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Multifaceted proteome analysis at solubility, redox, and expression dimensions for target identification

ABSTRACT: Multifaceted interrogation of the proteome deepens the system-wide understanding of biological systems; however, mapping the redox changes in the proteome has so far been significantly less informative than expression and solubility/stability analyses. Here, we devise the first high-throughput redox proteomics approach integrated with expression analysis (REX) and combine it with Proteome Integral Solubility Alteration (PISA) assay. The whole PISA-REX experiment in three biological replicates is multiplexed in a single tandem mass tag set (TMTpro). For benchmarking this compact PISA-REX tool, we analyzed HCT116 cells treated with auranofin. Then we applied PISA-REX to study the targets of Pladienolide B in SW620 cells, proteome remodeling upon stimulation of human monocytes by interferon α, and to paired primary and metastatic colon cancer cells. Providing comprehensive multifaceted information on the proteome, the compact PISA-REX has the potential to become an industry-standard in proteomics and to open new windows into the biology of health and disease.

INSTRUMENT(S): Orbitrap Fusion Lumos, Q Exactive HF

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Blood Cell, Cell Culture

SUBMITTER: Amir Ata Saei

LAB HEAD: Roman A. Zubarev

PROVIDER: PXD042967 | Pride | 2024-08-10

REPOSITORIES: Pride

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			Action	DRS
	PISA-REX_Auranofin_HCT116_1st_dataset_peptides.xlsx	Xlsx
	PISA-REX_Auranofin_HCT116_1st_dataset_proteins.xlsx	Xlsx
	PISA-REX_Auranofin_HCT116_2nd_dataset_peptides.xlsx	Xlsx
	PISA-REX_Auranofin_HCT116_2nd_dataset_proteins.xlsx	Xlsx
	PISA-REX_Interferon_THP1_peptides.xlsx	Xlsx

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