Dataset Information

MASPECTRAS: a platform for management and analysis of proteomics LC-MS/MS data.

ABSTRACT: BACKGROUND: The advancements of proteomics technologies have led to a rapid increase in the number, size and rate at which datasets are generated. Managing and extracting valuable information from such datasets requires the use of data management platforms and computational approaches. RESULTS: We have developed the MAss SPECTRometry Analysis System (MASPECTRAS), a platform for management and analysis of proteomics LC-MS/MS data. MASPECTRAS is based on the Proteome Experimental Data Repository (PEDRo) relational database schema and follows the guidelines of the Proteomics Standards Initiative (PSI). Analysis modules include: 1) import and parsing of the results from the search engines SEQUEST, Mascot, Spectrum Mill, X! Tandem, and OMSSA; 2) peptide validation, 3) clustering of proteins based on Markov Clustering and multiple alignments; and 4) quantification using the Automated Statistical Analysis of Protein Abundance Ratios algorithm (ASAPRatio). The system provides customizable data retrieval and visualization tools, as well as export to PRoteomics IDEntifications public repository (PRIDE). MASPECTRAS is freely available at http://genome.tugraz.at/maspectras CONCLUSION: Given the unique features and the flexibility due to the use of standard software technology, our platform represents significant advance and could be of great interest to the proteomics community.

SUBMITTER: Hartler J

PROVIDER: S-EPMC1906842 | biostudies-literature | 2007

REPOSITORIES: biostudies-literature

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MASPECTRAS: a platform for management and analysis of proteomics LC-MS/MS data.

Hartler Jürgen J Thallinger Gerhard G GG Stocker Gernot G Sturn Alexander A Burkard Thomas R TR Körner Erik E Rader Robert R Schmidt Andreas A Mechtler Karl K Trajanoski Zlatko Z

BMC bioinformatics 20070613

<h4>Background</h4>The advancements of proteomics technologies have led to a rapid increase in the number, size and rate at which datasets are generated. Managing and extracting valuable information from such datasets requires the use of data management platforms and computational approaches.<h4>Results</h4>We have developed the MAss SPECTRometry Analysis System (MASPECTRAS), a platform for management and analysis of proteomics LC-MS/MS data. MASPECTRAS is based on the Proteome Experimental Data ...[more]

PMID: 17567892

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Project description:BackgroundAlthough fold change is a commonly used criterion in quantitative proteomics for differentiating regulated proteins, it does not provide an estimation of false positive and false negative rates that is often desirable in a large-scale quantitative proteomic analysis. We explore the possibility of applying the Significance Analysis of Microarray (SAM) method (PNAS 98:5116-5121) to a differential proteomics problem of two samples with replicates. The quantitative proteomic analysis was carried out with nanoliquid chromatography/linear iron trap-Fourier transform mass spectrometry. The biological sample model included two Mycobacterium smegmatis unlabeled cell cultures grown at pH 5 and pH 7. The objective was to compare the protein relative abundance between the two unlabeled cell cultures, with an emphasis on significance analysis of protein differential expression using the SAM method. Results using the SAM method are compared with those obtained by fold change and the conventional t-test.ResultsWe have applied the SAM method to solve the two-sample significance analysis problem in liquid chromatography/mass spectrometry (LC/MS) based quantitative proteomics. We grew the pH5 and pH7 unlabelled cell cultures in triplicate resulting in 6 biological replicates. Each biological replicate was mixed with a common 15N-labeled reference culture cells for normalization prior to SDS/PAGE fractionation and LC/MS analysis. For each biological replicate, one center SDS/PAGE gel fraction was selected for triplicate LC/MS analysis. There were 121 proteins quantified in at least 5 of the 6 biological replicates. Of these 121 proteins, 106 were significant in differential expression by the t-test (p < 0.05) based on peptide-level replicates, 54 were significant in differential expression by SAM with Delta = 0.68 cutoff and false positive rate at 5%, and 29 were significant in differential expression by the t-test (p < 0.05) based on protein-level replicates. The results indicate that SAM appears to overcome the false positives one encounters using the peptide-based t-test while allowing for identification of a greater number of differentially expressed proteins than the protein-based t-test.ConclusionWe demonstrate that the SAM method can be adapted for effective significance analysis of proteomic data. It provides much richer information about the protein differential expression profiles and is particularly useful in the estimation of false discovery rates and miss rates.

Dataset Information

MASPECTRAS: a platform for management and analysis of proteomics LC-MS/MS data.

Publications

MASPECTRAS: a platform for management and analysis of proteomics LC-MS/MS data.

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