Lysine crotonylation is involved in hepatocellular carcinoma progression

Wan, Junhu; Li, Hongyang; Ming, Liang

doi:10.1016/j.biopha.2018.12.148

Cited by 68 publications

(76 citation statements)

References 25 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Cancer is a life‐threatening malignancy that has become a global healthcare problem . Using immunohistochemical methods, we recently reported that levels of crotonylation in eight types of cancer . We found the expression level of crotonylation was down‐regulated in liver, stomach and kidney carcinomas, and up‐regulated in thyroid, oesophagus, colon, pancreas and lung carcinomas, suggesting that crotonylation may modulate different cancer progression.…”

Section: Functional Roles Of Lysine Crotonylationmentioning

confidence: 83%

“…In vivo Interventional study Mice model 2018 42 Regulation of telomere maintenance Cell culture Interventional study MEF cells 2018 44 Regulation of HIV latency Cell culture Interventional study J-Lat A1 and CD4 + T cells 2018 47 Regulation of cancer In vivo and cell culture Interventional study HCC tissues and human hepatoma-derived cell 2019 51 In general, one protein may occur simultaneously multiple PTMs. 53 Indeed, recent years gradually intensifying research on crotonylation and many publications were dedicated to only one of the many possible lysine crotonylations.…”

Section: Regulation Of Depressionmentioning

confidence: 99%

See 1 more Smart Citation

Functions and mechanisms of lysine crotonylation

Wan

Chu

et al. 2019

J Cellular Molecular Medi

Self Cite

View full text Add to dashboard Cite

Lysine crotonylation is a newly discovered post‐translational modification, which is structurally and functionally different from the widely studied lysine acetylation. Recent advances in the identification and quantification of lysine crotonylation by mass spectrometry have revealed that non‐histone proteins are frequently crotonylated, implicating it in many biological processes through the regulation of chromatin remodelling, metabolism, cell cycle and cellular organization. In this review, we summarize the writers, erasers and readers of lysine crotonylation, and their physiological functions, including gene transcription, acute kidney injury, spermatogenesis, depression, telomere maintenance, HIV latency and cancer process. These findings not only point to the new functions for lysine crotonylation, but also highlight the mechanisms by which crotonylation regulates various cellular processes.

show abstract

Section: Functional Roles Of Lysine Crotonylationmentioning

confidence: 83%

Section: Regulation Of Depressionmentioning

confidence: 99%

Functions and mechanisms of lysine crotonylation

Wan

Chu

et al. 2019

J Cellular Molecular Medi

Self Cite

View full text Add to dashboard Cite

show abstract

“…Protein PTM was usually evolutionarily conserved and regulated protein stability, localization, function, protein-protein interaction, and protein-nucleic acid interaction. Omics studies of protein PTM including ubiquitination, methylation, glycosylation, acetylation, crotonylation, and lactylation showed significant difference between tumor and normal samples, which indicated that protein PTM played an important role in cancer development (Zhang et al, 2019;Wan et al, 2019;Zhong and Huang, 2016;Sun et al, 2006;Chen et al, 2018). For example, studies showed that the glycosylation levels of proteins significantly changed in different types of tumor tissues, and some glycosylated proteins were promising biomarkers for diagnosis of HCC at early stage (Wang et al, 2017;Block et al, 2005).…”

Section: Introductionmentioning

confidence: 99%

Lysine Acetylome Study of Human Hepatocellular Carcinoma Tissues for Biomarkers and Therapeutic Targets Discovery

Zhao

Zhang

et al. 2020

Front. Genet.

