1992 Fiscal Year Final Research Report Summary
On the role of heme oxygenase as a oxygen radical scavenger
| Project/Area Number |
03670137
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| Research Category |
Grant-in-Aid for General Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Research Field |
Pathological medical chemistry
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| Research Institution | Yamagata University |
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Principal Investigator |
SATO Michihiko Central Lab. for Res. and Edu. Yamagata Univ. Sch. of Med. Associate Prof., 医学部, 助教授 (00135344)
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| Co-Investigator(Kenkyū-buntansha) |
YOSHIDA Tadashi Dept. of Biochem. Yamagata Univ. Sch. of Med. Prof., 医学部, 教授 (10004673)
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| Project Period (FY) |
1991 – 1992
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| Keywords | heme oxygenase / transcriptional control / stress protein / heat shock protein / cadmium / HSP32 / degradation of heme / ヒートショックタンパク質 |
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| Research Abstract |
Heme oxygenase, a key enzyme of heme degradation, is a major stress-related protein, which is induced with heme, heavy metals, heat shock, organic compounds, UV radiation, hydrogen peroxide and hypoxia. In order to elucidate the transcriptional regulation, we isolated the 4.3 kb 5' flanking region of rat heme oxygenase gene. To localize heme and cadmium responsive elements, various regions of 5' upstream sequence were fused to the cat gene, and a transient expression assay was conducted in the rat glioma cells treated with 10 mu M cadmium chloride or 10 mu M hemin. These studies indicated that the sequence from -3.3/-2.9kb was essential for the induction by cadmium. However, hemin failed to induce cat activity. Using gel sift assay, a DNA-protein complex band was observed only when nuclear extracts prepared from cadmium treated rat (14 mg/kg) were used. Our findings suggested that a transcription factor affected with cadmium binds to the region and regulates the transcription of heme oxygenase gene.
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