Abstract
The endogenous peptides and small proteins extracted from bovine ovarian follicular cells (oocytes, cumulus and granulosa cells) were identified by Top-down High Resolution Mass Spectrometry (TD-HR-MS/MS) in order to annotate peptido- and proteoforms detected using qualitative and quantitative profiling method based on ICM-MS (Intact Cell Matrix-Assisted Laser Desorption/Ionization Time-of-Flight Mass Spectrometry). The description and analysis of these Top-down MS data in the context of oocyte quality biomarkers research are available in the original research article of Labas et al. (2017) http://dx.doi.org/10.1016/j.jprot.2017.03.027[1]. Raw data derived from this peptidomic/proteomic analysis have been deposited to the ProteomeXchange Consortium via the PRIDE partner repository (dataset identifier PXD004892). Here, we described the inventory of all identified peptido- and proteoforms including their biochemical and structural features, and functional annotation of correspondent proteins. This peptide/protein inventory revealed that TD-HR-MS/MS was appropriate method for both global and targeted proteomic analysis of ovarian tissues, and it can be further employed as a reference for other studies on follicular cells including single oocytes.
Highlights
Raw and processed/analyzed mass spectrometry data obtained by Top-down high resolution mass spectrometry High Resolution Mass Spectrometry (HR-MS/MS) analyses of protein extracts performed by : 1) direct infusion to a LTQ orbitrap Velos Mass Spectrometer (ThermoFisher), 2) mLiquid Chromatography using an Ultimates3000 Ultra High Pressure Liquid Chromatographer combined to HR-MS/MS, 3) mLCHR-MS/MS with pre-fractionations based on Reverse Phase-High Pressure Liquid Chromatography (RP-HPLC) or gel filtration separation methods
The data presents the first inventory of endogenous peptides and small proteins identified in bovine ovarian follicular cells to annotate biomolecules detected by ICM-MS on whole follicular cells including single oocytes
The identifications of the proteoforms and peptidoforms from granulosa cells protein extract by combining mLC-HR-MS/MS and four different pre-fractionation strategies (3 separation methods based on reverse phase chromatography and one on gel filtration chromatography) could be compared to others separation and MS identification methods
Summary
Valérie Labas a,c, Ana-Paula Teixeira-Gomes b,c, Laura Bouguereau b,c, Audrey Gargaros a,c, Lucie Spina c,d, Aurélie Marestaing a,c, Svetlana Uzbekova a,c,n a UMR PRC, INRA 85, CNRS, Université de Tours, IFCE, 37380 Nouzilly, France b UMR ISP, INRA, Université de Tours, 37380 Nouzilly, France c INRA, Plateforme d’Analyse Intégrative des Biomolécules, Laboratoire de Spectrométrie de Masse, 37380 Nouzilly, France d INSA/CNRS 5504 - UMR INSA/INRA 792, Toulouse, France article info. We described the inventory of all identified peptido- and proteoforms including their biochemical and structural features, and functional annotation of correspondent proteins. V. Labas et al / Data in Brief 13 (2017) 175–179 was appropriate method for both global and targeted proteomic analysis of ovarian tissues, and it can be further employed as a reference for other studies on follicular cells including single oocytes.
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