Disease Glycomics Team

Most of membrane receptors such as growth factor receptors are glycoproteins but the study on the role of their glycans are very limited. Very recently we found that these glycans directly or indirectly play pivotal roles as intra- and internal cell signaling molecules under physiological and disease conditions and also involved in the gene expression. Our laboratory aims to explore the role of glycans in the development and differentiation under physiological conditions, and down-regulated signals in the life tyle-related diseases such as diabetes and up-regulated signals in cancer, angogenesis and neurodegenerative diseases such as Alzheimer diseases. We will also focus on basic research in order to develop biomarkers and therapeutics using glycans.

Research Subjects

• Glycan signals in cancer and lung emphysema
• Develpemtn of Cancer Biomarker
• Role of glycans in Alzheimer's disease
• Analysis of nucleotide sugars
• Role of glycans in angiogenesis

Publications

1. Li W., Lu, Q., Pang, Y., Jin, J., Wang, H., Cao, H., Li, Z., Wang, X., Ma, B., Chi, Y., Wang, R., Kondo, A., Gu, J., and Taniguchi, N.:
   "Core Fucosylation of Heavy Chains Regulates Assembly and Intracellular Signaling of Precursor B Cell Receptors"
   J. Biol. Chem. 287, 2500-2508. (2012)
2. Kamio, K., Yoshida, T., Gao, C., Ishii, T., Ota, F., Motegi, T., Kobayashi, S., Fujinawa, R., Ohtsubo, K., Kitazume, S., Angata, T., Azuma, A., Gemma, A., Nishimura, M., Betsuyaku, T., Kida, K. and Taniguchi, N.:
   "α1,6 Fucosyltransferase (Fut8) is implicated in vulnerability to elastase-induced emphysema in mice and a possible non-invasive predictive marker for disease progression and exacerbation in chronic obstructive pulmonary disease (COPD). "
   Biochem Biophys Res Commun., 424, 121-117. (2012)
3. Kitazume,S., Yoshihisa, A., Yamaki,T., Oikawa, M.,Tachida,Y., Ogawa, K., Imamaki, R.,Hagiwara, Y.,Kinoshita,N., Takeishi,Y., Furukawa, K., Tomita, N., Arai, H., Iwata,N., Saido, T.C., Yamamoto, N. and Taniguchi, N.:
   "Soluble amyloid precursor protein 770 is released from inflamed endothelial cells and activated platelets: a novel biomarker for acute coronary syndrome."
   J. Biol. Chem. (2012) 287, 40817-40825.
4. Kizuka, Y., Kitazume, S., Yoshida, M., and Taniguchi, N.
   "Brain-specific expression of N-acetylglucosaminyltransferase IX (GnT-IX) is regulated by epigenetic histone modifications"
   J. Biol. Chem. 286, 31875-31884.(2011)
5. Takamatsu, S., Antonopoulos, A., Ohtsubo, K., Ditto, D., Chiba, Y., Le, DT., Morris, HR., Haslam, SM., Dell, A., Marth, JD., Taniguchi, N.:
   "Physiological and glycomic characterization of N-acetylglucosaminyltransferase-IVa and -IVb double deficient mice."
   Glycobiology, 2010, 20, 485-497
6. Kitazume,S.,Imamaki,R.,Ogawa,K.,Komi,N.,Futakawa,S,.Kojima,S.,Hashimoto,Y.,Marth J.D.,Paulson,J.C.and Taniguchi,N.:
   "α2,6-Sialic Acid on Platelet Endothelial Cell Adhesion Molecule (PECAM) Regulates Its Homophilic Interactions and Downstream Antiapoptotic Signaling"
   J. Biol. Chem. 285, 6515-6521. (2010)
7. Kitazume, S.,Tachida,Y., Kato, M., Yamaguchi,Y., Honda,T., Hashimoto,Y., Wada,Y., Saito,T.,Iwata,N., Saido, T and Taniguchi, N.:
   "Brain endothelial cells produce amyloid β from amyloid precursor protein 770 and preferentially secrete the O-glycosylated form"
   J. Biol. Chem. 285, 40097-40103.(2010)
8. Nakajima, K,, Kitazume, S., Angata, T., Fujinawa, R., Ohtsubo, K., Miyoshi, E., and Taniguchi, N.:
   "Simultaneous determination of nucleotide sugars involved in glycosylation with ion-pair reversed -phase HPLC"
   Glycobiology 20, 865-871. (2010)
9. Kitazume,S., Oka,R., Ogawa, K., Futakawa,S., Hagiwara, S., Takigawa, H., Kato, M., Kasahara, A., Miyoshi, E., Taniguchi, N and Hashimoto, Y.:
   "Molecular insights into β-galactoside α2,6-sialyltransferase secretion in vivo"
   Glycobiology 19, 479-487. (2009)
10. Tachida, Y., Nakagawa, K., Saito, T., Saido, T.C., Honda, T, Saito, Y., Murayama, S., Endo, T., Sakaguchi, G.,Kato, A., Kitazume, S., and Hashimoto, Y.:
    "Interleukin-1β up-regulates TACE to enhance -cleavage of APP in neurons: resulting decrease in Aβproduction"
    J. Neurochem. 204, 1387-1393. (2008)