Comprehensive Characterization of Protein Turnover by Comparative SILAC Labeling Analysis in 3T3-L1

J Proteome Res. 2023 Jun 2;22(6):1723-1733. doi: 10.1021/acs.jproteome.2c00763. Epub 2023 Apr 14.

Abstract

A balance between the synthesis and degradation of proteins is referred to as protein turnover, which is crucial for cellular protein homeostasis. Proteome-wide analysis of protein turnover in adipocytes, which are well-known for their role in energy storage and their link to obesity and metabolism disorders, is yet to be conducted. Thus, with this objective in mind, our investigation utilized a comparative analysis of time-dependent SILAC labeling to assess protein turnover in 3T3-L1 adipocytes, spanning a period of 0 to 144 h. We observed that relatively faster or slower protein half-lives in several protein groups were associated with the PPARγ signaling pathway, energy metabolism, extracellular matrix, ubiquitin-proteasome system, RNA splicing, Golgi complex, and lysosome. It is anticipated that these protein half-life profiles will provide greater clarity on the life cycle of adipocyte proteome and shed light on how they maintain protein homeostasis.

Keywords: SILAC; adipocytes; mass spectrometry; protein turnover; proteomics.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 3T3-L1 Cells
  • Adipocytes* / metabolism
  • Animals
  • Cell Differentiation
  • Mice
  • Proteasome Endopeptidase Complex / metabolism
  • Proteolysis
  • Proteome* / genetics
  • Proteome* / metabolism

Substances

  • Proteome
  • Proteasome Endopeptidase Complex