Satoshi Endo

Summary

Affiliation: Gifu Pharmaceutical University
Country: Japan

Publications

  1. Endo S, Matsunaga T, Mamiya H, Ohta C, Soda M, Kitade Y, et al. Kinetic studies of AKR1B10, human aldose reductase-like protein: endogenous substrates and inhibition by steroids. Arch Biochem Biophys. 2009;487:1-9 pubmed publisher
    ....
  2. Endo S, Fujimoto A, Kumada S, Matsunaga T, Ohno S, Mano J, et al. Modulation of activity and inhibitor sensitivity of rabbit aldose reductase-like protein (AKR1B19) by oxidized glutathione and SH-reagents. Chem Biol Interact. 2013;202:146-52 pubmed publisher
    ..Furthermore, such an activity alteration by GSSG was not detected in AKR1B10 and rat ARLPs, suggesting the presence of a GSSG-binding site near Cys299 in AKR1B19. ..
  3. Endo S, Hoshi M, Matsunaga T, Inoue T, Ichihara K, Ikari A. Autophagy inhibition enhances anticancer efficacy of artepillin C, a cinnamic acid derivative in Brazilian green propolis. Biochem Biophys Res Commun. 2018;497:437-443 pubmed publisher
    ..Therefore, the combination of ArtC and autophagy inhibitors may be a novel complementary-alternative treatment for prostate cancer. ..
  4. Hara A, Endo S, Matsunaga T, Soda M, El Kabbani O, Yashiro K. Inhibition of aldo-keto reductase family 1 member B10 by unsaturated fatty acids. Arch Biochem Biophys. 2016;609:69-76 pubmed publisher
    ..Thus, the cis-unsaturated fatty acids may be used as an adjuvant therapy for treatment of cancers that up-regulate AKR1B10. ..
  5. Endo S, Matsunaga T, Fujita A, Kuragano T, Soda M, Sundaram K, et al. Activation of aldo-keto reductase family member 1B14 (AKR1B14) by bile acids: Activation mechanism and bile acid-binding site. Biochimie. 2011;93:1476-86 pubmed publisher
    ....
  6. Endo S, Matsunaga T, Kumada S, Fujimoto A, Ohno S, El Kabbani O, et al. Characterization of rabbit aldose reductase-like protein with 3?-hydroxysteroid dehydrogenase activity. Arch Biochem Biophys. 2012;527:23-30 pubmed publisher
    ..Single and double mutations (F303Q, M304S and F303Q/M304S) significantly impaired this activity, suggesting the two residues play critical roles in recognition of the steroidal substrate. ..
  7. Endo S, Matsunaga T, Matsumoto A, Arai Y, Ohno S, El Kabbani O, et al. Rabbit 3-hydroxyhexobarbital dehydrogenase is a NADPH-preferring reductase with broad substrate specificity for ketosteroids, prostaglandin D?, and other endogenous and xenobiotic carbonyl compounds. Biochem Pharmacol. 2013;86:1366-75 pubmed publisher
    ....
  8. Sonoki H, Sato T, Endo S, Matsunaga T, Yamaguchi M, Yamazaki Y, et al. Quercetin Decreases Claudin-2 Expression Mediated by Up-Regulation of microRNA miR-16 in Lung Adenocarcinoma A549 Cells. Nutrients. 2015;7:4578-92 pubmed publisher
    ..These results suggest that quercetin decreases claudin-2 expression mediated by up-regulation of miR-16 expression and instability of claudin-2 mRNA in lung adenocarcinoma cells. ..
  9. Endo S, Miyagi N, Matsunaga T, Hara A, Ikari A. Human dehydrogenase/reductase (SDR family) member 11 is a novel type of 17β-hydroxysteroid dehydrogenase. Biochem Biophys Res Commun. 2016;472:231-6 pubmed publisher
    ..Thus, DHRS11 represents a novel type of 17β-hydroxysteroid dehydrogenase with unique catalytic properties and tissue distribution. ..
  10. Endo S, Matsunaga T, Kitade Y, Ohno S, Tajima K, El Kabbani O, et al. Human carbonyl reductase 4 is a mitochondrial NADPH-dependent quinone reductase. Biochem Biophys Res Commun. 2008;377:1326-30 pubmed publisher
    ..We further demonstrate that the in vitro quinone reduction by CBR4 generates superoxide through the redox cycling, and suggest that the enzyme may be involved in the induction of apoptosis by cytotoxic 9,10-phenanthrenequinone. ..