View full text Add to dashboard Cite

Lysine acetylation is a vital post-translational modification (PTM) of proteins, which plays an important role in cancer development. In healthy human liver tissues, multiple non-histone proteins were identified with acetylation modification, however, the role of acetylated proteins in hepatocellular carcinoma (HCC) development remains largely unknown. Here we performed a quantitative acetylome study of tumor and normal liver tissues from HCC patients. Overall, 598 lysine acetylation sites in 325 proteins were quantified, and almost 59% of their acetylation levels were significantly changed. The differentially acetylated proteins mainly consisted of non-histone proteins located in mitochondria and cytoplasm, which accounted for 42% and 24%, respectively. Bioinformatics analysis showed that differentially acetylated proteins were enriched in metabolism, oxidative stress, and signal transduction processes. In tumor tissues, 278 lysine sites in 189 proteins showed decreased acetylation levels, which occupied 98% of differentially acetylated proteins. Moreover, we collected twenty pairs of tumor and normal liver tissues from HCC male patients, and found that expression levels of SIRT1 (p = 0.002), SIRT2 (p = 0.01), and SIRT4 (p = 0.045) were significantly up-regulated in tumor tissues. Over-expression of possibly accounted for the widespread deacetylation of non-histone proteins identified in HCC tumor tissues, which could serve as promising predictors of HCC. Taken together, our work illustrates abundant differentially acetylated proteins in HCC tumor tissues, and offered insights into the role of lysine acetylation in HCC development. It provided potential biomarker and drug target candidates for clinical HCC diagnosis and treatment.

show abstract

“…However, in our study, no effect of FEZF1-AS1 on the expression level of FEZF1 was found, and we speculated that FEZF1-AS1 promoted the invasion and migration of ESCC cell through other channels. The activation of embryonic epithelial-to-mesenchymal (EMT) program is generally accepted as a vital component of carcinoma progression 33,34. EMT is a complicated process, and molecular reprogramming occurring during EMT is triggered by various factors.…”

Section: Discussionmentioning

confidence: 99%

<p>Long noncoding RNA FEZF1-AS1 promotes the motility of esophageal squamous cell carcinoma through Wnt/β-catenin pathway</p>

Yang

Chu

et al. 2019

CMAR

Self Cite

View full text Add to dashboard Cite

Background: Long noncoding RNAs (lncRNAs), a class of noncoding RNA nucleotides >200 bp, has been demonstrated to play vital role in the development of cancer. FEZ family zinc finger 1 antisense RNA 1 (FEZF1-AS1) has been reported as an lncRNA which acts as a tumor-promoting effect in some cancers. However, the role of it in esophageal squamous cell carcinoma (ESCC) and its potential regulatory mechanism was unclear now. Methods: qRT-PCR was used to detect the levels of FEZF1-AS1 and mRNA CTNNB1 (β-catenin) in ESCC tissues and cells. Cell transfection experiments were used to knock down or overexpress the level of FEZF1-AS1 in EC1 and EC9706 cell lines. WST-1 assays, cell cycle assays, scratch wound assays, migration, and invasion assays were used to evaluate the function of FEZF1-AS1 in ESCC progression. Results: FEZF1-AS1 was remarkably upregulated in ESCC tissues and cell lines. Silencing of FEZF1-AS1 significantly inhibited the migration and invasion of ESCC cells, while overexpression of FEZF1-AS1 notably accelerated ESCC migration and invasion. Meanwhile, the levels of FEZF1-AS1 had no effect on ESCC cell proliferation and cell cycle. We also found that β-catenin was upregulated in ESCC tissues, and the level of it was positively correlated with the expression of FEZF1-AS1. Silencing of FEZF1-AS1 could decrease the mRNA and protein level of β-catenin, while overexpression FEZF1-AS1 could lead to the contrary. Conclusion: Our results suggested that the expression of lncRNA FEZF1-AS1 played an important role in ESCC progression, especially the motility of the tumor. FEZF1-AS1 may provide us with a new sight for ESCC treatment.

show abstract

Lysine crotonylation is involved in hepatocellular carcinoma progression

Cited by 68 publications

References 25 publications

Functions and mechanisms of lysine crotonylation

Functions and mechanisms of lysine crotonylation

Lysine Acetylome Study of Human Hepatocellular Carcinoma Tissues for Biomarkers and Therapeutic Targets Discovery

<p>Long noncoding RNA FEZF1-AS1 promotes the motility of esophageal squamous cell carcinoma through Wnt/β-catenin pathway</p>

Contact Info

Product

Resources

About