In vivo quantitative proteomics for the study of oncometabolism

Area of Science:

• Biochemistry
• Molecular Biology
• Oncology

Background:

• Cellular metabolism reprogramming drives oncogenesis.
• Metabolic enzyme expression and post-translational modifications (PTMs) are crucial.
• Understanding these changes is key to cancer research.

Purpose of the Study:

• To describe a proteomic approach for comparing protein levels and phosphorylation status.
• To utilize Stable Isotope Labeling of Amino Acids in Culture (SILAC) for in-depth proteomic quantification.
• To investigate oncometabolism and proteomic alterations in cancer progression.

Main Methods:

• Stable Isotope Labeling of Amino Acids in Culture (SILAC) for comparative protein assessment.
• Mass spectrometry (MS) for analyzing protein levels and PTMs.
• High-resolution chromatography and high-accuracy MS for detailed proteomic analysis.

Main Results:

• Accurate and in-depth quantification of proteomes from various cell and tissue samples.
• Ability to infer the metabolic state of neoplastic lesions.
• Profound understanding of proteomic alterations during oncogenesis and tumor progression.

Conclusions:

• The described SILAC-based proteomic approach enables precise comparison of protein levels and phosphorylation.
• This method is applicable to murine tissues, cellular samples, and human specimens.
• It offers a powerful tool for studying oncometabolism and cancer-related proteomic changes.