<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Igarashi Y</submitter><funding>the Japan Society for the Promotion of Science</funding><funding>the Urakami Foundation for Food and Food Culture Promotion</funding><pagination>e0161282</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC4990220</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>11(8)</volume><pubmed_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 o</pubmed_abstract><journal>PloS one</journal><pubmed_title>Possible Contribution of Zerumbone-Induced Proteo-Stress to Its Anti-Inflammatory Functions via the Activation of Heat Shock Factor 1.</pubmed_title><pmcid>PMC4990220</pmcid><funding_grant_id>22.3355</funding_grant_id><funding_grant_id>26450156</funding_grant_id><pubmed_authors>Ohnishi K</pubmed_authors><pubmed_authors>Igarashi Y</pubmed_authors><pubmed_authors>Irie K</pubmed_authors><pubmed_authors>Murakami A</pubmed_authors></additional><is_claimable>false</is_claimable><name>Possible Contribution of Zerumbone-Induced Proteo-Stress to Its Anti-Inflammatory Functions via the Activation of Heat Shock Factor 1.</name><description>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 o</description><dates><release>2016-01-01T00:00:00Z</release><publication>2016</publication><modification>2025-04-04T11:55:24.399Z</modification><creation>2019-03-26T22:54:10Z</creation></dates><accession>S-EPMC4990220</accession><cross_references><pubmed>27536885</pubmed><doi>10.1371/journal.pone.0161282</doi></cross_references></HashMap>