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Fulltext Salivary proteins associated with periodontitis in patients with Type 2 diabetes mellitus

Chan HH, Rahim ZH, Jessie K, Hashim OH, Taiyeb-Ali TB

Int J Mol Sci, 2012;13(4):4642-54.
PMID: 22606001 DOI: 10.3390/ijms13044642

The objective of this study was to investigate the salivary proteins that are associated with periodontitis in patients with Type 2 diabetes mellitus (T2DM). Volunteers for the study were patients from the Diabetic Unit, University of Malaya Medical Centre, whose periodontal status was determined. The diabetic volunteers were divided into two groups, i.e., patients with periodontitis and those who were periodontally healthy. Saliva samples were collected and treated with 10% TCA/acetone/20 mM DTT to precipitate the proteins, which were then separated using two-dimensional polyacrylamide gel electrophoresis. Gel images were scanned using the GS-800(TM) Calibrated Densitometer. The protein spots were analyzed and expressed in percentage volumes. The percentage volume of each protein spot was subjected to Mann-Whitney statistical analysis using SPSS software and false discovery rate correction. When the expression of the salivary proteins was compared between the T2DM patients with periodontitis with those who were periodontally healthy, seven proteins, including polymeric immunoglobulin receptor, plastin-2, actin related protein 3, leukocyte elastase inhibitor, carbonic anhydrases 6, immunoglobulin J and interleukin-1 receptor antagonist, were found to be differentially expressed (p < 0.01304). This implies that the proteins may have the potential to be used as biomarkers for the prediction of T2DM patients who may be prone to periodontitis.

Matched MeSH terms: Salivary Proteins and Peptides/analysis
Proteomic profile of edible bird's nest proteins

Liu X, Lai X, Zhang S, Huang X, Lan Q, Li Y, et al.

J Agric Food Chem, 2012 Dec 26;60(51):12477-81.
PMID: 23214475 DOI: 10.1021/jf303533p

Edible bird's nest (EBN) is made of the swiftlets' saliva, which has attracted rather more attention owing to its nutritious and medical properties. Although protein constitutes the main composition and plays an important role in EBN, few studies have focused on the proteomic profile of EBN. The purpose of this study was to produce a proteomic map and clarify common EBN proteins. Liquid-phase isoelectric focusing (LIEF) was combined with two-dimensional electrophoresis (2-DE) for comprehensive analysis of EBN proteins. From 20 to 100 protein spots were detected on 2-DE maps of EBN samples from 15 different sources. The proteins were mainly distributed in four taxa (A, B, C, and D) according to their molecular mass. Taxa A and D both contained common proteins and proteins that may be considered another characteristic of EBN. Taxon A was identified using MALDI-TOF-TOF/MS and found to be homologous to acidic mammalian chitinase-like ( Meleagris gallopavo ), which is in glycosyl hydrolase family 18.

Matched MeSH terms: Salivary Proteins and Peptides/analysis
Electrophoretic detection of salivary alpha-amylase activity

Rahim ZH, Yaacob HB

J Nihon Univ Sch Dent, 1992 Dec;34(4):273-7.
PMID: 1283755

Fresh samples of human whole saliva containing approximately 20-40 micrograms protein were analyzed using SDS-polyacrylamide slab gel electrophoresis systems. More than 20 protein bands were revealed by Coomassie Brilliant Blue R 250 staining. Some of the protein bands were shown to be glycoprotein-positive with PAS (periodic acid-Schiff) reagent. The protein bands with alpha-Amylase activity appeared within a molecular weight range of 120,000-180,000, which is 2 to 2.8 times higher than the normal molecular weight reported for alpha-Amylase from parotid saliva, and showed positive staining with PAS reagent. These results show that the alpha-Amylase in whole saliva appears to exist in a macromolecular form which is not dissociated in the presence of sodium dodecyl sulfate (SDS).

Matched MeSH terms: Salivary Proteins and Peptides/analysis*
Effects of fasting on saliva composition

Rahim ZH, Yaacob HB

J Nihon Univ Sch Dent, 1991 Dec;33(4):205-10.
PMID: 1787416

The concentrations of calcium, phosphate, protein and nitrite in whole unstimulated saliva, and the salivary flow rate under fasting conditions (saliva collected at least after 6 h without food and water) were compared with those under control conditions (saliva collected within 30 min to 1 h after food). The flow rate of fasting saliva was half that of control (0.098 ml/min vs 0.208 ml/min) and no significant differences in the flow rate were observed between sexes. The concentration of nitrite under fasting conditions was 50% higher than that in control saliva (p less than 0.05). The protein concentration was decreased, but not significantly, under fasting conditions. The composition of fasting saliva with regard to calcium and phosphate concentrations was comparable to that of the control. No significant variations in these components between sexes were observed under either condition.

Matched MeSH terms: Salivary Proteins and Peptides/analysis
Fulltext Salivary Amylase as a Marker of Salivary Gland Function in Patients Undergoing Radiotherapy for Oral Cancer

Vedam VKV, Boaz K, Natarajan S, Ganapathy S

J Clin Lab Anal, 2017 May;31(3).
PMID: 27637993 DOI: 10.1002/jcla.22048

BACKGROUND: The aim of this study was to evaluate salivary amylase in patients with primary oral cancer undergoing radiotherapy as the main modality of treatment.
MATERIALS/METHODS: The study was conducted on ten histologically proven cases of oral cancer undergoing radiotherapy. Stimulated whole saliva was collected at three stages of radiotherapy-0, 3, and 6 weeks. Salivary amylase was estimated using Henry-Chiamori method and comparison was made with appropriate age- and gender-matched controls.
RESULTS: Salivary amylase levels showed significant decrease in healthy subjects when compared to oral cancer patients (P < 0.001). The latter group also showed changing trend with initial decrease from 0 to 3 weeks followed by increase from 3 to 6 weeks following radiotherapy (P < 0.0528).
CONCLUSIONS: The trend in changes in the levels of salivary amylase could be used as a surrogate marker of salivary gland function in patients with oral cancer undergoing radiotherapy as primary treatment.

Matched MeSH terms: Salivary Proteins and Peptides/analysis*
Aberrant proteins featured in the saliva of habitual betel quid chewers: an indication of early oral premalignancy?

Jessie K, Jayapalan JJ, Rahim ZH, Hashim OH

Electrophoresis, 2014 Dec;35(24):3504-11.
PMID: 25223738 DOI: 10.1002/elps.201400252

Prolonged chewing of betel quid is known to cause oral diseases, including cancer. The present study was performed to screen for aberrant proteins in the saliva of habitual betel quid chewers compared to nonchewers. Saliva of female subjects (n = 10) who had been chewing betel quid for more than 20 years and nonbetel quid chewers (n = 10) of the same gender and range of age was analyzed by gel-based proteomics. Increased structural microheterogeneity of saliva haptoglobin beta chains indicated by shifts of focused spots similar to that earlier reported in patients with oral squamous cell carcinoma, and their relatively higher abundance compared to nonbetel quid chewers, were detected in saliva protein profiles of all chewers. In addition, the majority of the betel quid chewers also showed significant higher abundance of hemopexin, alpha-1B glycoprotein, alpha1-antitrypsin, complement C3, and transthyretin. These proteins had previously been associated with several different cancers. Our data demonstrated different forms of protein aberration in the saliva of betel quid chewers, which may be indicative of early oral precancerous conditions.

Matched MeSH terms: Salivary Proteins and Peptides/analysis*