PXD012462 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Unbiased mapping of human cerebrospinal fluid proteome dynamics |
Description | Our purpose is to explore the dynamics of a clinically relevant proteome by determining protein turnover, synthesis and breakdown. ]. The alteration of protein turnover represents a new type of biological information which might provide unique insight in disease pathophysiology, e.g. Alzheimer disease (AD), amyotrophic lateral sclerosis or diabetes. The use of tracer methods makes it however possible to follow protein synthesis on a proteome-scale based on the incorporation of stable isotope-labeled precursors such as 13C6-leucine. The latest mass spectrometry (MS) technologies on quantitative approach called stable isotope labeling kinetics (SILK) was applied to humans after the intravenous administration of 13C6-leucine. The SILK approach has therefore the potential to generate unique in vivo information that is not accessible using classical quantitative techniques. As a matter of fact, the concentration of a given protein in a tissue or a biological fluid is the combination of multiple events and mechanisms. The translation rate at the cellular level is obviously the initial determinant which will directly impact the presence/absence of a given protein. Translation is dependent on transcription and its genetic and epigenetic regulation. Transcriptomics is therefore one of the way to follow protein synthesis, but it is known that it reflects only partially protein concentration. In fact, many subsequent events will modify protein presence starting by post-translational maturation (which in case of pathologic mutation could lead to proteins misfolding, degradation or mis-trafficking. In our study, we are focusing on CSF proteins which originate locally from resident cells (lymphocytes...) or after compartment transfer, from central nervous system (CNS) and systemic tissues. In this work, we relied on high resolution MS (HRMS) to follow the kinetics incorporation of labelled Leucine in thousands of peptides corresponding to hundreds of proteins and their isoforms. This new approach necessitated first to develop original data processing and modelling of protein turnover which is the foundation for the SILK analysis of other types of samples, including blood and urine. The information that derived from this type of large scale analysis will help build a new vision of human physiology based on protein turnovers, and compartment transfer investigation. |
HostingRepository | PRIDE |
AnnounceDate | 2020-01-22 |
AnnouncementXML | Submission_2020-01-22_02:01:40.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Jerome Vialaret |
SpeciesList | scientific name: Homo sapiens (Human); NCBI TaxID: 9606; |
ModificationList | monohydroxylated residue; acetylated residue; iodoacetamide derivatized residue; deamidated residue |
Instrument | maXis |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2019-01-22 03:08:43 | ID requested | |
⏵ 1 | 2020-01-22 02:01:42 | announced | |
Publication List
Lehmann S, Hirtz C, Vialaret J, Ory M, Combes GG, Corre ML, Badiou S, Cristol JP, Hanon O, Cornillot E, Bauchet L, Gabelle A, Colinge J, In Vivo Large-Scale Mapping of Protein Turnover in Human Cerebrospinal Fluid. Anal Chem, 91(24):15500-15508(2019) [pubmed] |
Keyword List
curator keyword: Biological |
submitter keyword: CSF, protein, dynamics, human |
Contact List
sylvain Lehmann |
contact affiliation | St Eloi hospital, IRMB, INSERM U1183 80 av A Fiche, 34295 Montpellier France |
contact email | s-lehmann@chu-montpellier.fr |
lab head | |
Jerome Vialaret |
contact affiliation | CHU Montpellier |
contact email | j-vialaret@chu-montpellier.fr |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD012462
- Label: PRIDE project
- Name: Unbiased mapping of human cerebrospinal fluid proteome dynamics