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Concentration of salivary protective proteins within the bound oral mucosal pellicle

Research output: Contribution to journalArticle

H. L. Gibbins, G. B. Proctor, G. E. Yakubov, S. Wilson, G. H. Carpenter

Original languageEnglish
Pages (from-to)707-713
Number of pages7
JournalOral Diseases
Issue number7
Accepted/In pressOct 2013
Published1 Oct 2014


  • Gibbins_et_al_2014_Oral_Diseases

    Gibbins_et_al_2014_Oral_Diseases.pdf, 458 KB, application/pdf

    Uploaded date:22 Jan 2016

    Version:Final published version

    Licence:CC BY-NC-ND

King's Authors


Objectives: To study which salivary proteins form the protective bound mucosal pellicle and to determine the role of transglutaminase in pellicle development. Materials and Methods: Oral epithelial cells were collected and underwent washes of different strengths, followed by homogenisation. SDS-PAGE, western blotting, IgA ELISAs and amylase activity assays were completed on cell homogenates and compared to saliva samples to confirm which salivary proteins were bound to cell surfaces. Results: Salivary mucins, MUC5B and MUC7, were strongly retained on the oral epithelial cell surface. Other bound proteins including cystatin S, carbonic anhydrase VI, secretory component and IgA could be washed off. IgA was present in concentrated levels in the bound mucosal pellicle compared to amounts in saliva. Amylase, one of the most abundant proteins present in saliva, showed minimal levels of binding. Transglutaminase 3 presence was confirmed, but proteins that it catalyses cross-links between, statherin and proline-rich proteins, showed minimal presence. Conclusion: Some protective salivary proteins including mucins and IgA become concentrated on oral surfaces in the bound mucosal pellicle, through specific interactions. Concentration of mucins would contribute to lubrication to prevent abrasion damage to soft tissues, whilst increased IgA could create an 'immune reservoir' against mucosal infection.

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