{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,12,12]],"date-time":"2025-12-12T13:15:13Z","timestamp":1765545313652},"reference-count":44,"publisher":"Wiley","issue":"1","license":[{"start":{"date-parts":[[2005,2,4]],"date-time":"2005-02-04T00:00:00Z","timestamp":1107475200000},"content-version":"vor","delay-in-days":5788,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Journal Cellular Physiology"],"published-print":{"date-parts":[[1989,4]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Many recent studies have suggested that heat and other inducers of the heat shock (stress) response in eukaryotic cells might result in the generation of abnormal proteins which would result in the overloading of protein degradation systems and the stabilization of proteins involved in positively regulating heat shock (hs) gene expression. In this study we have examined the effects different heat treatments and other hs inducers have on protein degradation in Chinese hamster ovary (CHO) and <jats:italic>Drosophila<\/jats:italic> Kc and Schneider cells. We have found that intermediate temperatures which induced the hs response (42\u00b0C in CHO and 34\u00b0C in Kc cells) did increase protein degradation rates whereas, higher temperatures which also induced the hs response (45\u00b0C in CHO and 37\u00b0C in Kc cells) initially increased but then decreased protein degradation rates. While these results are consistent with a model in which the protein degradation system is being overloaded and\/or components of it are being depleted, we have found several conditions which induce hs proteins which rule out this mechanism. Exposure of either cell type to amino acid analogs (5mM canavanine or 5 mM S\u2010aminoethyl cysteine) resulted in the rapid degradation of those proteins which had incorporated the analogs in both CHO and <jats:italic>Drosophila<\/jats:italic> cells. However, the addition of analogs had little or no effect on the degradation of preexisting proteins, indicating that the introduction of abnormal proteins probably didn't overload the protein degradation system(s). The addition of 100 (\u03bc)M cadmium sulfate or 100 (\u03bc)M sodium arsenite had little or no effect on protein degradation rates in CHO cells even though both were good inducers of the hs proteins. Thus, exposure to inducers of the hs response does not universally increase protein degradation rates nor does it stabilize preexisting proteins. Therefore, the degradation of abnormal proteins is probably not involved in inducing the hs genes.<\/jats:p>","DOI":"10.1002\/jcp.1041390127","type":"journal-article","created":{"date-parts":[[2005,2,26]],"date-time":"2005-02-26T10:08:39Z","timestamp":1109412519000},"page":"196-209","source":"Crossref","is-referenced-by-count":13,"title":["Effects of heat and other inducers of the stress response on protein degradation in Chinese hamster and <i>Drosophila<\/i> cells"],"prefix":"10.1002","volume":"139","author":[{"given":"J. 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