Locale

Detail Information

Publications17

  1. Endo S, Matsunaga T, Mamiya H, Ohta C, Soda M, Kitade Y, et al. Kinetic studies of AKR1B10, human aldose reductase-like protein: endogenous substrates and inhibition by steroids. Arch Biochem Biophys. 2009;487:1-9 pubmed publisher
    ....
  2. Endo S, Fujimoto A, Kumada S, Matsunaga T, Ohno S, Mano J, et al. Modulation of activity and inhibitor sensitivity of rabbit aldose reductase-like protein (AKR1B19) by oxidized glutathione and SH-reagents. Chem Biol Interact. 2013;202:146-52 pubmed publisher
    ..Furthermore, such an activity alteration by GSSG was not detected in AKR1B10 and rat ARLPs, suggesting the presence of a GSSG-binding site near Cys299 in AKR1B19. ..
  3. Endo S, Hoshi M, Matsunaga T, Inoue T, Ichihara K, Ikari A. Autophagy inhibition enhances anticancer efficacy of artepillin C, a cinnamic acid derivative in Brazilian green propolis. Biochem Biophys Res Commun. 2018;497:437-443 pubmed publisher
    ..Therefore, the combination of ArtC and autophagy inhibitors may be a novel complementary-alternative treatment for prostate cancer. ..
  4. Hara A, Endo S, Matsunaga T, Soda M, El Kabbani O, Yashiro K. Inhibition of aldo-keto reductase family 1 member B10 by unsaturated fatty acids. Arch Biochem Biophys. 2016;609:69-76 pubmed publisher
    ..Thus, the cis-unsaturated fatty acids may be used as an adjuvant therapy for treatment of cancers that up-regulate AKR1B10. ..
  5. Endo S, Matsunaga T, Fujita A, Kuragano T, Soda M, Sundaram K, et al. Activation of aldo-keto reductase family member 1B14 (AKR1B14) by bile acids: Activation mechanism and bile acid-binding site. Biochimie. 2011;93:1476-86 pubmed publisher
    ....
  6. Endo S, Matsunaga T, Kumada S, Fujimoto A, Ohno S, El Kabbani O, et al. Characterization of rabbit aldose reductase-like protein with 3?-hydroxysteroid dehydrogenase activity. Arch Biochem Biophys. 2012;527:23-30 pubmed publisher
    ..Single and double mutations (F303Q, M304S and F303Q/M304S) significantly impaired this activity, suggesting the two residues play critical roles in recognition of the steroidal substrate. ..
  7. Endo S, Matsunaga T, Matsumoto A, Arai Y, Ohno S, El Kabbani O, et al. Rabbit 3-hydroxyhexobarbital dehydrogenase is a NADPH-preferring reductase with broad substrate specificity for ketosteroids, prostaglandin D?, and other endogenous and xenobiotic carbonyl compounds. Biochem Pharmacol. 2013;86:1366-75 pubmed publisher
    ....
  8. Sonoki H, Sato T, Endo S, Matsunaga T, Yamaguchi M, Yamazaki Y, et al. Quercetin Decreases Claudin-2 Expression Mediated by Up-Regulation of microRNA miR-16 in Lung Adenocarcinoma A549 Cells. Nutrients. 2015;7:4578-92 pubmed publisher
    ..These results suggest that quercetin decreases claudin-2 expression mediated by up-regulation of miR-16 expression and instability of claudin-2 mRNA in lung adenocarcinoma cells. ..
  9. Endo S, Miyagi N, Matsunaga T, Hara A, Ikari A. Human dehydrogenase/reductase (SDR family) member 11 is a novel type of 17β-hydroxysteroid dehydrogenase. Biochem Biophys Res Commun. 2016;472:231-6 pubmed publisher
    ..Thus, DHRS11 represents a novel type of 17β-hydroxysteroid dehydrogenase with unique catalytic properties and tissue distribution. ..
