Proteomics

Dataset Information

85

Copy number analysis of the murine platelet proteome spanning the complete abundance range


ABSTRACT: Knowledge of the identity and quantity of expressed proteins of a cell type is a prerequisite for a complete understanding of its molecular functions. Mass spectrometry (MS)-based proteomics has allowed the identification of the entire protein complement of yeast and the close-to-complete set of proteins expressed in mammalian cell lines. Using recent technological advances we here characterize the proteome of murine platelets, key actors in mediating hemostasis and thrombosis. We accurately measured the absolute protein concentrations of thirteen platelet proteins by SILAC-Protein Epitope Signature Tags (PrESTs) and used them as reference points to estimate the copy number of all proteins of the platelet proteome. To distinguish contaminants such as plasma or erythrocyte proteins from true platelet proteins, we monitored protein abundance profiles across multiple purification steps. In total, we absolutely quantified 4,400 platelet proteins, with estimated copy numbers ranging from less than ten to about a million per cell. Stoichiometries derived from our data correspond well with previous studies. Our study provides a close-to-complete reference map of platelet proteins, which will be useful to the community, for instance for interpreting mouse models of human platelets diseases.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Mus musculus  

TISSUE(S): Blood Platelet

DISEASE(S): Disease Free

SUBMITTER: Nadin Neuhauser  

LAB HEAD: Matthias Mann

PROVIDER: PXD000747 | Pride | 2015-08-18

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
20130528_EXQ4_MaZe_SA_P1_11.raw Raw
20130528_EXQ4_MaZe_SA_P1_4.raw Raw
20130528_EXQ4_MaZe_SA_P1_5.raw Raw
20130528_EXQ4_MaZe_SA_P1_6.raw Raw
20130528_EXQ4_MaZe_SA_P1_8.raw Raw
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Publications

Copy number analysis of the murine platelet proteome spanning the complete abundance range.

Zeiler Marlis M   Moser Markus M   Mann Matthias M  

Molecular & cellular proteomics : MCP 20140909 12


Knowledge of the identity and quantity of expressed proteins of a cell type is a prerequisite for a complete understanding of its molecular functions. Mass-spectrometry-based proteomics has allowed the identification of the entire protein complement of yeast and the close-to-complete set of proteins expressed in mammalian cell lines. Using recent technological advances, we here characterized the proteome of murine platelets, key actors in mediating hemostasis and thrombosis. We accurately measur  ...[more]

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