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Deep Proteome Profiling by Isobaric Labeling, Extensive Liquid Chromatography, Mass Spectrometry, and Software-assisted Quantification
Published on: November 15, 2017
12.8K
[Multiomics study of HepG2 cell line proteome].
E V Poverennaya1, O I Kiseleva1, E A Ponomarenko1
1Institute of Biomedical Chemistry, Moscow, Russia.
Biomeditsinskaia Khimiia
|October 30, 2017
Summary
This study explores HepG2 proteome heterogeneity using a multi-omics approach. Combining transcriptomic (RNAseq) and proteomic (2DE-MS/MS) data aids in identifying aberrant proteoforms beyond canonical sequences.
Area of Science:
- Proteomics
- Genomics
- Molecular Biology
Background:
- Current proteomic studies primarily focus on abundant proteoforms from canonical sequences.
- Advancements in transcriptomic and proteomic technologies enable the identification of non-canonical proteoforms.
- Aberrant proteoforms arise from alternative splicing, single nucleotide polymorphism, and post-translational modifications.
Purpose of the Study:
- To estimate the heterogeneity of the HepG2 proteome.
- To explore the potential of a multi-omics approach for comprehensive proteome analysis.
- To identify aberrant proteoforms in HepG2 cells.
Main Methods:
- Utilized a multi-omics strategy combining transcriptomic (RNAseq) and proteomic (2DE-MS/MS) methods.
- Analyzed HepG2 cell samples to capture a broad spectrum of proteoforms.
- Employed state-of-the-art analytical technologies for data acquisition and analysis.
Main Results:
- The study provides insights into the complexity and heterogeneity of the HepG2 proteome.
- Demonstrated the feasibility of identifying non-canonical proteoforms using the integrated approach.
- Characterized a range of proteoforms, including those resulting from alternative splicing, SNPs, and PTMs.
Conclusions:
- A multi-omics approach integrating RNAseq and 2DE-MS/MS is a powerful strategy for exploring proteome heterogeneity.
- This methodology facilitates the identification of aberrant proteoforms, expanding our understanding of cellular proteomes.
- The findings contribute to a more comprehensive view of the HepG2 proteome, moving beyond canonical sequences.

