System Glycobiology Research Group
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.Through the above researches, we will establish systems glycobiology in order to understand glycan structure and function from integrative and dynamic aspects, which may develop biomarkers and therapeutics of the diseases such as cancer, infectious diseases, life style-related diseases, and neuromuscular degenerative diseases.
Additionally, our group continuously contributes to the activities of Japan Consortium for Glycobiology and Glycotechnology (JCGG), which is launched to integrate glycobiology and glycotechnology in Japan.
- 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
- Sano M, Korekane H, Ohtsubo K, Yamaguchi Y, Kato M, Shibukawa Y, Tajiri M, Adachi H, Wada Y, Asahi M, Taniguchi N.:
"N-glycans of SREC-I (Scavenger receptor expressed by endothelial cells) : Essential role for ligand binding, trafficking and stability."
Glycobiology. 2012 (in Press) - Korekane H, Hasegawa T, Matsumoto A, Kinoshita N, Miyoshi E, Taniguchi N.:
"Development of an antibody-lectin enzyme immunoassay for fucosylated α-fetoprotein."
Biochim Biophys Acta. 2011(in Press) - Y. Kizuka, S. Kitazume, M. Yoshida, N. Taniguchi,:
"Brain-specific expression of N-acetylglucosaminyltransferase IX (GnT-IX) is regulated by epigenetic histone modifications"
J. Biol. Chem. 2011, 286, 31875 - Taniguchi N, Korekane H.:
"Branched N-glycans and their implications for cell adhesion, signaling and clinical applications for cancer biomarkers and in therapeutics."
BMB Rep. 2011 Dec;44(12):772-81. - Haga, Y., Ishii, K., Suzuki, T.:
"N-glycan is essential for stability and intracellular trafficking of glucose transporter, GLUT4."
J. Biol. Chem. 2011, 286, 31320. - Kanagawa, M., Sato, T., Ikeda, A., Adachi, Y., Ohno, N., and Y. Yamaguchi,:
"Structural insights into recognition of triple-helical & beta-glucan by insect fungal receptor"
J. Biol. Chem., 2011, 286, 29158-29165. - Mitra, N., Banda, K., Altheide, TK., Schaffer, L., Johnson-Pais, TL., Beuten, J., Leach, RJ., Angata, T., Varki, N., Varki, A.:
"SIGLEC12, a human-specific segregating (pseudo)gene, encodes a signaling molecule expressed in prostate carcinomas"
J Biol Chem 2011, 286, 23003-11 - Fukuda, T., Hashimoto, H., Okayasu, N., Kameyama, A., Onogi, H., Nakagawasai, O., Nakazawa, T., Kurosawa, T., Hao, Y., Isaji, T., Tadano, T., Narimatsu, H., Taniguchi, N., Gu, J.:
"Alpha1,6-fucosyltransferase-deficient mice exhibit multiple behavioral abnormalities associated with a schizophrenia-like phenotype: importance of the balance between the dopamine and serotonin systems."
J. Biol. Chem. 2011, 286, 18434-18443 - 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) - Taniguchi,N.
"Toward cancer biomarker discovery using the glycomics approach."
Proteomics 8, 3205-3208.(2008)
Principal Investigator
- Naoyuki TANIGUCHI
- Group Director

