Hyperglycaemia and oxidative stress upregulate HSP60 & HSP70 expression in HeLa cells

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dc.contributor.authorHall, Luke
dc.contributor.authorMartinus, Ryan Dennis
dc.coverage.spatialSwitzerlanden_NZ
dc.date.accessioned2013-10-01T02:09:34Z
dc.date.available2013-10-01T02:09:34Z
dc.date.copyright2013
dc.date.issued2013
dc.description.abstractHeat Shock Proteins 60 & 70 (HSP60 & HSP70) are intracellular protein that has been shown to be present at elevated levels in systemic circulation in Type 2 Diabetes mellitus (T2DM) patients. Conditions that lead to its secretion, and the mechanism of its translocation from cells, have not yet been defined. The aim of this study was to determine if specific cell stressors associated with T2DM, namely hyperglycaemia and oxidative stress, result in the upregulation of HSP60 in human cells in vitro. Human HeLa cells were grown in media supplemented with 100 mM glucose, 200 μM hydrogen peroxide (H₂O₂), and 50 μM sodium azide. Initially, the effect of these treatments on cell growth rate was examined, with each treatment significantly inhibiting growth rate. LDH and MTT assays were also used to successfully demonstrate that these treatments do not significantly increase cell lysis, but do significantly impair mitochondrial dehydrogenase activity. To confirm this mitochondria specific form of inhibition, DCFDA assay were used to investigate any increases in intracellular reactive oxygen species (ROS) generation. All three treatments resulted in significantly increased ROS generation, with greater ROS production occurring with a greater exposure time. Interestingly, when the protein levels of HSP60 and HSP70 were measured after 3 and 7 days of exposure of the HeLa cells to 100 mM glucose, 200 μM H₂O₂, and 50 μM sodium azide significant induction of these two molecular stress proteins were observed ranging from 2.43-5.08 fold compared to untreated control cells.en_NZ
dc.format.mimetypeapplication/pdf
dc.identifier.citationHall, L., Martinus, R. R. (2013). Hyperglycaemia and oxidative stress upregulate HSP60 & HSP70 expression in HeLa cells. SpringerPlus, 2:431.en_NZ
dc.identifier.doi10.1186/2193-1801-2-431en_NZ
dc.identifier.urihttps://hdl.handle.net/10289/8040
dc.language.isoenen_NZ
dc.publisherSpringeren_NZ
dc.relation.isPartOfSpringerPlusen_NZ
dc.relation.ispartofSpringerPlus
dc.relation.urihttp://www.springerplus.com/content/2/1/431/abstracten_NZ
dc.rights© 2013 Hall and Martinus; licensee Springer. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.en_NZ
dc.subjectHSP60en_NZ
dc.subjectHSP70en_NZ
dc.subjectmitochondriaen_NZ
dc.subjectdiabetes mellitusen_NZ
dc.subjectdiabetes mellitusen_NZ
dc.subjectoxidative stressen_NZ
dc.titleHyperglycaemia and oxidative stress upregulate HSP60 & HSP70 expression in HeLa cellsen_NZ
dc.typeJournal Articleen_NZ
pubs.begin-page1en_NZ
pubs.elements-id38843
pubs.end-page20en_NZ
pubs.issue1en_NZ
pubs.volumeonlineen_NZ
uow.identifier.article-noARTN 431en_NZ
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