Proteome analysis of whole saliva: A new tool for rheumatic diseases – the example of Sjögren's syndrome

Giusti, Laura; Baldini, Chiara; Bazzichi, Laura; Ciregia, Federica; Tonazzini, Ilaria; Mascia, G.; Giannaccini, Gino; Bombardieri, Stefano; Lucacchini, Antonio

doi:10.1002/pmic.200600783

Cited by 137 publications

(134 citation statements)

References 36 publications

(21 reference statements)

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“…Proteomic characterization of human whole saliva for identification of disease-specific biomarkers is guaranteed to provide an easy-to-use and powerful diagnostic tool for defining the onset, progression and prognosis of human systemic diseases and, in particular, oral autoimmune and cancer diseases [4][5][6][7][8]. However, it is widely recognized that the protein profile of whole saliva is dominated by a subset of abundant proteins mainly alpha amylase [9][10][11][12] that mask potential low-abundance biomarkers.…”

Section: Introductionmentioning

confidence: 99%

An approach to remove alpha amylase for proteomic analysis of low abundance biomarkers in human saliva

et al. 2008

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Proteomic characterization of human whole saliva for the identification of disease-specific biomarkers is guaranteed to be an easy-to-use and powerful diagnostic tool for defining the onset, progression and prognosis of human systemic diseases and, in particular, oral diseases. The high abundance of proteins, mainly alpha amylase, hampers the detection of low abundant proteins appearing in the disease state and therefore should be removed. In the present study a 2-DE was used to analyze human whole saliva following the removal of alpha amylase by affinity adsorption to potato starch. After alpha amylase removal whole saliva was analyzed by SDS-PAGE showing at least sixfold removal efficiency and by an alpha amylase activity assay showing 97% reduced activity. MS identification of the captured alpha amylase after elution demonstrated specific removal; 2-DE analysis showed the selective removal of alpha amylase and consequently increased gel resolution. MS identification of protein spots in the 60 kDa area revealed 15 proteins, which were masked before alpha amylase removal. In conclusion, treatment of human whole saliva with an alpha amylase removal device increases gel resolution and enables a higher protein sample for analysis.

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Section: Introductionmentioning

confidence: 99%

An approach to remove alpha amylase for proteomic analysis of low abundance biomarkers in human saliva

et al. 2008

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“…Saliva is also easy to store and transport and in contrast to blood there are minimal collection-associated risks. The search of dynamic marker for rheumatic disease like Sjögren's syndrome [6] found with the proteome of whole saliva an interesting field of action [7][8][9]. The proteome of saliva has been investigated by numerous researchers over the last decades and around 1400 distinct precursor proteins were identified [10].…”

Section: Introductionmentioning

confidence: 99%

Analysis of the Human Salivary Peptidome by Differential Peptide Display and LC-MS/MS Overview Sequencing

Yondre¹,

Tammen²,

Hess³

et al. 2008

TOPROTJ

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Abstract:In recent years interest in the characterization of the human salivary proteome has increased in order to explore its diagnostic potential. Major constituents of human saliva are highly polymorphic proteins that may have biological roles in oral lubrication and protection, e.g. proline-rich proteins (PRPs), statherins, histatins and cystatins. Interestingly, many of theses proteins are rapidly degraded in the oral cavity by host-and bacteria-or viral-derived proteases. Thus, comprehensive analysis of peptides up to 15 kDa (peptidomics) of whole saliva may yield basic information on proteolytic patterns. By employing a LC-ESI-MS/MS approach a total of 107 native peptides from 17 distinct protein precursors was identified from whole saliva. Subsequently the catalog of peptides was used to analyze inter-individual differences in saliva samples from four donors by differential peptide display technology. Genetic polymorphisms were found in peptides from the PRB4M_HUMAN and PROL4_HUMAN precursors. Analysis of the proposed N-and C-termini of the peptides revealed frequent cleavage after Lys or Arg which is characteristic for salivary kallikrein enzymes. Furthermore, we highlight the cleavage motif Gln/Gly in the PRP-C precursor, which suggests a new proteolytic pattern in saliva.

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“…Based on mass spectrometric screening, peptidome analysis is able to complete high throughout proteomic profiling within only a few hours [15,16], which could provide possible solutions of multiple biomarker detection for disease diagnosis. There are several studies performed essentially by analyzing saliva, tears, and salivary gland tissue in pSS [17][18][19][20][21][22]. Driss et al [23] identified a 7,606-Da biomarker peptide unique to the salivary samples from the SS subjects.…”

Section: Discussionmentioning

confidence: 98%

Establishment of a novel diagnostic model for Sjögren’s syndrome by proteomic fingerprinting

Sun

Zhang

et al. 2014

Clin Rheumatol

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Primary Sjögren's syndrome (pSS) is a systemic autoimmune disease that lacks sensitive and specific diagnostic methods. The aim of this study was to identify potential biomarkers specific for pSS and to establish a diagnostic model. Serum samples from patients with pSS, disease controls (DC, patients with systemic lupus erythematosus (SLE), rheumatoid arthritis (RA)), and healthy controls (HC)) were randomly divided into a training set (35 pSS, 50 DC, and 26 HC) and a testing set (25 pSS, 50 DC, and 25 HC). Weak cationic exchange (WCX) magnetic beads were used to differentially capture serum proteins prior to proteomic analysis. Proteomic mass spectra were generated by matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOF-MS). One hundred differential M/Z peaks associated with pSS were identified, and the m/z peaks at 8,133.85, 11,972.8, 2,220.81, and 4,837.66 were used to establish a diagnostic model for pSS. This diagnostic model was able to distinguish pSS from non-pSS controls with a sensitivity of 77.1 % and a specificity of 85.5 %, and its efficacy was confirmed in our blinded testing set with good sensitivity and specificity of 95.5 and 88 %, respectively. The results indicated that the proteomic fingerprinting model was effective in the diagnosis of pSS.

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Proteome analysis of whole saliva: A new tool for rheumatic diseases – the example of Sjögren's syndrome

Cited by 137 publications

References 36 publications

An approach to remove alpha amylase for proteomic analysis of low abundance biomarkers in human saliva

An approach to remove alpha amylase for proteomic analysis of low abundance biomarkers in human saliva

Analysis of the Human Salivary Peptidome by Differential Peptide Display and LC-MS/MS Overview Sequencing

Establishment of a novel diagnostic model for Sjögren’s syndrome by proteomic fingerprinting

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