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Your search keyword '"Ikekita, Masahiko"' showing total 254 results
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254 results on '"Ikekita, Masahiko"'

1. Plakevulin a Induces Apoptosis and Suppresses Il-6-Induced Stat3 Activation in Hl60 Cells

Author

Kabasawa, Misaki, primary, Furuta, Masateru, additional, Ibayashi, Yuuka, additional, Kanemaru, Kaori, additional, Kohatsu, Haruki, additional, Kuramochi, Fumiyo, additional, Yamatoya, Kenji, additional, Nakata, Kazuya, additional, Nakamura, Yoshikazu, additional, Tomoshige, Shusuke, additional, Ohgane, Kenji, additional, Furuyama, Yuuki, additional, Takasawa, Ryoko, additional, Kobayashi, Susumu, additional, Sugawara, Fumio, additional, Ikekita, Masahiko, additional, and Kuramochi, Kouji, additional

Published
2024
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2. Epo-C12 inhibits peroxiredoxin 1 peroxidase activity

Author

Yoda, Tomoka, Furuta, Masateru, Tsutsumi, Tomohiko, Ikeda, Seiki, Yukizawa, Shunsuke, Arai, Satoshi, Morita, Akinori, Yamatoya, Kenji, Nakata, Kazuya, Tomoshige, Shusuke, Ohgane, Kenji, Furuyama, Yuuki, Sakaguchi, Kengo, Sugawara, Fumio, Kobayashi, Susumu, Ikekita, Masahiko, and Kuramochi, Kouji

Published
2021
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5. Supplementary Methods, Figure Legends 1-6 from Sodium Orthovanadate Inhibits p53-Mediated Apoptosis

Author

Morita, Akinori, primary, Yamamoto, Shinichi, primary, Wang, Bing, primary, Tanaka, Kaoru, primary, Suzuki, Norio, primary, Aoki, Shin, primary, Ito, Azusa, primary, Nanao, Tomohisa, primary, Ohya, Soichiro, primary, Yoshino, Minako, primary, Zhu, Jin, primary, Enomoto, Atsushi, primary, Matsumoto, Yoshihisa, primary, Funatsu, Osamu, primary, Hosoi, Yoshio, primary, and Ikekita, Masahiko, primary

Published
2023
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6. Supplementary Methods, Figures 1-6 from Sodium Orthovanadate Inhibits p53-Mediated Apoptosis

Author

Morita, Akinori, primary, Yamamoto, Shinichi, primary, Wang, Bing, primary, Tanaka, Kaoru, primary, Suzuki, Norio, primary, Aoki, Shin, primary, Ito, Azusa, primary, Nanao, Tomohisa, primary, Ohya, Soichiro, primary, Yoshino, Minako, primary, Zhu, Jin, primary, Enomoto, Atsushi, primary, Matsumoto, Yoshihisa, primary, Funatsu, Osamu, primary, Hosoi, Yoshio, primary, and Ikekita, Masahiko, primary

Published
2023
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7. Data from Sodium Orthovanadate Inhibits p53-Mediated Apoptosis

Author

Morita, Akinori, primary, Yamamoto, Shinichi, primary, Wang, Bing, primary, Tanaka, Kaoru, primary, Suzuki, Norio, primary, Aoki, Shin, primary, Ito, Azusa, primary, Nanao, Tomohisa, primary, Ohya, Soichiro, primary, Yoshino, Minako, primary, Zhu, Jin, primary, Enomoto, Atsushi, primary, Matsumoto, Yoshihisa, primary, Funatsu, Osamu, primary, Hosoi, Yoshio, primary, and Ikekita, Masahiko, primary

Published
2023
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8. Supplementary Figure 4 from Sodium Orthovanadate Inhibits p53-Mediated Apoptosis

Author

Morita, Akinori, primary, Yamamoto, Shinichi, primary, Wang, Bing, primary, Tanaka, Kaoru, primary, Suzuki, Norio, primary, Aoki, Shin, primary, Ito, Azusa, primary, Nanao, Tomohisa, primary, Ohya, Soichiro, primary, Yoshino, Minako, primary, Zhu, Jin, primary, Enomoto, Atsushi, primary, Matsumoto, Yoshihisa, primary, Funatsu, Osamu, primary, Hosoi, Yoshio, primary, and Ikekita, Masahiko, primary

Published
2023
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9. Supplementary Figure 2 from Sodium Orthovanadate Inhibits p53-Mediated Apoptosis

