Expression, synthesis, and phosphorylation of HSP28 family during development and decay of thermotolerance in CHO plateau-phase cells
Autor: | Yong J. Lee, Lindali Curetty, Zi-Zheng Hou, Peter M. Corry |
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Rok vydání: | 1992 |
Předmět: |
Silver
Physiology Clinical Biochemistry Gene Expression Hamster CHO Cells Biology Cricetinae Heat shock protein Gene expression medicine Animals Electrophoresis Gel Two-Dimensional Phosphorylation Heat-Shock Proteins Messenger RNA Staining and Labeling Cell growth Temperature Cell Biology Blotting Northern Molecular biology Kinetics Multigene Family Shock (circulatory) medicine.symptom Cell Division Intracellular |
Zdroj: | Journal of Cellular Physiology. 150:441-446 |
ISSN: | 1097-4652 0021-9541 |
Popis: | We investigated a correlation between development of thermotolerance and expression, synthesis, or phosphorylation of HSP28 family in CHO plateau phase cells. After heating at 45.5 degrees C for 10 min, thermotolerance developed rapidly and reached its maximum 12-18 hr after heat shock. This acquired thermal resistance was maintained for 72 hr and then gradually decayed. In parallel, the levels of three 28 kDa heat shock proteins, HSP28a along with its two phosphorylated isoforms (HSP28b,c), increased and reached their maximum 24-48 hr after heat shock. The levels of these polypeptides, except HSP28c, remained elevated for 72 hr and then decreased. The level of HSP28 mRNA increased rapidly and reached its maximum 12 hr after heat shock. However, unlike thermotolerance and the levels of HSP28 family proteins, the level of HSP28 mRNA decreased rapidly within 72 hr. These results demonstrate a correlation between the amount of intracellular HSP28 family proteins and development and decay of thermotolerance. |
Databáze: | OpenAIRE |
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