  10. Endo S, Matsunaga T, Kitade Y, Ohno S, Tajima K, El Kabbani O, et al. Human carbonyl reductase 4 is a mitochondrial NADPH-dependent quinone reductase. Biochem Biophys Res Commun. 2008;377:1326-30 pubmed publisher
    ..We further demonstrate that the in vitro quinone reduction by CBR4 generates superoxide through the redox cycling, and suggest that the enzyme may be involved in the induction of apoptosis by cytotoxic 9,10-phenanthrenequinone. ..
  11. Hara A, Endo S, Matsunaga T, El Kabbani O, Miura T, Nishinaka T, et al. Human carbonyl reductase 1 participating in intestinal first-pass drug metabolism is inhibited by fatty acids and acyl-CoAs. Biochem Pharmacol. 2017;138:185-192 pubmed publisher
    ..The results suggest a possible new food-drug interaction through inhibition of CBR1-mediated intestinal first-pass drug metabolism by dietary fatty acids. ..
  12. Sonoki H, Tanimae A, Endo S, Matsunaga T, Furuta T, Ichihara K, et al. Kaempherol and Luteolin Decrease Claudin-2 Expression Mediated by Inhibition of STAT3 in Lung Adenocarcinoma A549 Cells. Nutrients. 2017;9: pubmed publisher
    ..The intake of foods and nutrients rich in these flavonoids may prevent lung adenocarcinoma development. ..
  13. request reprint
    Endo S, Sanai M, Horie K, Matsunaga T, Ishikura S, Tajima K, et al. Characterization of rat and mouse NAD+-dependent 3alpha/17beta/20alpha-hydroxysteroid dehydrogenases and identification of substrate specificity determinants by site-directed mutagenesis. Arch Biochem Biophys. 2007;467:76-86 pubmed
    ..The replacement of Asp128, Phe129 and Ser137 of AKR1C16 with the corresponding residues (Glu, Ser and Phe, respectively) of AKR1C24 increased the catalytic efficiency for 17beta- and 20alpha-hydroxysteroids. ..
  14. Endo S, Matsunaga T, Kuragano T, Ohno S, Kitade Y, Tajima K, et al. Properties and tissue distribution of a novel aldo-keto reductase encoding in a rat gene (Akr1b10). Arch Biochem Biophys. 2010;503:230-7 pubmed publisher
    ..The results suggest that R1B10 functions as a defense system against oxidative stress and glycation in rat tissues. ..
  15. Endo S, Matsunaga T, Ohta C, Soda M, Kanamori A, Kitade Y, et al. Roles of rat and human aldo-keto reductases in metabolism of farnesol and geranylgeraniol. Chem Biol Interact. 2011;191:261-8 pubmed publisher
    ..Thus, AKRs (1C15 in rats, and 1B10 and 1C3 in humans) may play an important role in controlling the bioavailability of FOH and GGOH. ..
  16. Endo S, Maeda S, Matsunaga T, Dhagat U, El Kabbani O, Tanaka N, et al. Molecular determinants for the stereospecific reduction of 3-ketosteroids and reactivity towards all-trans-retinal of a short-chain dehydrogenase/reductase (DHRS4). Arch Biochem Biophys. 2009;481:183-90 pubmed publisher
    ....
  17. Endo S, Takada S, Honda R, Müller K, Weishaupt J, Andersen P, et al. Instability of C154Y variant of aldo-keto reductase 1C3. Chem Biol Interact. 2017;276:194-202 pubmed publisher
    ..In contrast, the overexpression of C154Y in the cells did not show such a significant protective effect, suggesting that C154Y is unstable in cells. ..