ULMC Plasma and serum exRNA from healthy donors at University of Michigan
Ontology highlight
ABSTRACT:
ORGANISM(S): Homo sapiens
PROVIDER: GSE121869 | GEO | 2018/10/27
REPOSITORIES: GEO
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Project description:ULMC Plasma and serum exRNA from healthy donors at University of Michigan
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2018-12-20 | GSE124131 | GEO
Project description:Previously, we published a dataset of human blood plasma and serum samples of 10 healthy males and 10 healthy females, fractionated on a set of sorbents (cation exchange Toyopearl CM-650M, CM Bio-Gel A, SP Sephadex C-25 and anion exchange QAE Sephadex A-25) and analyzed by LC-MS/MS individually and pooled in equal amounts (Supplementary Table S1, Sheet 1) [33]. The mass spectrometry peptidomics data was deposited to the ProteomeXchange Consortium via the PRIDE partner repository (dataset identifiers PXD008141 and 10.6019/PXD008141). Direct download link: http://www.ebi.ac.uk/pride/archive/projects/PXD008141. We analyzed this dataset again within this work. The detailed information about the dataset of blood plasma/serum samples of 20 healthy donors fractionated on a set of sorbents is available in the original paper [33], including the clinical parameters of the donors, sample collection, plasma/serum fractionation, peptide extraction and LC-MS/MS analysis. 33. Arapidi, G. et al. Peptidomics dataset: Blood plasma and serum samples of healthy donors fractionated on a set of chromatography sorbents. Data Brief 18, 1204–1211 (2018).
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Project description:Blood as connective tissue potentially contains evidence of all processes occurring within the organism, at least in trace amounts (Petricoin et al., 2006) [1]. Because of their small size, peptides penetrate cell membranes and epithelial barriers more freely than proteins. Among the peptides found in blood, there are both fragments of proteins secreted by various tissues and performing their function in plasma and receptor ligands: hormones, cytokines and mediators of cellular response (Anderson et al., 2002) [2]. In addition, in minor amounts, there are peptide disease markers (for example, oncomarkers) and even foreign peptides related to pathogenic organisms and infection agents. To propose an approach for detailed peptidome characterization, we carried out an LC-MS/MS analysis of blood serum and plasma samples taken from 20 healthy donors on a TripleTOF 5600+ mass-spectrometer. We prepared samples based on our previously developed method of peptide desorption from the surface of abundant blood plasma proteins followed by standard chromatographic steps (Ziganshin et al., 2011) [3]. The mass-spectrometry peptidomics data presented in this article have been deposited to the ProteomeXchange Consortium (Deutsch et al., 2017) [4] via the PRIDE partner repository with the dataset identifier PXD008141 and 10.6019/PXD008141.
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Project description:The Michael J. Fox Foundation (MJFF) collected AGO2 exRNA samples for distribution to interested individuals.
2018-12-22 | GSE124269 | GEO
Project description:Previously, we published a dataset of human blood plasma and serum samples of 10 healthy males and 10 healthy females, fractionated on a set of sorbents (cation exchange Toyopearl CM-650M, CM Bio-Gel A, SP Sephadex C-25 and anion exchange QAE Sephadex A-25) and analyzed by LC-MS/MS individually and pooled in equal amounts (Supplementary Table S1, Sheet 1) [33]. Blood is a complex tissue and can theoretically contain products of all processes occurring in different parts of the body. To identify potential sources of “alien” (non-human) plasma peptides, we performed a de novo analysis of mass spectrometry data. De novo analysis is a less efficient method of identification than search against databases, since the accuracy and resolution of modern mass spectrometers such as QTOF or Orbitrap remains not high enough. However, we use de novo analysis to identify organisms that include the most abundant components of the complex peptide mixture. This procedure allows us to develop a hypothesis and then perform a standard search against a database of proteins of identified organisms. The de novo identification was carried out using PEAKS Studio 8.0 (Bioinformatics Solutions Inc., Canada) and mass spectrometry driven BLAST analysis against the RefSeq non-redundant database NCBInr (https://www.ncbi.nlm.nih.gov/protein/). Mass spectra identified as fragments of proteins from different organisms were assigned to a taxonomic level at which these different organisms converged (Supplementary Table S2). 33. Arapidi, G. et al. Peptidomics dataset: Blood plasma and serum samples of healthy donors fractionated on a set of chromatography sorbents. Data Brief 18, 1204–1211 (2018).
2024-06-14 | PXD027701 | Pride
Project description:Blood as connective tissue potentially contain evidence of all processes occurring within the organism, at least in trace amounts. Because of their small size, peptides overcome cell membranes and epithelial barriers more freely than proteins. Among the peptides found in blood, there are both fragments of proteins secreted by various tissues and performing their function in plasma, as well as receptor ligands: hormones, cytokines, mediators of the cellular response. In addition, in minor amounts, there are disease peptide markers (for example, oncomarkers) and even foreign peptides related to pathogenic organisms and infection agents. To characterize the normal peptidome LC-MS/MS analysis was carried out of blood serum and plasma samples taken from 20 healthy donors on TripleTOF 5600+ mass-spectrometer. Sample preparation was carried out based on our previously developed method of peptide desorption from the surface of abundant blood plasma proteins followed by standard chromatographic steps.
2017-11-14 | PXD008141 | Pride
Project description:Previously, we published a dataset of human blood plasma and serum samples of 10 healthy males and 10 healthy females, fractionated on a set of sorbents (cation exchange Toyopearl CM-650M, CM Bio-Gel A, SP Sephadex C-25 and anion exchange QAE Sephadex A-25) and analyzed by LC-MS/MS individually and pooled in equal amounts (Supplementary Table S1, Sheet 1) [33]. We focused on those peptides that could be found in the blood plasma and serum using a standard search against the database of human proteins (UniProt Knowledgebase, taxon human). The combination of search engines MASCOT and X! Tandem, based on Scaffold 4 software with FDR less than 1%, allowed us to identify 15,530 unique peptides that belong to 2,127 protein groups (Table 1, Supplementary Table S1, Sheets 2 and 3). The Venn diagram shows that slightly less than 40% of the peptides are found in all four analyzed samples (Figures 1A and 1B). About 70% of the peptides are found in at least two samples. The accumulation diagram (Figure 1C) shows that the number of new unique peptides does not reach a plateau after repeated analyses of the same plasma sample — even after six runs. The high variability of the plasma and serum peptidome most likely indicates its sophisticated composition. 33. Arapidi, G. et al. Peptidomics dataset: Blood plasma and serum samples of healthy donors fractionated on a set of chromatography sorbents. Data Brief 18, 1204–1211 (2018).
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Project description:To further understanding of mature microRNA in plasma from healthy people, we have employed microRNA microarray as a discovery platform with the potential to identify the plasma microRNA levels of healthy people. Human peripheral blood was drawn from 4 healthy donors, and plasma was obtained by two-step centrifugation. Equal of total RNA from the plasma was detected by microRNA microarray including 866 human and 89 human viral miRNAs (Sanger miRBase, release 12.0). About 170 miRNAs could be detected by microarray in all 4 samples of plasma. Among them, 6 microRNAs (miR-451, miR-16, miR-133a, miR-1, miR-499 and miR-208a) were detected in the RNA from the same plasma by real-time PCR.
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