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Allose

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Masaaki Tokuda – 1st expert on this subject based on the ideXlab platform

  • combined treatment with d Allose docetaxel and radiation inhibits the tumor growth in an in vivo model of head and neck cancer
    Oncology Letters, 2018
    Co-Authors: Hiroshi Hoshikawa, Kazuyo Kamitori, Kanako Indo, Terushige Mori, Mizuna Kamata, Tomoko Takahashi, Masaaki Tokuda

    Abstract:

    : The present study was designed to evaluate the effect of one rare sugar, D-Allose, on normal human cells and cutaneous tissue, and to investigate the radiosensitizing and chemosensitizing potential of D-Allose in an in vivo model of head and neck cancer. Results indicated that D-Allose did not inhibit the growth of normal human fibroblasts TIG-1 cells, and no apoptotic changes were observed after D-Allose and D-glucose treatment. The mRNA expression levels of thioredoxin interacting protein (TXNIP) in TIG-1 cells after D-Allose treatment increased by 2-fold (50.4 to 106.5). Conversely, the mRNA expression levels of TXNIP in HSC3 cancer cells increased by 74-fold (1.5 to 110.6), and the thioredoxin (TRX)/TXNIP ratio was markedly reduced from 61.7 to 1.4 following D-Allose treatment. Combined multiple treatments with docetaxel, radiation and D-Allose resulted in the greatest antitumor response in the in vivo model. Hyperkeratosis, epidermal thickening and tumor necrosis factor-α immunostaining were observed following irradiation treatment, but these pathophysiological reactions were reduced following D-Allose administration. Thus, the present findings suggest that D-Allose may enhance the antitumor effects of chemoradiotherapy whilst sparing normal tissues.

  • additive antitumour effect of d Allose in combination with cisplatin in non small cell lung cancer cells
    Oncology Reports, 2018
    Co-Authors: Nobuhiro Kanaji, Kazuyo Kamitori, Akram Hossain, Chisato Noguchi, Ayako Katagi, Norimitsu Kadowaki, Masaaki Tokuda

    Abstract:

    : D‑Allose is a rare sugar which has been shown to have growth inhibitory effects in several kinds of malignancies. However, the effect of D‑Allose on lung cancer progression has not been previously studied. To investigate the antitumour effect of D‑Allose in lung cancer cells and its mechanism, human non-small cell lung cancer (NSCLC) cell lines (squamous cell carcinomas: EBC1 and VMRC‑LCD; adenocarcinomas: A549, HI1017, RERF‑LC‑A1 and NCI-H1975) were treated with D‑Allose (50 mM) with or without cisplatin (5 µM). D‑Allose inhibited cell growth, particularly in EBC1 and VMRC‑LCD cells. In combination with cisplatin, D‑Allose had a synergistic growth inhibitory effect. D‑Allose increased the expression of thioredoxin interacting protein (TXNIP) at mRNA and protein levels. D‑Allose decreased the proportion of cells in G1 phase and increased those in S and G2/M phases. For in vivo experiments, EBC1 cells were inoculated into BALB/c-nu mice. After tumourigenesis, D‑Allose and cisplatin were injected. In this mouse xenograft model, additional treatment with D‑Allose showed a significantly greater tumour inhibitory effect compared with cisplatin alone, accompanied by lower Ki‑67 and higher TXNIP expression. In conclusion, D‑Allose inhibited NSCLC cell proliferation in vitro and tumour progression in vivo. In combination with cisplatin, D‑Allose had an additional antitumour effect. Specifically, increased TXNIP expression and subsequent G2/M arrest play a role in D‑Allose-mediated antitumour effects in NSCLC.

  • Additive antitumour effect of D‑Allose in combination with cisplatin in non-small cell lung cancer cells.
    Oncology Reports, 2018
    Co-Authors: Nobuhiro Kanaji, Kazuyo Kamitori, Akram Hossain, Chisato Noguchi, Ayako Katagi, Norimitsu Kadowaki, Masaaki Tokuda

    Abstract:

    : D‑Allose is a rare sugar which has been shown to have growth inhibitory effects in several kinds of malignancies. However, the effect of D‑Allose on lung cancer progression has not been previously studied. To investigate the antitumour effect of D‑Allose in lung cancer cells and its mechanism, human non-small cell lung cancer (NSCLC) cell lines (squamous cell carcinomas: EBC1 and VMRC‑LCD; adenocarcinomas: A549, HI1017, RERF‑LC‑A1 and NCI-H1975) were treated with D‑Allose (50 mM) with or without cisplatin (5 µM). D‑Allose inhibited cell growth, particularly in EBC1 and VMRC‑LCD cells. In combination with cisplatin, D‑Allose had a synergistic growth inhibitory effect. D‑Allose increased the expression of thioredoxin interacting protein (TXNIP) at mRNA and protein levels. D‑Allose decreased the proportion of cells in G1 phase and increased those in S and G2/M phases. For in vivo experiments, EBC1 cells were inoculated into BALB/c-nu mice. After tumourigenesis, D‑Allose and cisplatin were injected. In this mouse xenograft model, additional treatment with D‑Allose showed a significantly greater tumour inhibitory effect compared with cisplatin alone, accompanied by lower Ki‑67 and higher TXNIP expression. In conclusion, D‑Allose inhibited NSCLC cell proliferation in vitro and tumour progression in vivo. In combination with cisplatin, D‑Allose had an additional antitumour effect. Specifically, increased TXNIP expression and subsequent G2/M arrest play a role in D‑Allose-mediated antitumour effects in NSCLC.

