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Expression of Difficult-to-Express Proteins, Human IL-12 and IFN-<i>γ</i>

American Journal of Molecular Biology 2021年第2期11卷 29-37页

作者： Yoshihito Hosaka Shun Matsutani Shinya Kawate Kei Itoh Atsuko Miura Yukaze Mizoura Sayumi Yamada Seiya Uemura Hiroshi Konno ewa grave Hideki Wakui Hideaki Itoh Department of Life Science Graduate School and Faculty of Engineering Science Akita University Akita Japan Akita Konno Co. Ltd. 248 Aza Kariwano Daisen-shi Akita Japan Department of Applied Biological Chemistry Graduate School of Agricultural and Life Sciences The University of Tokyo Tokyo Japan

It is known to be that lactic acid bacteria induce the IL-12. IL-12 activates NK cells and promotes the production of IFN-γ. IFN-γ activates macrophages, resulting in enhanced phagocytosis and bactericidal activity. We have been investigating fermented foods that activate the immune function. For that purpose, a specific antibody is required. We tried to express IL-12p35 by the usual method, but IL-12p35 was not expressed at all. In the present study, we constructed, purified human IL-12p35 and obtained a specific antibody against IL-12p35. We also purified human IFN-γ and obtained specific antibody against IFN-γ. We have established a method for expressing poorly expressed proteins. The method we have established can be applied to the purification of poorly expressed proteins and antibody production.

关键词： Difficult-to-Express Proteins IL-12 IFN-γ Purification Antibody Production

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Cisplatin Inhibits AhR Activation

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American Journal of Molecular Biology 2018年第1期8卷 69-82页

作者： Erina Sasaki-Kudoh Ikuru Kudo Yuka Kakizaki Miki Hosaka Shun-Ichi Ikeda Seiya Uemura ewa grave Shuntaro Togashi Taku Sugawara Hiroaki Shimizu Hideaki Itoh Department of Neurosurgery Akita University Graduate School of Medicine Akita Japan Department of Life Science Akita University Graduate School of Engineering Science Akita Japan Department of Spinal Cord and Spine Surgery Research Institute for Brain and Blood Vessels-Akita Akita Japan

The AhR binds to contain ligands, such as 2, 3, 7, 8-tetrachlorodibenzo-p-dioxin, 3-methylcholantrene, or β-naphthoflavone. The activation mechanism of AhR is not yet fully understood, but it is known that AhR associates with the molecular chaperone HSP90 in the cytoplasm. There are a few reports about the association or dissociation of AhR and HSP90, and which domain of HSP90 binds to AhR. We reported the association and activation mechanisms between HSP90 and AhR-PAS or AhR-bHLH. In the current study, we found that cisplatin inhibits the AhR activation. Although ATP and 17-DMAG have no effect on the dissociation of HSP90 from AhR, some contents of HSP90 were dissociated from AhR in the presence of cisplatin. We could detect the increase of CYP1A in the presence of 3-MC. On the contrary, the induction of CYP1A1 was inhibited in the presence of cisplatin. We couldn’t detect AhR in the HeLa cell soluble fraction in the presence of 50 μM cisplatin. In the presence of MG-132, we could detect AhR. These results suggested that AhR was dissociated from the HSP90 chaperone complex and processed during the protein proteasome degradation system in the presence of cisplatin.

关键词： Cisplatin CDDP AhR Aryl Hydrocarbon Receptor HSP90 17-DMAG

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