Effects of acrylamide on protein degradation pathways in human liver-derived cells and the efficacy of N-acetylcysteine and curcumin

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dc.authoridOZGUN, ERAY/0000-0002-6744-1519
dc.contributor.authorAl-Hajm, Abdullah Yahya Salih
dc.contributor.authorOzgun, Eray
dc.date.accessioned2024-06-12T10:50:29Z
dc.date.available2024-06-12T10:50:29Z
dc.date.issued2022
dc.departmentTrakya Üniversitesien_US
dc.description.abstractAcrylamide is a harmful chemical, and its metabolism occurs mainly in the liver. Acrylamide can form adducts on proteins. Protein homeostasis is vital for metabolic and secretory functions of the liver. No study has investigated the effect of acrylamide on the ubiquitin-proteasome system (UPS). Also, the effect of acrylamide on autophagy and its regulation is not fully known. We aimed to investigate the effects of acrylamide on the UPS, autophagy, mammalian target of rapamycin (mTOR), and heat shock protein 70 (HSP70) in HepG2 cells as well as to examine the effects of N-acetylcysteine and curcumin on these parameters in acrylamide-treated cells. HepG2 cells were initially treated with variable concentrations of acrylamide (0.01-0.1-1-10 mM) for 24 hours. Then, HepG2 cells were treated with 5 mM N-acetylcysteine and 6.79 mu M curcumin in the presence of 10 mM acrylamide for 24 hours. Cell viability was evaluated by 3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H-tetrazolium bromide assay. Ubiquitinated protein, mTOR, microtubule-associated proteins 1 A/1B light chain 3B-II (LC3B-II), and HSP70 levels were measured by immunoblotting. Acrylamide at 10 mM concentration, without any significant change at lower concentrations, caused an increase in ubiquitinated protein, LC3B-II, and HSP70 levels and a decrease in mTOR phosphorylation. Furthermore, 5 mM N-acetylcysteine caused a decrease in ubiquitinated protein and HSP70 levels; however, 6.79 mu M curcumin did not affect 10 mM in acrylamide-treated cells. Our study showed that acrylamide at high concentration inhibits UPS and mTOR, activates autophagy, and increases HSP70 levels in HepG2 cells, and N-acetylcysteine reduces UPS inhibition and HSP70 levels in acrylamide-treated cells.en_US
dc.description.sponsorshipScientific Research Appropriation of Trakya University - Turkey [TUBAP 2018/265]en_US
dc.description.sponsorshipThis study was supported by Scientific Research Appropriation of Trakya University - Turkey under grant number [TUBAP 2018/265].en_US
dc.identifier.doi10.1080/01480545.2020.1846548
dc.identifier.endpage1543en_US
dc.identifier.issn0148-0545
dc.identifier.issn1525-6014
dc.identifier.issue4en_US
dc.identifier.pmid33198515en_US
dc.identifier.scopus2-s2.0-85096124954en_US
dc.identifier.scopusqualityQ2en_US
dc.identifier.startpage1536en_US
dc.identifier.urihttps://doi.org/10.1080/01480545.2020.1846548
dc.identifier.urihttps://hdl.handle.net/20.500.14551/18009
dc.identifier.volume45en_US
dc.identifier.wosWOS:000589846500001en_US
dc.identifier.wosqualityQ2en_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.indekslendigikaynakScopusen_US
dc.indekslendigikaynakPubMeden_US
dc.language.isoenen_US
dc.publisherTaylor & Francis Ltden_US
dc.relation.ispartofDrug And Chemical Toxicologyen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectAcrylamideen_US
dc.subjectLiveren_US
dc.subjectHepg2 Cell Lineen_US
dc.subjectUbiquitin-Proteasome Systemen_US
dc.subjectAutophagyen_US
dc.subjectMammalian Target Of Rapamycinen_US
dc.subjectHeat Shock Protein 70en_US
dc.subjectN-Acetylcysteineen_US
dc.subjectCurcuminen_US
dc.subjectUbiquitin-Proteasome Systemen_US
dc.subjectHeat-Shock Proteinsen_US
dc.subjectHepg2 Cellsen_US
dc.subjectToxicityen_US
dc.subjectDysfunctionen_US
dc.subjectInhibitionen_US
dc.subjectApoptosisen_US
dc.subjectReleaseen_US
dc.subjectCanceren_US
dc.titleEffects of acrylamide on protein degradation pathways in human liver-derived cells and the efficacy of N-acetylcysteine and curcuminen_US
dc.typeArticleen_US

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