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309 results on '"Azuma, Toshifumi"'

10. Hedgehog Activation Regulates Human Osteoblastogenesis

Author

Onodera, Shoko, Saito, Akiko, Hojo, Hironori, Nakamura, Takashi, Zujur, Denise, Watanabe, Katsuhito, Morita, Nana, Hasegawa, Daigo, Masaki, Hideki, Nakauchi, Hiromitsu, Nomura, Takeshi, Shibahara, Takahiko, Yamaguchi, Akira, Chung, Ung-il, Azuma, Toshifumi, and Ohba, Shinsuke

Published
2020
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32. sup_figure_legend_2_ – Supplemental material for A novel GNAS-mutated human induced pluripotent stem cell model for understanding GNAS-mutated tumors

Author

Watanabe, Katsuhito, Nakamura, Takashi, Onodera, Shoko, Saito, Akiko, Shibahara, Takahiko, and Azuma, Toshifumi

Subjects
musculoskeletal diseases, FOS: Clinical medicine, Cell Biology, 111299 Oncology and Carcinogenesis not elsewhere classified
Abstract

Supplemental material, sup_figure_legend_2_ for A novel GNAS-mutated human induced pluripotent stem cell model for understanding GNAS-mutated tumors by Katsuhito Watanabe, Takashi Nakamura, Shoko Onodera, Akiko Saito, Takahiko Shibahara and Toshifumi Azuma in Tumor Biology

Published
2020
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33. Runx2 Regulates Chromatin Accessibility to Direct Skeletal Cell Programs

Author

Hojo, Hironori, primary, Saito, Taku, additional, He, Xinjun, additional, Guo, Qiuyu, additional, Onodera, Shoko, additional, Azuma, Toshifumi, additional, Koebis, Michinori, additional, Nakao, Kazuki, additional, Aiba, Atsu, additional, Seki, Masahide, additional, Suzuki, Yutaka, additional, Okada, Hiroyuki, additional, Tanaka, Sakae, additional, Chung, Ung-il, additional, McMahon, Andrew P., additional, and Ohba, Shinsuke, additional

Published
2021
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34. Leptin deficiency enhances sensitivity of rats to alcoholic steatohepatitis through suppression of metallothionein

Author

Tomita, Kengo, Azuma, Toshifumi, Kitamura, Naoto, Tamiya, Gen, Ando, Satoshi, Nagata, Hiroshi, Kato, Shinzo, Inokuchi, Sayaka, Nishimura, Takeshi, Ishii, Hiromasa, and Hibi, Toshifumi

Subjects
Tumor necrosis factor -- Research, Leptin -- Research, Biological sciences
Abstract

Leptin deficiency enhances sensitivity of rats to alcoholic steatohepatitis through suppression of metallothionein. Am J Physiol Gastrointest Liver Physiol 287: G1078-G1085, 2004; doi:10.1152/ ajpgi.00107.2004.--Oxidative stress is stated to be a central mechanism of hepatocellular injury in alcohol-induced liver injury. Recent reports have shown that Kupffer cell dysfunction in the leptin-deficient state contributes partly to the increased sensitivity to endotoxin liver injury. Here we report that leptin also plays a key role in the development of alcoholic liver injury and that leptin signaling in hepatocytes is involved in cellular mechanisms that mediate ethanol-induced oxidative stress. We found that chronic ethanol feeding in leptin receptor-deficient Zucker (fa/fa) rats for 6 wk resulted in a much more severe liver injury and augmented accumulation of hepatic lipid peroxidation compared with control littermates. The hepatic induction of stress-response and antioxidant proteins, such as metallothionein (MT)-1 and -2, was significantly suppressed in fa/fa rats after chronic ethanol feeding. Zinc concentration in liver was also decreased in fa/fa rats, compared with control littermates. In primary cultured hepatocytes from fa/fa rats, incubation with ethanol significantly suppressed MT-1 and -2 expressions. Addition of leptin to leptin-deficient ob/ob mouse primary hepatocytes led to an increase in MT-1 and -2 mRNA levels and a decrease in oxidative stress after incubation with ethanol. In conclusion, leptin deficiency enhances sensitivity of rats to alcohol-induced steatohepatitis through hepatocyte-specific interaction of MT-1 and -2 and resultant exaggeration of oxidative stress in hepatocytes. These findings suggest that leptin resistance in hepatocytes is an important mechanism of alcohol-induced liver injury. oxidative stress; zinc; tumor necrosis factor-[alpha];

Published
2004

35. Bax interacts with the voltage-dependent anion channel and mediates ethanol-induced apoptosis in rat hepatocytes

Author

Adachi, Masayuki, Higuchi, Hajime, Miura, Soichiro, Azuma, Toshifumi, Inokuchi, Sayaka, Saito, Hidetsugu, Kato, Shinzo, and Ishii, Hiromasa

Subjects
Liver cells -- Research, Liver cells -- Physiological aspects, Apoptosis -- Research, Apoptosis -- Physiological aspects, Alcohol -- Physiological aspects, Alcohol, Denatured -- Physiological aspects, Biological sciences
Abstract

Acute ethanol exposure induces oxidative stress and apoptosis in primary rat hepatocytes. Previous data indicate that the mitochondrial permeability transition (MPT) is essential for ethanol-induced apoptosis. However, the mechanism by which ethanol induces the MPT remains unclear. In this study, we investigated the role of Bax, a proapoptotic Bcl-2 family protein, in acute ethanol-induced hepatocyte apoptosis. We found that Bax translocates from the cytosol to mitochondria before mitochondrial cytochrome c release. Bax translocation was oxidative stress dependent. Mitochondrial Bax formed a protein complex with the mitochondrial voltage-dependent anion channel (VDAC). Prevention of Bax-VDAC interactions by a microinjection of anti-VDAC antibody effectively prevented hepatocyte apoptosis by ethanol. In conclusion, these data suggest that Bax translocation from the cytosol to mitochondria leads to the subsequent formation of a Bax-VDAC complex that plays a crucial role in acute ethanol-induced hepatocyte apoptosis. alcoholic liver disease; mitochondria; oxidative stress; cytochrome c

Published
2004

44. Hemostatic, inflammatory, and fibroblast responses are blunted in mice lacking gelsolin

Author

Witke, Walter, Sharpe, Arlene H., Hartwig, John H., Azuma, Toshifumi, Stossel, Thomas P., and Kwiatkowski, David J.

Subjects
Actin -- Observations, Genetically modified mice -- Research, Fibroblasts -- Analysis, Inflammation -- Observations, Hemostasis -- Observations, Proteins -- Analysis, Biological sciences
Abstract

The gelsolin, an 82 kDa actin-binding protein, regulates the motility of cells which help in hemostasis, inflammation, and wound healing. The gelsolin is not present in embryonic cells and the process of actin filament dynamics is not required for motility in the early embryogenesis. The transgenic gelsolinnull (Gsn-) mice were produced for the vivo experiments on the functioning of gelsolin. The Gsn-mice show less changed platelet shape and this led to more continuous bleeding.

Published
1995

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