Document Detail


Protein and mucin retention on oral mucosal surfaces in dry mouth patients.
MedLine Citation:
PMID:  20572857     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Oral homeostasis depends largely on proteins and mucins present in saliva that coat all oral surfaces. The present study compared the protein composition of residual fluid on mucosal surfaces in subjects with normal salivary flow with that of patients with dry mouth caused by salivary hypofunction. Samples of residual mucosal fluid were collected using paper strips and then analysed by protein electrophoresis and immunoblotting. In both patients and controls, residual fluids on mucosal surfaces (except the anterior tongue in control subjects) had higher protein concentrations than unstimulated whole-mouth saliva. High-molecular-weight mucin (MUC5B) was present in greater amounts on the anterior tongue than on other surfaces in control subjects. In dry mouth patients who were unable to provide a measurable saliva sample, MUC5B was often still present on all mucosal surfaces but in reduced amounts on the anterior tongue. The membrane-bound mucin, MUC1, was prominent on buccal and labial surfaces in patients and controls. Statherin was still present on surfaces that were dried to remove salivary fluid, suggesting that it may be adsorbed as a protein pellicle. It is concluded that oral mucosal surfaces in dry mouth patients can retain MUC5B and other salivary proteins, although the functional integrity of these proteins is uncertain.
Authors:
Rashida Pramanik; Samira M Osailan; Stephen J Challacombe; David Urquhart; Gordon B Proctor
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Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  European journal of oral sciences     Volume:  118     ISSN:  1600-0722     ISO Abbreviation:  Eur. J. Oral Sci.     Publication Date:  2010 Jun 
Date Detail:
Created Date:  2010-06-24     Completed Date:  2010-09-28     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9504563     Medline TA:  Eur J Oral Sci     Country:  Denmark    
Other Details:
Languages:  eng     Pagination:  245-53     Citation Subset:  D; IM    
Affiliation:
NIHR Biomedical Research Centre & KCL Salivary Research Unit, Kings College London and Guy's & St Thomas' NHS, Guy'sCampus, London, UK. rashida.pramanik@kcl.ac.uk
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MeSH Terms
Descriptor/Qualifier:
Adult
Aged
Amylases / analysis
Arthritis, Rheumatoid / metabolism,  physiopathology
Case-Control Studies
Cysteine Proteinase Inhibitors / analysis
Dental Pellicle / metabolism
Female
Humans
Lip / metabolism
Male
Middle Aged
Mouth Mucosa / metabolism*
Mucin-1 / analysis
Mucin-5B / analysis
Mucins / analysis,  metabolism*
Palate, Hard / metabolism
Saliva / secretion
Salivary Cystatins / analysis
Salivary Proline-Rich Proteins / analysis
Salivary Proteins and Peptides / analysis,  metabolism*
Secretory Rate / physiology
Sialadenitis / metabolism,  physiopathology
Sjogren's Syndrome / metabolism,  physiopathology
Tongue / metabolism
Viscosity
Xerostomia / metabolism*,  physiopathology
Grant Support
ID/Acronym/Agency:
//Department of Health
Chemical
Reg. No./Substance:
0/CST4 protein, human; 0/Cysteine Proteinase Inhibitors; 0/MUC1 protein, human; 0/MUC5B protein, human; 0/MUC7 protein, human; 0/Mucin-1; 0/Mucin-5B; 0/Mucins; 0/STATH protein, human; 0/Salivary Cystatins; 0/Salivary Proline-Rich Proteins; 0/Salivary Proteins and Peptides; EC 3.2.1.-/Amylases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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