System Glycobiology Research Group
Group Director
Naoyuki TANIGUCHI (D.Med.Sci.)
Over 50% of proteins are glycosylated and glycosylation reaction is one of the most important posttranslational modifications of proteins. The sugar chains have different kinds of function, which we are unable to understand from the research on DNA, RNA and proteins. This project focuses on structure and functions of glycoproteins, and we aim to elucidate (1) abnormality of signaling via membrane receptor glycans, and its underlying mechanism of diseases, (2) novel metabolic pathway of free glycans and its role in the quality control of glycoproteins, (3) tertiary structures of glycans and their roles in molecular recognition, and to develop (4) single-molecule imaging of glycans. Through the above researches, we will pursue the basic research, which may develop biomarkers and therapeutics of the diseases such as cancer, infectious diseases, life style-related diseases, and neuromuscular degenerative diseases.
- Glycans in the growth receptors and underlying mechanism of diseases
- Molecular mechanism of non-lysosomal catabolic pathway for N-glycans
- Development of conformational analysis of glycans
- Taniguchi, N.:
"From the γ-Glutamyl Cycle to the Glycan Cycle: A Road with Many Turns and Pleasant Surprises.:"
J. Biol. Chem. 284, 34469-78 (2009) - Kitazume, S., Imamaki, R., Ogawa, K., Komi, Y., Futakawa, Y., 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, in press.(2010) - Wada, Y., Dell, A., Haslam, S. M., Tissot, B., Canis, K., Azadi, P., Bäckström, B., Costello, C.E., Gunnar C. Hansson, Hiki, Y,, Ishihara, M., ItoH., Kakehi, K., Karlsson, N., Kato, K., Kawasaki, N., Khoo, K-H., Kobayashi, K., Kolarich, D., Kondo, A., Lebrilla, C., Nakano, M. , Narimatsu, H., Novak, J., Novotny, M. V., Ohno, E., Packer, N. H., Renfrow, M. B., Tajiri, M., Thomsson, K. H., Yagi, H., Yu, S-Y., and Taniguchi, N.:
"Comparison of Methods for Profiling O-glycosylation: HUPO Human Disease Glycomics/Proteome Initiative Multi-Institutional Study of IgA1."
Mol Cell Proteomics, in press. (2010) - 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) - Funakoshi, Y., and Suzuki, T.:
"Glycobiology in the cytosol: the bitter side of a sweet world."
Biochim. Biophys. Acta 1790, 81-94 (2009) - Haga, Y., Totani, K., Ito, Y.,and Suzuki, T.:
"Establishment of a real-time analytical method for free oligosaccharide transport from the ER to the cytosol."
Glycobiology 19, 987-994 (2009) - Hirayama, H., Seino, J., Kitajima, T., Jigami, Y., and Suzuki, T.:
"Free oligosaccharides to monitor glycoprotein endoplasmic reticulum-associated degradation in Saccharomyces cerevisiae."
J. Biol. Chem. 285, in press (2010) - Hanashima, S., Sato, K., .Ito, Y., and Yamaguchi, Y.:
"Silylene/oxazolidinone double-locked sialic acid building blocks for the efficient sialylation reaction in dichloromethane."
Eur. J. Org. Chem. 2009, 4215-4220 (2009) - Hanashima, S., Sato, K., .Ito, Y., and Yamaguchi, Y.:
"Synthesis of the starfish ganglioside AG2 pentasaccharide."
Tetrahedron Letters 50, 6150-6153 (2009) - Sakata, E., Satoh, T., Yamamoto, S., Yamaguchi, Y., Yagi-Utsumi, M., Kurimoto, E., Tanaka, K., Wakatsuki, S., and Kato, K.:
"Crystal structure of UbcH5b˜ubiquitin intermediate: Insight into the formation of the self-assembled E2˜Ub conjugates."
Structure 18, 138-147 (2010)