Related Experiment Video

Updated: Oct 20, 2025

Quantification of Site-specific Protein Lysine Acetylation and Succinylation Stoichiometry Using Data-independent Acquisition Mass Spectrometry
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Quantification of Site-specific Protein Lysine Acetylation and Succinylation Stoichiometry Using Data-independent Acquisition Mass Spectrometry

Published on: April 4, 2018

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Comprehensive analysis of lysine crotonylation modification in patients with chronic renal failure

Jiahuang Huang1, Donge Tang1, Fengping Zheng1

  • 1Clinical Medical Research Center, Guangdong Provincial Engineering Research Center of Autoimmune Disease Precision Medicine, Shenzhen Engineering Research Center of Autoimmune Disease,, The First Affiliated Hospital of Southern University of Science and Technology, Shenzhen People's Hospital,, Guangdong, 518020, Shenzhen, P.R. China.

BMC Nephrology
|September 14, 2021
PubMed
Abstract

Insights

This study reveals altered protein crotonylation in chronic renal failure (CRF) patients, identifying key modifications and pathways. These findings suggest crotonylation

Area of Science:

  • Biochemistry and Molecular Biology
  • Proteomics
  • Renal Physiology

Background:

  • Post-translational modifications (PTMs) regulate protein function and cellular signaling.
  • Crotonylation is a significant PTM involved in diverse biological processes.
  • The role of lysine crotonylation in chronic renal failure (CRF) remains unexplored.

Purpose of the Study:

  • To investigate the global lysine crotonylation proteome in patients with chronic renal failure.
  • To identify differentially crotonylated proteins and associated biological pathways in CRF.

Main Methods:

  • Comparative analysis of crotonylation proteomes between normal controls and CRF patients.
  • Utilized liquid chromatography-tandem mass spectrometry (LC-MS/MS).
  • Employed highly sensitive immune-affinity purification for site identification.

Main Results:

  • Identified 1109 lysine modification sites, with 772 up-regulated and 69 down-regulated in CRF.
  • Crotonylation levels are elevated in CRF patients.
  • Enriched pathways include platelet alpha granule lumen, degranulation, cell adhesion molecule binding, and CD36 signaling, linked to renal failure.

Conclusions:

  • This is the first global analysis of the crotonylation proteome in CRF.
  • Altered crotonylation of histone and non-histone proteins may influence renal function.
  • Potential role of crotonylation in mitigating the progression of chronic kidney disease.
Keywords:
Chronic renal failureCrotonylation ModificationEpigeneticsMass Spectrometry Failure

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