Project description:Intact mass analyses (HPLC-ESI-MS) of GELFREE separated fractions of yeast. A total of 66 raw files, representing two replicate analyses.
Project description:This data set contains the following:
1) 66 raw files for NeuCode-labeled human proteoforms from the Jurkat cell line analyzed via "intact-mass" (i.e., LC-MS, with no precursor fragmentation). Three biological replicates were performed (files from the different replicates are labeled with 022317, 031617, or 031817, respectively). For each replicate, proteoforms were separated offline using a 12% Tris-acetate Gelfree cartridge and 11 fractions were collected. Two technical replicate LC-MS injections of each fraction were performed, yielding a total of 66 raw files (3 biological replicates x 11 fractions x 2 injections).
2) 22 raw files for label-free human proteoforms from the Jurkat cell line analyzed via "top-down" (i.e., LC-MS/MS, with precursor fragmentation). One biological replicate was performed (labeled 032017). Proteoforms were separated offline using a 12% Tris-acetate Gelfree cartridge and 11 fractions were collected. Two technical replicate LC-MS/MS injections of each fraction were performed, yielding a total of 22 raw files (1 biological replicate x 11 fractions x 2 injections).
3) Multi-protease and trypsin-only pruned G-PTM-D databases used for proteoform identification. Note that the bottom-up data used to generate these databases can be found elsewhere on MassIVE (MSV000083304).
Project description:Raw top-down LC-MS/MS files from 12% GELFREE separated fractions of yeast. Raw files for 2 technical replicates of each fraction, in total 24 raw files.
Project description:The “quality” rather than “quantity” of lipoprotein particles is more relevant to cardiovascular diseases (CVD), since lipoprotein particles are highly heterogeneous. However, the targeted separation, detection, and exploration of the heterogeneous on omic-scale for lipoprotein remain challenging and rarely touched. Here, we established a high-resolution proteomics and lipidomics (HiPL) method. Briefly, the lipoprotein particles were separated into nine fractions (Lipo-HiPL) using anion-exchange chromatography (AEC), in which HDL, LDL, and VLDL were fractionated into three more fractions respectively. Furthermore, the HDL subclasses were delicately purified within nine fractions (HDL-HiPL), covering diverse protein-lipid heterogeneity. Integration of proteomic and lipidomic analysis revealed proteome-lipidome connectivity (PLC) in lipoprotein and HDL particles, which highly correlated with the atherosclerotic phenotype in rabbit model. Importantly, the lipoprotein “quality” revealed by PLC was found to be related more closely to clinical status in acute coronary syndrome patients than direct proteome and lipidome quantification. Thus, proteome-lipidome connectivity (PLC) as novel HDL “quality” features could be highly associated with atherosclerotic cardiovascular diseases.
Project description:Apolipoprotein E (apoE) plays a pivotal role in the pathogenesis of Alzheimer’s disease (AD). In the brain, apoE is predominantly expressed and secreted by astrocytes, but is dramatically up-regulated in microglia under AD-associated conditions. Although the function of astrocytic apoE has been widely investigated, whether and how apoE particles derived from different types of glia differ in biological features and function remains elusive. Here, we show that apoE particles derived from astrocytes and microglia exhibit dissimilar sizes. Microglial apoE particles impaired neurite growth and synapses and promoted neuronal senescence, whereas GPNMB-deficient microglial apoE particles abolished these detrimental effects. These findings provide direct evidence supporting that microglia-derived apoE particles contribute to neuronal senescence and toxicity.