Ken Izumori – 2nd expert on this subject based on the ideXlab platform

  • the rare sugar d Allose acts as a triggering molecule of rice defence via ros generation
    Journal of Experimental Botany, 2013
    Co-Authors: Akihito Kano, Ken Izumori, Takeshi Fukumoto, Kouhei Ohtani, Akihide Yoshihara, Toshiaki Ohara, Shigeyuki Tajima, Keiji Tanaka, Takeo Ohkouchi, Yutaka Ishida

    Abstract:

    Only d-Allose, among various rare monosaccharides tested, induced resistance to Xanthomonas oryzae pv. oryzae in susceptible rice leaves with defence responses: reactive oxygen species, lesion mimic formation, and PR-protein gene expression. These responses were suppressed by ascorbic acid or diphenylene iodonium. Transgenic rice plants overexpressing OsrbohC, encoding NADPH oxidase, were enhanced in sensitivity to d-Allose. d-Allose-mediated defence responses were suppressed by the presence of a hexokinase inhibitor. 6-Deoxy-d-Allose, a structural derivative of d-Allose unable to be phosphorylated, did not confer resistance. Transgenic rice plants expressing Escherichia coli AlsK encoding d-Allose kinase to increase d-Allose 6-phosphate synthesis were more sensitive to d-Allose, but E. coli AlsI encoding d-Allose 6-phosphate isomerase expression to decrease d-Allose 6-phosphate reduced sensitivity. A d-glucose 6-phosphate dehydrogenase-defective mutant was also less sensitive, and OsG6PDH1 complementation restored full sensitivity. These results reveal that a monosaccharide, d-Allose, induces rice resistance to X. oryzae pv. oryzae by activating NADPH oxidase through the activity of d-glucose 6-phosphate dehydrogenase, initiated by hexokinase-mediated conversion of d-Allose to d-Allose 6-phosphate, and treatment with d-Allose might prove to be useful for reducing disease development in rice.

  • phosphorylation of d Allose by hexokinase involved in regulation of osabf1 expression for growth inhibition in oryza sativa l
    Planta, 2013
    Co-Authors: Takeshi Fukumoto, Ken Izumori, Akihito Kano, Kouhei Ohtani, Akihide Yoshihara, Shigeyuki Tajima, Keiji Tanaka, Megumi Inoue, Yoshio Shigematsu, Takeo Ohkouchi

    Abstract:

    We previously reported that a rare sugar d-Allose, which is the d-glucose epimer at C3, inhibits the gibberellin-dependent responses such as elongation of the second leaf sheath and induction of α-amylase in embryo-less half seeds in rice (Fukumoto et al. 2011). d-Allose suppresses expressions of gibberellin-responsive genes downstream of SLR1 protein in the gibberellin-signaling through hexokinase (HXK)-dependent pathway. In this study, we discovered that d-Allose induced expression of ABA-related genes including OsNCED1-3 and OsABA8ox1-3 in rice. Interestingly, d-Allose also up-regulated expression of OsABF1, encoding a conserved bZIP transcription factor in ABA signaling, in rice. The d-Allose-induced expression of OsABF1 was diminished by a hexokinase inhibitor, d-mannoheptulose (MNH). Consistently, d-Allose also inhibited Arabidopsis growth, but failed to trigger growth retardation in the glucose-insensitive2 (gin2) mutant, which is a loss-of-function mutant of the glucose sensor AtHXK1. d-Allose activated AtABI5 expression in transgenic gin2 over-expressing wild-type AtHXK1 but not in gin2 over-expressing the catalytic mutant AtHXK1S177A, indicating that the d-Allose phosphorylation by HXK to d-Allose 6-phosphate (A6P) is the first step for the up-regulation of AtABI5 gene expression as well as d-Allose-induced growth inhibition. Moreover, overexpression of OsABF1 showed increased sensitivity to d-Allose in rice. These findings indicated that the phosphorylation of d-Allose at C6 by hexokinase is essential and OsABF1 is involved in the signal transduction for d-Allose-induced growth inhibition.

