Regulation of HSP70 and HSP28 gene expression: absence of compensatory interactions
Autor: | Geza Erdos, Peter M. Corry, Yong J. Lee, Stephen W. Carper, Lindali Curetty, Joong M. Cho, Jannifer S. Stromberg, Zi-Zheng Hou |
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Rok vydání: | 1994 |
Předmět: |
Clinical Biochemistry
Blotting Western HSP30 Heat-Shock Proteins Molecular Sequence Data Biology Transfection Mice L Cells Western blot Heat Shock Transcription Factors Heat shock protein Gene expression medicine Animals Humans Electrophoresis Gel Two-Dimensional HSP70 Heat-Shock Proteins Northern blot Promoter Regions Genetic Molecular Biology Heat-Shock Proteins Regulation of gene expression medicine.diagnostic_test Base Sequence Membrane Proteins Cell Biology General Medicine Blotting Northern Molecular biology Recombinant Proteins Hsp70 Heat shock factor DNA-Binding Proteins Gene Expression Regulation Oligodeoxyribonucleotides Transcription Factors |
Zdroj: | Molecular and cellular biochemistry. 137(2) |
ISSN: | 0300-8177 |
Popis: | We have previously reported the lack of HSP28 gene expression during acute and chronic thermotolerance development in L929 cells (J Cell Physiol 152: 118-125, 1992; Cancer Res 52: 5787, 1992). In contrast to HSP28, an extremely high level of inducible HSP70 synthesis was observed. These results led us to investigate the possibility of compensatory interactions between HSP70 and HSP28. To test the hypothesis, L929 cells were transfected with the human HSP28 gene contained in plasmid pCMV27. Data from Western blot and two-dimensional gel electrophoresis of [3H] leucine and [32P] orthophosphate-labeled proteins showed the synthesis and phosphorylation of HSP28 in transfected cells after heating at 45 degrees C for 10 min. However, the expression of constitutive and inducible HSP70 genes, along with the synthesis of their proteins, was not decreased after heat shock. These results suggest an independent regulation of HSP28 and HSP70 gene expression. |
Databáze: | OpenAIRE |
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