Open Access

Quantitative analysis of protein crotonylation identifies its association with immunoglobulin A nephropathy

  • Authors:
    • Hua Lin
    • Donge Tang
    • Yong Xu
    • Ruohan Zhang
    • Minglin Ou
    • Fengping Zheng
    • Jiejing Chen
    • Yue Zhang
    • Guimian Zou
    • Wen Xue
    • Yaoshuang Zou
    • Weier Dai
    • Weiguo Sui
    • Yong Dai
  • View Affiliations

  • Published online on: January 13, 2020     https://doi.org/10.3892/mmr.2020.10931
  • Pages: 1242-1250
  • Copyright: © Lin et al. This is an open access article distributed under the terms of Creative Commons Attribution License.

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Abstract

Posttranslational modifications (PTMs) to histones such as lysine crotonylation are classified as epigenetic changes. Lysine crotonylation participates in various cellular processes and occurs in active promoters, directly accelerating transcription. The present study performed a proteomics analysis of crotonylation between healthy controls and patients with immunoglobulin A (IgA) nephropathy using tandem mass spectrometry and high‑resolution liquid chromatography. The present results identified 353 crotonylated proteins and 770 modification sites, including 155 upregulated and 198 downregulated crotonylated proteins. In total, seven conserved motifs were identified in the present study. The present bioinformatics analysis results suggested a number of the crotonylated proteins exhibited various subcellular localization patterns, such as in the cytoplasm. Protein domains, including thioredoxin, moesin tail and myosin like IQ motif domains were markedly enriched in crotonylated proteins. Kyoto Encyclopedia of Genes and Genomes and functional enrichment analyses suggested significant enrichment of crotonylated proteins in complement and coagulation cascades, and antigen processing and presentation pathways displaying important relationships with IgA nephropathy. The present results suggested that crotonylation occurred in numerous proteins and may play key regulatory roles in IgA nephropathy.
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March 2020
Volume 21 Issue 3

Print ISSN: 1791-2997
Online ISSN:1791-3004

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APA
Lin, H., Tang, D., Xu, Y., Zhang, R., Ou, M., Zheng, F. ... Dai, Y. (2020). Quantitative analysis of protein crotonylation identifies its association with immunoglobulin A nephropathy. Molecular Medicine Reports, 21, 1242-1250. https://doi.org/10.3892/mmr.2020.10931
MLA
Lin, H., Tang, D., Xu, Y., Zhang, R., Ou, M., Zheng, F., Chen, J., Zhang, Y., Zou, G., Xue, W., Zou, Y., Dai, W., Sui, W., Dai, Y."Quantitative analysis of protein crotonylation identifies its association with immunoglobulin A nephropathy". Molecular Medicine Reports 21.3 (2020): 1242-1250.
Chicago
Lin, H., Tang, D., Xu, Y., Zhang, R., Ou, M., Zheng, F., Chen, J., Zhang, Y., Zou, G., Xue, W., Zou, Y., Dai, W., Sui, W., Dai, Y."Quantitative analysis of protein crotonylation identifies its association with immunoglobulin A nephropathy". Molecular Medicine Reports 21, no. 3 (2020): 1242-1250. https://doi.org/10.3892/mmr.2020.10931