Complexity of the human whole saliva proteome

Hirtz, Christophe; Chevalier, François; Centeno, Delphine; Egea, Jean-Christophe; Rossignol, Michel; Sommerer, Nicolas; Périère, Deville de

doi:10.1007/bf03168453

Cited by 48 publications

(29 citation statements)

References 23 publications

(44 reference statements)

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“…[63][64][65][66][67] Many of these investigators employed samples of whole saliva, which, in addition to secretions from the parotid and the SM/SL glands, contains the protein products of the cells that make up the oral cavity, minor gland and nasal secretions, gingival crevicular fluid, and contributions from microorganisms. [68][69][70][71][72][73] Other investigators focused on subsets of salivary secretions. For example, 2-D SDS-PAGE separation followed by MS identification was used to characterize parotid, SM, SL, and/or SM/SL salivas collected as the ductal secretions.…”

Section: Discussionmentioning

confidence: 99%

The Proteomes of Human Parotid and Submandibular/Sublingual Gland Salivas Collected as the Ductal Secretions

et al. 2008

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Saliva is a body fluid with important functions in oral and general health. A consortium of three research groups catalogued the proteins in human saliva collected as the ductal secretions: 1166 identifications-914 in parotid and 917 in submandibular/sublingual saliva-were made. The results showed that a high proportion of proteins that are found in plasma and/or tears are also present in saliva along with unique components. The proteins identified are involved in numerous molecular processes ranging from structural functions to enzymatic/catalytic activities. As expected, the majority mapped to the extracellular and secretory compartments. An immunoblot approach was used to validate the presence in saliva of a subset of the proteins identified by mass spectrometric approaches. These experiments focused on novel constituents and proteins for which the peptide evidence was relatively weak. Ultimately, information derived from the work reported here and related published studies can be used to translate blood-based clinical laboratory tests into a format that utilizes saliva. Additionally, a catalogue of the salivary proteome of healthy individuals allows future analyses of salivary samples from individuals with oral and systemic diseases, with the goal of identifying biomarkers with diagnostic and/or prognostic value for these conditions; another possibility is the discovery of therapeutic targets.

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Section: Discussionmentioning

confidence: 99%

The Proteomes of Human Parotid and Submandibular/Sublingual Gland Salivas Collected as the Ductal Secretions

et al. 2008

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“…Numerous studies have been performed to identify saliva proteins using 2-DE/MS [362][363][364][365][366][367][368][369][370]. A significant number of spots on a typical saliva 2-D gel actually correspond to amylases, cystatins, and Igs [369,370].…”

Section: Analysis and Characterization Of Human Saliva Proteomementioning

confidence: 99%

“…A significant number of spots on a typical saliva 2-D gel actually correspond to amylases, cystatins, and Igs [369,370]. Therefore, depletion of amylase and Igs prior to 2-DE analysis should improve mapping and identification of saliva proteins.…”

Section: Analysis and Characterization Of Human Saliva Proteomementioning

confidence: 99%

Human body fluid proteome analysis

2006

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The focus of this article is to review the recent advances in proteome analysis of human body fluids, including plasma/serum, urine, cerebrospinal fluid, saliva, bronchoalveolar lavage fluid, synovial fluid, nipple aspirate fluid, tear fluid, and amniotic fluid, as well as its applications to human disease biomarker discovery. We aim to summarize the proteomics technologies currently used for global identification and quantification of body fluid proteins, and elaborate the putative biomarkers discovered for a variety of human diseases through human body fluid proteome (HBFP) analysis. Some critical concerns and perspectives in this emerging field are also discussed. With the advances made in proteomics technologies, the impact of HBFP analysis in the search for clinically relevant disease biomarkers would be realized in the future.

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“…Antibodies against viruses and viral components can also be detected in saliva, therefore making it easier to diagnose various infections such as, for example, hepatitis A, B, or C; HIV; rubella; and dengue [16][17][18][19]. Identification of all saliva proteins [20][21][22][23][24][25][26][27][28][29][30][31][32][33][34][35][36][37][38][39] allowed comparative analysis of proteomic maps of healthy and ill people, which revealed differentially expressed proteins as potential biomarkers [26,28,32,35,36,38].…”

Section: Introductionmentioning

confidence: 99%

Proteomic Studies of Saliva: A Proposal for a Standardized Handling of Clinical Samples

Chevalier

Hirtz

Chay³

et al. 2007

Clin Proteom

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Background In recent years, differential analysis of proteins from human saliva, i.e., proteomic analysis, has received much attention mainly due to its unstressful sampling and its great potential for biomarker research. It is widely considered that saliva is a highly stable medium for proteins thanks to a large amount of antiprotease agents, even at ambient and physiological temperatures. Objective To find the best protocol for the handling of samples, we have investigated the stability of saliva proteins stored at different temperatures (from −80 to 20°C) by oneand two-dimensional electrophoresis. Results At 20°C, no major changes were observed on protein one-dimensional profiles following 1 day of storage; however, between 7 days and 30 days, the native alphaamylase band decreased slightly to give several bands with molecular weight between 35 and 25 kDa. The same phenomenon appeared after 30 days of storage at 4°C. Two-dimensional analysis of salivary maps revealed degradation from day 7 of several protein groups for samples stored at 20°C. Conclusion All these findings have to be carefully considered when saliva is collected for clinical proteomic analysis. We can conclude that, to maintain the optimum stability of saliva proteins, saliva samples should be collected on ice followed by the addition of protease inhibitor cocktail, centrifuged to remove insoluble material, and stored at −20 or −80°C.

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Complexity of the human whole saliva proteome

Cited by 48 publications

References 23 publications

The Proteomes of Human Parotid and Submandibular/Sublingual Gland Salivas Collected as the Ductal Secretions

The Proteomes of Human Parotid and Submandibular/Sublingual Gland Salivas Collected as the Ductal Secretions

Human body fluid proteome analysis

Proteomic Studies of Saliva: A Proposal for a Standardized Handling of Clinical Samples

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