ArticleScientific reports2017
Proteomic analysis of proteome and histone post-translational modifications in heat shock protein 90 inhibition-mediated bladder cancer therapeutics.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 57 citations in OpenAlex.
- Succinylation: A Functional Nexus Between Metabolic Reprogramming and Epigenetic Modifications in Cancer.Molecules (Basel, Switzerland) · 2026Review
- The role of post-translational modifications in osteonecrosis of the femoral head.Frontiers in cell and developmental biology · 2026Review
- Unlocking the Hidden Potential of Cancer Therapy Targeting Lysine Succinylation.Journal of Cancer · 2025Review
- Molecular mechanism of anticancer effect of heat shock protein 90 inhibitor BIIB021 in human bladder cancer cell line.Naunyn-Schmiedeberg's archives of pharmacology · 2024Article
- A glimpse into novel acylations and their emerging role in regulating cancer metastasis.Cellular and molecular life sciences : CMLS · 2024Review
- The Role of Emodin in the Treatment of Bladder Cancer Based on Network Pharmacology and Experimental Verification.Combinatorial chemistry & high throughput screening · 2024Article
- Investigating the role of HSP90 in cancer cell phenotypic plasticity.Journal of breast cancer research · 2024Article
- Functions and mechanisms of protein lysine butyrylation (Kbu): Therapeutic implications in human diseases.Genes & diseases · 2023Review
- Protein post-translational modification by lysine succinylation: Biochemistry, biological implications, and therapeutic opportunities.Genes & diseases · 2023Review
- Epigenetic and Immunological Features of Bladder Cancer.International journal of molecular sciences · 2023Review
- Hsp90 mutants with distinct defects provide novel insights into cochaperone regulation of the folding cycle.PLoS genetics · 2023Article
- The APE2 Exonuclease Is a Client of the Hsp70-Hsp90 Axis in Yeast and Mammalian Cells.Biomolecules · 2022Article
- Oncometabolites drive tumorigenesis by enhancing protein acylation: from chromosomal remodelling to nonhistone modification.Journal of experimental & clinical cancer research : CR · 2022Review
- A prognostic signature based on cuprotosis-related long non-coding RNAs predicts the prognosis and sensitivity to chemotherapy in patients with colorectal cancer.Frontiers in medicine · 2022Article
- TargetingFrontiers in oncology · 2022Review
- Methylation of histone H3 at lysine 37 by Set1 and Set2 prevents spurious DNA replication.Molecular cell · 2021Article
- Histone citrullination: a new target for tumors.Molecular cancer · 2021Review
- Identification of Predictive Biomarkers of Response to HSP90 Inhibitors in Lung Adenocarcinoma.International journal of molecular sciences · 2021Article
- Article
- Up-Regulating ERIC by CRISPR-dCas9-VPR Inhibits Cell Proliferation and Invasion and Promotes Apoptosis in Human Bladder Cancer.Frontiers in molecular biosciences · 2021Article
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Authors and funding
9 authors at 3 institutions in 1 country.
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Abstract
Heat shock protein 90 (HSP90) inhibition is an attractive strategy for cancer treatment. Several HSP90 inhibitors have shown promising effects in clinical oncology trials. However, little is known about HSP90 inhibition-mediated bladder cancer therapy. Here, we report a quantitative proteomic study that evaluates alterations in protein expression and histone post-translational modifications (PTMs) in bladder carcinoma in response to HSP90 inhibition. We show that 5 HSP90 inhibitors (AUY922, ganetespib, SNX2112, AT13387, and CUDC305) potently inhibited the proliferation of bladder cancer 5637 cells in a dose- and time-dependent manner. Our proteomic study quantified 518 twofold up-regulated and 811 twofold down-regulated proteins common to both AUY922 and ganetespib treatment. Bioinformatic analyses revealed that those differentially expressed proteins were involved in multiple cellular processes and enzyme-regulated signaling pathways, including chromatin modifications and cell death-associated pathways. Furthermore, quantitative proteome studies identified 14 types of PTMs with 93 marks on the core histones, including 34 novel histone marks of butyrylation, citrullination, 2-hydroxyisobutyrylation, methylation, O-GlcNAcylation, propionylation, and succinylation in AUY922- and ganetespib-treated 5637 cells. Together, this study outlines the association between proteomic changes and histone PTMs in response to HSP90 inhibitor treatment in bladder carcinoma cells, and thus intensifies the understanding of HSP90 inhibition-mediated bladder cancer therapeutics.
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