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

Abstract Background: 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...

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Autores principales: Odanaka,Hibiki, Obama,Takashi, Sawada,Naoko, Sugano,Marika, Itabe,Hiroyuki, Yamamoto,Matsuo
Lenguaje:English
Publicado: Sociedad de Biología de Chile 2020
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Acceso en línea:http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602020000100202
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spelling oai:scielo:S0716-976020200001002022020-06-25Comparison of protein profiles of the pellicle, gingival crevicular fluid, and saliva: possible origin of pellicle proteinsOdanaka,HibikiObama,TakashiSawada,NaokoSugano,MarikaItabe,HiroyukiYamamoto,Matsuo Pellicle Saliva Gingival crevicular fluid Proteome Isobaric tag labeling Serotransferrin Cystatin Alpha-amylase Abstract Background: 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. Results: 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. Conclusions: Our study revealed that the gingival crevicular fluid appears to contribute to pellicle formation in addition to saliva.info:eu-repo/semantics/openAccessSociedad de Biología de ChileBiological Research v.53 20202020-01-01text/htmlhttp://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602020000100202en10.1186/s40659-020-0271-2
institution Scielo Chile
collection Scielo Chile
language English
topic Pellicle
Saliva
Gingival crevicular fluid
Proteome
Isobaric tag labeling
Serotransferrin
Cystatin
Alpha-amylase
spellingShingle Pellicle
Saliva
Gingival crevicular fluid
Proteome
Isobaric tag labeling
Serotransferrin
Cystatin
Alpha-amylase
Odanaka,Hibiki
Obama,Takashi
Sawada,Naoko
Sugano,Marika
Itabe,Hiroyuki
Yamamoto,Matsuo
Comparison of protein profiles of the pellicle, gingival crevicular fluid, and saliva: possible origin of pellicle proteins
description Abstract Background: 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. Results: 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. Conclusions: Our study revealed that the gingival crevicular fluid appears to contribute to pellicle formation in addition to saliva.
author Odanaka,Hibiki
Obama,Takashi
Sawada,Naoko
Sugano,Marika
Itabe,Hiroyuki
Yamamoto,Matsuo
author_facet Odanaka,Hibiki
Obama,Takashi
Sawada,Naoko
Sugano,Marika
Itabe,Hiroyuki
Yamamoto,Matsuo
author_sort Odanaka,Hibiki
title Comparison of protein profiles of the pellicle, gingival crevicular fluid, and saliva: possible origin of pellicle proteins
title_short Comparison of protein profiles of the pellicle, gingival crevicular fluid, and saliva: possible origin of pellicle proteins
title_full Comparison of protein profiles of the pellicle, gingival crevicular fluid, and saliva: possible origin of pellicle proteins
title_fullStr Comparison of protein profiles of the pellicle, gingival crevicular fluid, and saliva: possible origin of pellicle proteins
title_full_unstemmed Comparison of protein profiles of the pellicle, gingival crevicular fluid, and saliva: possible origin of pellicle proteins
title_sort comparison of protein profiles of the pellicle, gingival crevicular fluid, and saliva: possible origin of pellicle proteins
publisher Sociedad de Biología de Chile
publishDate 2020
url http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602020000100202
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