Decreased stress inducibility of the HSP68 protein in a rat hepatoma variant clone
| Autor: | Melinda K. Pirity, Olivier Bensaude, Van Trung Nguyen, Marie Francoise Dubois, Aniko Venetianer, Anna Hever-Szabo |
|---|---|
| Rok vydání: | 1992 |
| Předmět: |
medicine.medical_specialty
Hot Temperature Transcription Genetic Arsenites Molecular Sequence Data Biology Biochemistry Arsenic Liver Neoplasms Experimental Transcription (biology) Heat shock protein Internal medicine Tumor Cells Cultured Protein biosynthesis medicine Animals Electrophoresis Gel Two-Dimensional RNA Messenger RNA Neoplasm Gene Cell Nucleus Messenger RNA Reporter gene Base Sequence DNA Neoplasm Blotting Northern Sodium Compounds Molecular biology Clone Cells Neoplasm Proteins Rats DNA-Binding Proteins Blot Kinetics Endocrinology Oligodeoxyribonucleotides Cell culture |
| Zdroj: | European Journal of Biochemistry. 210:793-800 |
| ISSN: | 1432-1033 0014-2956 |
| DOI: | 10.1111/j.1432-1033.1992.tb17482.x |
| Popis: | Analysis of the stress response of closely related rat hepatoma clones revealed that the major inducible heat-shock protein 68 (HSP68) was only slightly inducible upon stress in the glucocorticoid-resistant, dedifferentiated clone-2 cells, but strongly activated in the differentiated, glucocorticoid-sensitive Faza 967 cells from which clone 2 was derived. The decreased inducibility of HSP68 in clone-2 cells was not the consequence of altered kinetics of protein synthesis recovery, was not correlated with the deficient inducibility of other major heat-shock proteins and had no effect on the heat sensitivity of the cells. This deficiency was observed after treatment with mild and strong heat and various chemicals. The results of nuclear run-on experiments suggested that the impairment of HSP68 mRNA induction most likely occurs at the transcriptional level and is probably specific for the corresponding gene. In Faza 967 and clone-2 cells, stress activated comparable levels of heat-shock-factor binding to the heat-shock element, and the expression of a reporter gene under the control of murine HSP70.1 promoter was strongly stimulated in both cells. Therefore, our results raise the possibility that the deficient stress inducibility of HSP68 is due to some specific regulation of the endogeneous HSP68 gene, rather than to a deficiency of the heat-shock factor or mutation of the corresponding gene. |
| Databáze: | OpenAIRE |
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