the antigen had occurred in 4 subjects (20%). 2. In the clarified samples of whole saliva, the B antigen was detected as intact (20%) or as degraded molecules (65%) or was not detected (15%) after the 1 week period. Conversion of the B antigen to the H antigen was detected in 7 subjects (35%). In the unclarified samples, the B antigen was detected as intact (5%) or as degraded molecules (65%), or was not detected (30%). Conversion of the antigen was observed in 2 subjects (10%). 3. In the glandular saliva samples, only one of the four subjects displayed an antigenic conversion from the A to H antigen or from the B to H antigen. The conversion had occurred in both the SMSL samples and the SMSL and PS mixture. No degradation of the antigens was detected in the other three samples of the A or B blood groups, nor was there any conversion. The results demonstrated that conversion of the blood group antigens could occur in saliva, and suggested that the enzymes responsible for the conversion are present in saliva. Further studies on the origin and activity of the specific glycosidases in saliva as well as quantitative measurements of the antigenic conversion will be needed.

• The Journal of the Korean dental association
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• v.24 no.12 s.211
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• pp.990-990
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• 1986

• The Journal of the Korean dental association
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• v.18 no.8 s.137
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• pp.629-632
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• 1980

• Proceedings of the Malacological Society of Korea Conference
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• 1999.11a
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• pp.11-11
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• 1999

• The Journal of the Korean dental association
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• v.24 no.2 s.201
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• pp.153-159
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• 1986

• The Journal of the Korean dental association
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• v.18 no.2 s.131
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• pp.87-90
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• 1980