Diamide-induced cytotoxicity and thermotolerance in CHO cells

✍ Scribed by Michael J. Borrelli; Diane M. Stafford; Cynthia M. Rausch; Laura J. Bernock; Michael L. Freeman; James R. Lepock; Peter M. Corry

• Publisher: John Wiley and Sons
• Year: 1998
• Tongue: English
• Weight: 234 KB
• Volume: 177
• Category: Article
• ISSN: 0021-9541
• DOI: 10.1002/(sici)1097-4652(199812)177:3<483::aid-jcp11>3.0.co;2-h

✦ Synopsis

Treatment with the sulfhydryl oxidant diamide denatures and aggregates cellular proteins, which prior studies have implicated as an oxidative damage that activates the heat shock transcription factor and induces thermotolerance. This study was initiated to further characterize cellular response to diamide-denatured proteins, including their involvement in diamide cytotoxicity. Cytotoxic diamide exposures at 37.0ЊC denatured and aggregated cellular proteins in a manner that was proportional to cell killing, but this correlation was different than that established for heated cells. Diamide exposures at 24.0ЊC were orders of magnitude less cytotoxic, with little additional killing occurring after diamide was removed and cells were returned to 37.0ЊC. Thus, protein denaturation that occurred at 37.0ЊC, after proteins were chemically destabilized by diamide at 24.0ЊC [