| Project/Area Number |
09672043
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Surgical dentistry
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| Research Institution | Nagoya University |
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Principal Investigator |
HAYASHI Yasushi School of Medicine, Nagoya University Assistant Proffessor, 医学部, 講師 (10238131)
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| Co-Investigator(Kenkyū-buntansha) |
KANEKO Ryuji School of Medicine, Assistant Proffessor, 医学部, 助手 (50293692)
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| Project Period (FY) |
1997 – 1998
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| Project Status |
Completed (Fiscal Year 1998)
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| Budget Amount *help |
¥3,000,000 (Direct Cost: ¥3,000,000)
Fiscal Year 1998: ¥900,000 (Direct Cost: ¥900,000)
Fiscal Year 1997: ¥2,100,000 (Direct Cost: ¥2,100,000)
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| Keywords | hyperthermia / heat shock protein / Hsp 70 / Hsp 40 / apoptosis / stress proteins / molecular chaperone / OK-432 / 温耐耐性 / 熱ショック蛋白質 / hsp70 / hsp40 |
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| Research Abstract |
The molecular mechanism for translent developmental thermotolerance is still obscue, but many studies suggest that heat shock proteins (Hsps), especially Hsp70, are involved in the development thermotolerance. The correlation between Hsps and thermotolerance has been extensively studied in in vitro systems using cultured mammalian cells so far. We investigated the relationship between Hsp40/Hsp70 synthesis and the development of thermotolerance using mouse squamous cell carcinoma in vivo. These results obtained in vivo were very similar to those in vitro. Next We examine the induction of apotosis on hyperthermia using transplanted mouse tumor. These results suggested that the induction of apotosis is closely related to the cell death caused by hyperthermia. And the antitumor effect of hyperthermia and OK-432 therapy is not ascribable to the induction of apotosis. Furthermore we investigated the induction of mammalian Hsp40 by various enviromental stresses in HeLa cells and the constitutive expression of Hsp40 in adult mouse tissues in comparison with those of Hsp70. induction pattems of Hsp40 and Hsp70 were very similar. Heat shock was the most effective. Azetidine carboxylic acid, sodium arsenite and ethanol were moderate stresses for the induction Hsps. lnterestingly, dinitrophenol and hydrogen peroxide could induce Hsp40 but not Hsp70. These results suggest differential regulation of the transcriptional activation between Hsp40 and Hsp70. Both Hsp40 and Hsp70 were expressed in all mouse tissues examined with some variation. However, Hsp40 was expressed in the testies at remarkably higher level as compared with other tissues. These results suggested that both Hsp70 and Hsp40 are ubiquitously expressed and have essential and indispensable functions as molecular chaperones and that Hsp40 in the testies might have some specific function in addition to the molecular chaperone activity.
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