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자료유형
학술저널
저자정보
Woo, Sang-Hyeok (Department of Molecular Biology, Pusan National University) Oh, Su-Young (Department of Molecular Biology, Pusan National University) Han, Song-Iy (Department of Molecular Biology, Pusan National University) Choi, Yung-Hyun (Department of Oriental Medicine, Dong-eui University) Kang, Kwang-Il (Department of Oriental Medicine, Dong-eui University) Yoo, Mi-Ae (Department of Molecular Biology, Pusan National University) Kim, Han-Do (Department of Molecular Biology, Pusan National University) Kang, Ho-Sung (Department of Molecular Biology, Pusan National University)
저널정보
한국통합생물학회 Korean journal of biological sciences Korean journal of biological sciences 제4권 제2호
발행연도
2000.1
수록면
181 - 186 (6page)

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The expression of $p21^{WAF1/ClP1/SDl1}$, one of the cyclin-dependent kinase inhibitors, is regulated by a variety of transcription factors including p53 and STAT. Heat shock induces the expression of p21 in a temperature- and time-dependent manner. Although the p21 induction by heat shock has been reported to be controlled by p53, a p53-independent mechanism Is also involved. To understand the p53-independent regulation of heat shock-induced p21 expression, we searched the promoter region of p21 gene and found one or two heat shock element (HSE)-like sequences in human, rat, and mouse. Electromobility shift assay (EMSA) showed that heat shock factor (HSF) could bind to these HSE-like sequences In response to heat shock, even though to a lesser extent than to HSE. In addition, p21 promoter deletion analysis revealed that heat shock activated a p21 deletion promoter construct containing the HSE-like sequences but lacking p53-binding sites, but not a promoter construct containing neither HSE-like sequences nor the p53-responsive element. Furthermore, the p21 induction by heat shook was significantly inhibited in confluent cells in which heat shock-induced HSF activation was reduced. These results suggest that the transcriptional regulation of p21 by heat shock may be mediated through activation and binding to HSE-like sequences of HSF.

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