A catalogue of human saliva proteins identified by free flow electrophoresis-based peptide separation and tandem mass spectrometry.
نویسندگان
چکیده
Human saliva has great potential for clinical disease diagnostics. Constructing a comprehensive catalogue of saliva proteins using proteomic approaches is a necessary first step to identifying potential protein biomarkers of disease. However, because of the challenge presented in cataloguing saliva proteins with widely varying abundance, new proteomic approaches are needed. To this end, we used a newly developed approach coupling peptide separation using free flow electrophoresis with linear ion trap tandem mass spectrometry to identify proteins in whole human saliva. We identified 437 proteins with high confidence (false positive rate below 1%), producing the largest catalogue of proteins from a single saliva sample to date and providing new information on the composition and potential diagnostic utility of this fluid. The statistically validated, transparently presented, and annotated dataset provides a model for presenting large scale proteomic data of this type, which should facilitate better dissemination and easier comparisons of proteomic datasets from future studies in saliva.
منابع مشابه
Proteomics analysis of cells in whole saliva from oral cancer patients via value-added three-dimensional peptide fractionation and tandem mass spectrometry.
Whole human saliva possesses tremendous potential in clinical diagnostics, particularly for conditions within the oral cavity such as oral cancer. Although many have studied the soluble fraction of whole saliva, few have taken advantage of the diagnostic potential of the cells present in saliva, and none have taken advantage of proteomics capabilities for their study. We report on a novel prote...
متن کاملProteome analysis of Cryptosporidium parvum and C. hominis using two-dimentional electrophoresis, image analysis and tandem mass spectrometry
Until recently, Cryptosporidium was thought to be a single species genus. Molecular studies now showthat there are at least 10 valid species of this parasite. Among them, two morphologically identical species, C.hominis and C. parvum are the most pathogenic identified to date and share 97% of identical genomes.Post-genomic analyses is therefore necessary to explore further the...
متن کاملProteomics Analysis of Cells in Whole Saliva from Oral Cancer Patients via Value-added Three-dimensional Peptide Fractionation and Tandem Mass Spectrometry*□S
Whole human saliva possesses tremendous potential in clinical diagnostics, particularly for conditions within the oral cavity such as oral cancer. Although many have studied the soluble fraction of whole saliva, few have taken advantage of the diagnostic potential of the cells present in saliva, and none have taken advantage of proteomics capabilities for their study. We report on a novel prote...
متن کاملSheep and goat saliva proteome analysis: a useful tool for ingestive behavior research?
Sheep and goats differ in diet selection, which may reflect different abilities to deal with the ingestion of plant secondary metabolites. Although saliva provides a basis for immediate oral information via sensory cues and also a mechanism for detoxification, our understanding of the role of saliva in the pre-gastric control of the intake of herbivores is rudimentary. Salivary proteins have im...
متن کاملSeparation and identification of soybean leaf proteins by two-dimensional gel electrophoresis and mass spectrometry.
To establish a proteomic reference map for soybean leaves, we separated and identified leaf proteins using two-dimensional polyacrylamide gel electrophoresis (2D-PAGE) and mass spectrometry (MS). Tryptic digests of 260 spots were subjected to peptide mass fingerprinting (PMF) by matrix-assisted laser desorption/ionization-time of flight (MALDI-TOF) MS. Fifty-three of these protein spots were id...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- Molecular & cellular proteomics : MCP
دوره 4 11 شماره
صفحات -
تاریخ انتشار 2005