J. Biochem, 1990, Vol. 108, No. 1 28-32
© 1990 Japanese Biochemical Society
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Induction in Mouse Peritoneal Macrophages of 34 kDa Stress Protein and Heme Oxygenase by Sulfhydryl-Reactive Agents1
*Department of Hygiene, Kansai Medical University Moriguchi, Osaka 570
**Department of Biochemistry, Tsukuba University Medical School Tsukuba, Ibaraki 305
***Department of Public Health, Faculty of Medicine, Kyoto University Sakyo-ku, Kyoto, Kyoto 606
2To whom correspondence should be addressed
The synthesis of 34-kDa stress protein was enhanced, with a simultaneous increase in heme oxygenase activity, when mouse macrophages were exposed to diethylmaleate or sodium arsenite. After 7 h of exposure to the sulfhydryl agents, the 34-kDa protein was the most actively synthesized protein. Immunoblot analysis showed that the induced 34-kDa protein reacted with an antibody raised against bovine heme oxygenase. Cadmium ions or 1-chloro-2,4-dinitrobenzene also induced the 34-kDa protein which reacted with the antibody. Treatments of the cells with buthionine sulfoximine or hydrogen peroxide weakly induced the protein, while diamide treatment or heat shock was without effect. These results are consistent with our previous findings that heavy metal ions including arsenite and cadmium ions induce heme oxygenase (32-kDa stress protein) in human cell lines [Taketani, S., Kohno, H., Yoshinaga, T., & Tokunaga, R. (1989) FEBS Lett 245,173–176], and also suggest that the formation of glutathione conjugate with sulfhydryl-reactive agents may mediate the induction of the stress protein in mouse peritoneal macrophages.
1This study was supported in part by a Grant-in-Aid for Scientific Research from the Ministry of Education, Science and Culture of Japan and a grant from the Fugaku Trust for medicinal research.
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