  • arabidopsis scaffold protein rack1a modulates rare sugar d Allose regulated gibberellin signaling
    Plant Signaling & Behavior, 2012
    Co-Authors: Herman Fennell, Ken Izumori, Abdulquadri Olawin, Rahman Md Mizanur, Jingui Chen, Hemayet Ullah

    Abstract:

    As energy sources and structural components, sugars are the central regulators of plant growth and development. In addition to the abundant natural sugars in plants, more than 50 different kinds of rare sugars exist in nature, several of which show distinct roles in plant growth and development. Recently, one of the rare sugars, D-Allose, an epimer of D-glucose at C3, is found to suppress plant hormone gibberellin (GA) signaling in rice. Scaffold protein RACK1A in the model plant Arabidopsis is implicated in the GA pathway as rack1a knockout mutants show insensitivity to GA in GA-induced seed germination. Using genetic knockout lines and a reporter gene, the functional role of RACK1A in the D-Allose pathway was investigated. It was found that the rack1a knockout seeds showed hypersensitivity to D-Allose-induced inhibition of seed germination, implicating a role for RACK1A in the D-Allose mediated suppression of seed germination. On the other hand, a functional RACK1A in the background of the double knocko…

Deok-kun Oh – 3rd expert on this subject based on the ideXlab platform

  • biotransformation of fructose to Allose by a one pot reaction using flavonifractor plautiid allulose 3 epimerase and clostridium thermocellum ribose 5 phosphate isomerase
    Journal of Microbiology and Biotechnology, 2018
    Co-Authors: Kyungchul Shin, Deok-kun Oh

    Abstract:

    : D-Allose is a potential medical sugar because it has anticancer, antihypertensive, anti-inflammatory, antioxidative, and immunosuppressant activities. Allose production from fructose as a cheap substrate was performed by a one-pot reaction using Flavonifractor plautiiD-allulose 3-epimerase (FP-DAE) and Clostridium thermocellum ribose 5-phosphate isomerase (CT-RPI). The optimal reaction conditions for Allose production were pH 7.5, 60°C, 0.1 g/l FP-DAE, 12 g/l CT-RPI, and 600 g/l fructose in the presence of 1 mM Co2+. Under these optimized conditions, FP-DAE and CT-RPI produced 79 g/l Allose for 2 h, with a conversion yield of 13%. This is the first biotransformation of fructose to Allose by a two-enzyme system. The production of Allose by a one-pot reaction using FP-DAE and CT-RPI was 1.3-fold higher than that by a two-step reaction using the two enzymes.

  • Microbial metabolism and biotechnological production of d-Allose
    Applied Microbiology and Biotechnology, 2011
    Co-Authors: Deok-kun Oh

    Abstract:

    d –Allose has attracted a great deal of attention in recent years due to its many pharmaceutical activities, which include anti-cancer, anti-tumor, anti-inflammatory, anti-oxidative, anti-hypertensive, cryoprotective, and immunosuppressant activities. d –Allose has been produced from d -psicose using d –Allose-producing enzymes, including l -rhamnose isomerase, ribose-5-phosphate isomerase, and galactose-6-phosphate isomerase. In this article, the properties, applications, and metabolism of d –Allose are described, and the biochemical properties of d –Allose-producing enzymes and their d –Allose production are reviewed and compared. Moreover, several methods for effective d –Allose production are suggested herein.

  • substrate specificity of a recombinant d lyxose isomerase from providencia stuartii for monosaccharides
    Journal of Bioscience and Bioengineering, 2010
    Co-Authors: Hyunjung Kwon, Chang-su Park, Soo Jin Yeom, Deok-kun Oh

    Abstract:

    The specific activity and catalytic efficiency (k(cat)/K(m)) of the recombinant putative protein from Providencia stuartii was the highest for D-lyxose among the aldose substrates, indicating that it is a D-lyxose isomerase. Gel filtration analysis suggested that the native enzyme is a dimer with a molecular mass of 44 kDa. The maximal activity for D-lyxose isomerization was observed at pH 7.5 and 45 degrees C in the presence of 1 mM Mn(2+). The enzyme exhibited high isomerization activity for aldose substrates with the C2 and C3 hydroxyl groups in the left-hand configuration, such as D-lyxose, D-mannose, L-ribose, D-talose, and L-Allose (listed in decreasing order of activity). The enzyme exhibited the highest activity for D-xylulose among all pentoses and hexoses. Thus, D-lyxose was produced at 288 g/l from 500 g/l D-xylulose by D-lyxose isomerase at pH 7.5 and 45 degrees C for 2 h, with a conversion yield of 58% and a volumetric productivity of 144 g l(-1) h(-1). The observed k(cat)/K(m) (920 mM(-1) s(-1)) of P. stuartiid-lyxose isomerase for D-xylulose is higher than any of the k(cat)/K(m) values previously reported for sugar and sugar phosphate isomerases with monosaccharide substrates. These results suggest that the enzyme will be useful as an industrial producer of D-lyxose.