ArticlePloS one2016
Possible Contribution of Zerumbone-Induced Proteo-Stress to Its Anti-Inflammatory Functions via the Activation of Heat Shock Factor 1.
Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed, 19 citations in OpenAlex.
- HnRNP K regulates inflammatory gene expression by mediating splicing pattern of transcriptional factors.Experimental biology and medicine (Maywood, N.J.) · 2023Article
- Role of heat shock protein 70 in regulation of anti-inflammatory response to curcumin in 3T3-L1 adipocytes.Nutrition research and practice · 2023Article
- Modulation of the tumor microenvironment by natural agents: implications for cancer prevention and therapy.Seminars in cancer biology · 2022Review
- Curcumin may induce lipolysis via proteo-stress in Huh7 human hepatoma cells.Journal of clinical biochemistry and nutrition · 2019Article
- Covalent adduction of endogenous and food-derived quinones to a protein: its biological significance.Journal of clinical biochemistry and nutrition · 2018Review
- Non-specific protein modifications may be novel mechanism underlying bioactive phytochemicals.Journal of clinical biochemistry and nutrition · 2018Review
- A Review of the Biomedical Applications of Zerumbone and the Techniques for Its Extraction from Ginger Rhizomes.Molecules (Basel, Switzerland) · 2017Review
- Immunosuppressive Effects of Natural α,β-Unsaturated Carbonyl-Based Compounds, and Their Analogs and Derivatives, on Immune Cells: A Review.Frontiers in pharmacology · 2017Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Zerumbone is a sesquiterpene present in Zinger zerumbet. Many studies have demonstrated its marked anti-inflammatory and anti-carcinogenesis activities. Recently, we showed that zerumbone binds to numerous proteins with scant selectivity and induces the expression of heat shock proteins (HSPs) in hepatocytes. To dampen proteo-toxic stress, organisms have a stress-responsive molecular machinery, known as heat shock response. Heat shock factor 1 (HSF1) plays a key role in this protein quality control system by promoting activation of HSPs. In this study, we investigated whether zerumbone-induced HSF1 activation contributes to its anti-inflammatory functions in stimulated macrophages. Our findings showed that zerumbone increased cellular protein aggregates and promoted nuclear translocation of HSF1 for HSP expression. Interestingly, HSF1 down-regulation attenuated the suppressive effects of zerumbone on mRNA and protein expressions of pro-inflammatory genes, including inducible nitric oxide synthase and interlukin-1β. These results suggest that proteo-stress induced by zerumbone activates HSF1 for exhibiting its anti-inflammatory functions.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.