Applications of Surface-Enhanced Laser Desorption/Ionization Time-Of-Flight (SELDI-TOF) Mass Spectrometry in Defining Salivary Proteomic Profiles

AlTarawneh, Sandra; Bencharit, Sompop

doi:10.2174/1874210600903010074

Cited by 22 publications

(19 citation statements)

References 32 publications

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“…19–22 It was important to note here that this proteomic profiling corresponds well with clinical and histological diagnosis of DS. More importantly, each protein is differentially expressed among the non-DS, DS II and DS III individuals.…”

Section: Discussionsupporting

confidence: 59%

Elucidating role of salivary proteins in denture stomatitis using a proteomic approach

et al. 2012

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Denture stomatitis (DS) is the most common oral pathology among denture wearers, affecting over one-third of this group. DS is usually associated with C. albicans. However, unlike other oral candidiasis, most DS patients have intact host immunity. The presence of a denture alone is usually sufficient for DS. Saliva and its protein contents can theoretically predispose some denture wearers to DS and others resistant toward DS. Here we proposed for the first time to define salivary proteomic profiles of denture wearers with and without DS. SELDI-TOF/MS analysis suggests that there is a proteomic differentiation among control, localized and generalized DS. Based on initial SELDI-TOF/MS profiling, we further used reversed phase liquid chromatography, MALDI-TOF/MS, and LC-MS/MS to characterize the salivary proteins associated with DS. Nineteen proteins based on SELDI-TOF/MS profiling were found including cystatin-SN, statherin, kininogen-1, desmocollin-2, carbonic anhydrase-6, peptidyl-prolyl cis–trans isomerase A like peptides, cystatin C, and several immunoglobulin fragments. The proteomic content gives evidence of the interaction between host tissue, saliva, and candida. Further examination in larger populations of these proteins may help to gain a better understanding of DS pathological processes and improve DS treatments.

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Section: Discussionsupporting

confidence: 59%

Elucidating role of salivary proteins in denture stomatitis using a proteomic approach

et al. 2012

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“…These proteases potentially degrade protein biomarkers. It has been shown that leaving saliva samples for a period of time can alter proteomic profiles and change the biomarker content (Al-Tarawneh and Bencharit, 2009). Shortening the time of storage before centrifugation, fast frozen (with dried ice or liquid nitrogen), storing the samples in low temperature (À808C), and avoiding multiple freeze-thaw processes, as well as consistent sample collection protocol, are known to enhance consistent proteomic analytical results and the degradation of sensitive protein biomarkers (Schipper et al, 2007).…”

Section: Saliva Collection and Handling Processmentioning

confidence: 99%

“…This technique was used in some studies for initial profiling prior to further identification using LC-MS techniques, whereas in other studies it has been used as the main identification technique after initial profiling with 2DE (Supplementary Table 2). In some cases the SELDI-TOF/MS technique where the sample matrix (Protein Chip) has an active role in sample purification, desorption/ionization, and protein separation] was used to quantify and reproduce results (Al-Tarawneh and Bencharit, 2009). …”

Section: Proteomic Techniquesmentioning

confidence: 99%

Defining Salivary Biomarkers Using Mass Spectrometry-Based Proteomics: A Systematic Review

AlTarawneh

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et al. 2011

OMICS: A Journal of Integrative Biology

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Recent advancements in mass spectrometric proteomics provide a promising result in utilizing saliva to explore biomarkers for diagnostic purposes. However, the issues of specificity or redundancy of disease-associated salivary biomarkers have not been described. This systematic review was therefore aimed to define and summarize disease-related salivary biomarkers identified by mass spectrometry proteomics. Peer-reviewed articles published through July 2009 within three databases were reviewed. Out of 243 articles, 21 studies were selected in this systematic review with conditions including Sjö gren's syndrome, squamous cell carcinoma, dental caries, diabetes, breast cancer, periodontitis, gastric cancer, systemic sclerosis, oral lichen planus, bleeding oral cavity, and graft-versus-host disease. The sample size ranged from 3-41 in both diseased and control subjects, with no consensus on sample collection protocol. One hundred eighty biomarkers were identified in total; 87 upregulated, 63 downregulated, and 30 varying based on disease. Except for Sjö gren's syndrome, the majority of studies with the same disease produce inconsistent biomarkers. Larger sample size and standardization of sample collection/treatment protocol may improve future studies.

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“…The use of surface-enhanced laser desorption/ionization time-of-flight (SELDI-TOF) mass spectrometry (MS), which allows rapid, high-throughput detection of proteins in minute sample volumes without pre-processing, has been reported for several diseases [58]. Recently, analysis of saliva for protein biomarker discovery has mainly been performed using two-dimensional difference gel electrophoresis (2D-DIGE) coupled with MS (which can identify around 300 proteins in a sample [59]), and liquid chromatograpy-MS (LC-MS) based techniques (which can identify more than 1,050 proteins in a sample; reviewed in [60]).…”

Section: The Salivary Proteomementioning

confidence: 99%

Salivary biomarker development using genomic, proteomic and metabolomic approaches

2012

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The use of saliva as a diagnostic sample provides a non-invasive, cost-efficient method of sample collection for disease screening without the need for highly trained professionals. Saliva collection is far more practical and safe compared with invasive methods of sample collection, because of the infection risk from contaminated needles during, for example, blood sampling. Furthermore, the use of saliva could increase the availability of accurate diagnostics for remote and impoverished regions. However, the development of salivary diagnostics has required technical innovation to allow stabilization and detection of analytes in the complex molecular mixture that is saliva. The recent development of cost-effective room temperature analyte stabilization methods, nucleic acid pre-amplification techniques and direct saliva transcriptomic analysis have allowed accurate detection and quantification of transcripts found in saliva. Novel protein stabilization methods have also facilitated improved proteomic analyses. Although candidate biomarkers have been discovered using epigenetic, transcriptomic, proteomic and metabolomic approaches, transcriptomic analyses have so far achieved the most progress in terms of sensitivity and specificity, and progress towards clinical implementation. Here, we review recent developments in salivary diagnostics that have been accomplished using genomic, transcriptomic, proteomic and metabolomic approaches.

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Applications of Surface-Enhanced Laser Desorption/Ionization Time-Of-Flight (SELDI-TOF) Mass Spectrometry in Defining Salivary Proteomic Profiles

Cited by 22 publications

References 32 publications

Elucidating role of salivary proteins in denture stomatitis using a proteomic approach

Elucidating role of salivary proteins in denture stomatitis using a proteomic approach

Defining Salivary Biomarkers Using Mass Spectrometry-Based Proteomics: A Systematic Review

Salivary biomarker development using genomic, proteomic and metabolomic approaches

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