Comparison of protein profiles of the pellicle, gingival crevicular fluid, and saliva: possible origin of pellicle proteins

• Published in: Biological research Vol. 53; no. 1; p. 3
• Main Authors: Odanaka, Hibiki, Obama, Takashi, Sawada, Naoko, Sugano, Marika, Itabe, Hiroyuki, Yamamoto, Matsuo
• Format: Journal Article
• Language: English; Portuguese
• Published: England BioMed Central Ltd 15.01.2020; BioMed Central; Sociedad de Biología de Chile; BMC
• Subjects: Adult; Amylases; BIOLOGY; Blotting, Western; Comparative analysis; Cystatins; Dental enamel; Dental Pellicle - chemistry; Electrophoresis, Polyacrylamide Gel; Enamel; Female; Gel electrophoresis; Gingiva; Gingival crevicular fluid; Gingival Crevicular Fluid - chemistry; Humans; Isobaric tag labeling; Male; Mass Spectrometry; Mass spectroscopy; Musical groups; Nitrogen; Parotid gland; Pellicle; Production increases; Proteins; Proteins - analysis; Proteome; Saliva; Saliva - chemistry; Scientific imaging; Serotransferrin; Sodium lauryl sulfate; Spectroscopy; Teeth; α-Amylase; United States > US; Japan; Alpha-amylase; Cystatin; Isobaric tag labeling; Serotransferrin; Pellicle; Proteome; Saliva; Gingival crevicular fluid
• ISSN: 0717-6287; 0716-9760; 0717-6287
• DOI: 10.1186/s40659-020-0271-2

The pellicle, the acellular organic material deposited on the surface of tooth enamel, has been thought to be derived from saliva. In this study, protein compositions of the pellicle, gingival crevicular fluid, and saliva collected from healthy adults were compared to elucidate the origin of pellicle proteins. The pellicle, gingival crevicular fluid, and saliva from the parotid gland or mixed gland were collected; subsequently, protein expression in samples from the respective individual was compared by SDS-PAGE and mass spectrometry. Following SDS-PAGE, proteins in the major bands were identified by mass spectrometry. The band pattern of pellicle proteins appeared different from those of gingival crevicular fluid, or saliva samples. Using mass spectrometry, 13 proteins in these samples were identified. The relative abundance of the proteins was quantitatively analyzed using mass spectrometry coupled with stable isotope labeling and by western blot. Cystatin S and α-amylase detected in pellicle were enriched in saliva samples, but not in gingival crevicular fluid, by western blot, and their abundance ratios were high in saliva and low in gingival crevicular fluid when analyzed by stable isotope labeling. Serotransferrin, however, was found only in the pellicle and gingival crevicular fluid by western blot and its abundance ratio was low in saliva. Our study revealed that the gingival crevicular fluid appears to contribute to pellicle formation in addition to saliva.