Author

Morita, Akinori, primary, Yamamoto, Shinichi, primary, Wang, Bing, primary, Tanaka, Kaoru, primary, Suzuki, Norio, primary, Aoki, Shin, primary, Ito, Azusa, primary, Nanao, Tomohisa, primary, Ohya, Soichiro, primary, Yoshino, Minako, primary, Zhu, Jin, primary, Enomoto, Atsushi, primary, Matsumoto, Yoshihisa, primary, Funatsu, Osamu, primary, Hosoi, Yoshio, primary, and Ikekita, Masahiko, primary

Published
2023
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10. Supplementary Figure 1 from Sodium Orthovanadate Inhibits p53-Mediated Apoptosis

Author

Morita, Akinori, primary, Yamamoto, Shinichi, primary, Wang, Bing, primary, Tanaka, Kaoru, primary, Suzuki, Norio, primary, Aoki, Shin, primary, Ito, Azusa, primary, Nanao, Tomohisa, primary, Ohya, Soichiro, primary, Yoshino, Minako, primary, Zhu, Jin, primary, Enomoto, Atsushi, primary, Matsumoto, Yoshihisa, primary, Funatsu, Osamu, primary, Hosoi, Yoshio, primary, and Ikekita, Masahiko, primary

Published
2023
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11. Supplementary Figure 6 from Sodium Orthovanadate Inhibits p53-Mediated Apoptosis

Author

Morita, Akinori, primary, Yamamoto, Shinichi, primary, Wang, Bing, primary, Tanaka, Kaoru, primary, Suzuki, Norio, primary, Aoki, Shin, primary, Ito, Azusa, primary, Nanao, Tomohisa, primary, Ohya, Soichiro, primary, Yoshino, Minako, primary, Zhu, Jin, primary, Enomoto, Atsushi, primary, Matsumoto, Yoshihisa, primary, Funatsu, Osamu, primary, Hosoi, Yoshio, primary, and Ikekita, Masahiko, primary

Published
2023
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12. Supplementary Figure 3 from Sodium Orthovanadate Inhibits p53-Mediated Apoptosis

Author

Morita, Akinori, primary, Yamamoto, Shinichi, primary, Wang, Bing, primary, Tanaka, Kaoru, primary, Suzuki, Norio, primary, Aoki, Shin, primary, Ito, Azusa, primary, Nanao, Tomohisa, primary, Ohya, Soichiro, primary, Yoshino, Minako, primary, Zhu, Jin, primary, Enomoto, Atsushi, primary, Matsumoto, Yoshihisa, primary, Funatsu, Osamu, primary, Hosoi, Yoshio, primary, and Ikekita, Masahiko, primary

Published
2023
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13. Supplementary Figure 5 from Sodium Orthovanadate Inhibits p53-Mediated Apoptosis

Author

Morita, Akinori, primary, Yamamoto, Shinichi, primary, Wang, Bing, primary, Tanaka, Kaoru, primary, Suzuki, Norio, primary, Aoki, Shin, primary, Ito, Azusa, primary, Nanao, Tomohisa, primary, Ohya, Soichiro, primary, Yoshino, Minako, primary, Zhu, Jin, primary, Enomoto, Atsushi, primary, Matsumoto, Yoshihisa, primary, Funatsu, Osamu, primary, Hosoi, Yoshio, primary, and Ikekita, Masahiko, primary

Published
2023
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19. Binding parameters and thermodynamics of the interaction of imino sugars with a recombinant human acid α-glucosidase (alglucosidase alfa): Insight into the complex formation mechanism

Author

Yoshimizu, Michiru, Tajima, Youichi, Matsuzawa, Fumiko, Aikawa, Sei-ichi, Iwamoto, Kunihiko, Kobayashi, Toshihide, Edmunds, Tim, Fujishima, Kaori, Tsuji, Daisuke, Itoh, Kohji, Ikekita, Masahiko, Kawashima, Ikuo, Sugawara, Kanako, Ohyanagi, Naho, Suzuki, Toshihiro, Togawa, Tadayasu, Ohno, Kazuki, and Sakuraba, Hitoshi

Published
2008
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21. Suppressive Effect of Tetrahydrobiopterin on L-β-( 3,4-Dihydroxyphenyl) alanine-Induced Cytotoxicity in PC-12 Cells

Author

Kojima Shuji, Kugenuma Hiroshi, Oyobe Sayaka, lizuka Hiroyuki, and Ikekita Masahiko

Subjects
tetrahydrobiopterin, dopa, cytotoxicity, pc-12 cells, Crystallography, QD901-999
Abstract

