Alliance Laboratory of ISIR,Osaka Univ. and RIKEN

Staff

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    Invited. Prof. N. TANIGUCHI
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    Invited Assoc. Prof. K. OTSUBO
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    Invited Faculty C. GAO
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    Invited Faculty H. KOREKANE
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    Invited Faculty S. TAKAMATSU

Higher organisms use "carbohydrate" as the energy source, as well as the transmitter "Sugar Chain" encoding enormous bio-information by constructing particular glycan structures. The bio-information encoded in glycan structure has been gradually decoded along with the development of glycobiology, and it is well known that sugar chain is essential for maintaining biological functions. Indeed, glycosylation defect evokes various intractable diseases and life style-related diseases. This laboratory is engaged in biochemical and molecular genetic approach to elucidate the disease process associated with dysglycosylation, to develop diagnostic marker of disease manifestation, and to develop novel strategies for therapy.

[ Current Research Programs ]

  1. The role of glycosylation in pathology of pulmonary emphysema
  2. Functional analyses of protein glycosylation in the disease process of diabetes
  3. In situ tracing of the fate of carbohydrate
  4. Exploring a novel regulator of cellular glycosylation system
  5. Functional analyses of protein glycosylation in the disease process of atherosclerosis

Figure / Graph

  • Fig.1
    Fig1. In Fut8 deficient mice, TGF-β receptor can not be fucosylated that diminishes the TGF-β signaling, that results in the MMP activation and pulmonary alveolus destruction diagnostic emphysema.
    Fig2. The proper N-glycosylation of glucose sensor is required for the cell surface residency in pancreatic β cells that contributes to insulin secretion. The failure of this mechanism evokes type 2 diabetes.
  • Fig.3
    Fig3. We will develop a fundamentalparadigm "Glycan Cycle" in whichliving cell regulates dynamicchanges of glycans in response tocellular environments. We could grasp the dynamic cellular information by analyzing theglycan cycle.
    Fig4. We have purified and identified a candidate regulatory protein for cellular glycosylation. We are biochemically engineering and characterizing the identified protein to elucidate physiological functions.

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