We examined the inhibitory effect of tetrahydrobiopterin (BPH4) on L-β-(3,4-dihydroxyphenyl)alanine (DOPA)-induced cytotoxicity in PC-12 cells. First in vitro inhibitory efficacy of BPH4 on lipid peroxidation induced by Fe3+-DOPA complex was confirmed by using PC-liposomes. Fe3+-DOPA complex at 50 μM caused drastic lipid peroxidation, which was significantly inhibited by BPH4 in a dose-dependent manner. Next, we confirmed the in vitro potency of BPH4 in cultured PC-12 cells. Fe3+-DOPA complex exerted time-and dose-dependent cytotoxicity, which was also dose-dependently inhibited by BPH4 possessed almost the same potency as deferoxamine and α-tocopherol. We also examined the cytotoxicity of DOPA itself. A higher dose of DOPA (250 μM) was necessary to afford the same cytotoxic potency towards PC-12 cells as that of Fe3+-DOPA complex (50 μM). The toxicity was essentially abolished by SOD and BPH4 and ameliorated by catalase . However, deferoxamine did not modify the toxicity. In conclusion, BPH4 protects both PC-liposomes and PC-12 cells from damage induced by DOPA with and without ferric ion, and may inhibit the degeneration of dopamine neurons through its antioxidatiye activity.

Published
1997
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25. Mouse [Na.sup.+]/[K.sup.+]-ATPase [beta]1-subunit has a [K.sup.+]-dependent cell adhesion activity for [beta]-GIcNAc-terminating glycans

Author

Kitamura, Noriaki, Ikekita, Masahiko, Sato, Takeshi, Akimoto, Yoshihiro, Hatanaka, Yasumaru, Kawakami, Hayato, Inomata, Mitsushi, and Furukawa, Kiyoshi

Subjects
Proteins -- Research, Brain -- Research, Mice -- Research, Lectins -- Research, Science and technology
Abstract

A 48-kDa [beta]-N-acetylglucosamine (GIcNAc)-binding protein was isolated from mouse brain by GIcNAc-agarose column chromatography. The N-terminal amino acid residues showed the protein to be a mouse [Na.sup.+]/[K.sup.+]-ATPase [beta]1-subunit. When the recombinant FLAG-[beta]1-subunit expressed in Sf-9 cells was applied to a GIcNAc-agarose column, only the glycosylated 38- and 40-kDa proteins bound to the column. In the absence of KCI, little of the proteins bound to a GIcNAc-agarose column, but the 38- and 40-kDa proteins bound in the presence of KCI at concentrations above 1 mM. Immunohistochemical study showed that the [beta]1-subunit and GIcNAc-terminating oligosaccharides are at the cell contact sites. Inclusion of anti-[beta]1-subunit antibody or chitobiose in cell aggregation assays using mouse neural cells resulted in inhibition of cell aggregation. These results indicate that the [Na.sup.+]/[K.sup.+]-ATPase [beta]1-subunit is a potassium-dependent lectin that binds to GIcNAc-terminating oligosaccharides: it may be involved in neural cell interactions. GIcNAc-binding lectin | cell surface | mouse brain

Published
2005

43. Upregulated expression of FGF13/FHF2 mediates resistance to platinum drugs in cervical cancer cells

Author

Okada, Tomoko, Murata, Kazuhiro, Hirose, Ryoma, Matsuda, Chie, Komatsu, Tsunehiko, Ikekita, Masahiko, Nakawatari, Miyako, Nakayama, Fumiaki, Wakatsuki, Masaru, Ohno, Tatsuya, Kato, Shingo, Imai, Takashi, and Imamura, Toru

Abstract

Cancer cells often develop drug resistance. In cisplatin-resistant HeLa cisRcells, fibroblast growth factor 13 (FGF13/FHF2) gene and protein expression was strongly upregulated, and intracellular platinum concentrations were kept low. When the FGF13 expression was suppressed, both the cells' resistance to platinum drugs and their ability to keep intracellular platinum low were abolished. Overexpression of FGF13 in parent cells led to greater resistance to cisplatin and reductions in the intracellular platinum concentration. These cisplatin-resistant cells also showed increased resistance to copper. In preoperative cervical cancer biopsy samples from poor prognoses patients after cisplatin chemoradiotherapy, FGF13-positive cells were detected more abundantly than in the biopsy samples from patients with good prognoses. These results suggest that FGF13 plays a pivotal role in mediating resistance to platinum drugs, possibly via a mechanism shared by platinum and copper. Our results point to FGF13 as a novel target and useful prognostic guide for cancer therapy.

Published
2013

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