Kazuo Yamamoto / Professor / Division of Biosciences
Department of Integrated Biosciences / / Biology of lectin-sugar interaction

Career Summary
1979: Graduated, Faculty of Pharmaceutical Sciences, The University of Tokyo
1984: Doctor of Pharmaceutical Sciences from The University of Tokyo
1984-1986: Research Associate, The Tokyo Metropolitan Institute of Medical Sciences
1986-1997: Research Associate, The University of Tokyo
1997-1999: Associate Professor, The University of Tokyo
1999-present: Professor, The University of Tokyo
Educational Activities
Graduate school: Statistical Analysis for Biosciences, Frontiers in Molecular Biology I
and II, Breakthroughs Now and Then, Bio-Medicine, Drug Discovery.
Research Activities
1) Role of N-glycans on quality control of glycoproteins in cells.
Carbohydrate chains attached to proteins play key roles in intracellular and extracellular processes. Several types of glycans have vital biological functions in embryogenesis, cell development, cellular recognition, and transport outside the cells. In the cells, high mannose-type glycans are essential for the quality control of glycoproteins, especially the folding of newly synthesized proteins, degradation of misfolded proteins, and sorting and trafficking of correctly folded proteins. The glycan function in the cells is conserved in both lower and higher organisms, and such a glycosylation step is unique to N-glycans compared to other types of sugar chains modified by stepwise addition.
Quality control of glycoproteins is critically regulated by several intracellular sugar-binding proteins, lectins. To understand the quality control mechanism through molecular-based sugar-lectin interaction is a current topic of our studies.

2) Functional studies on new kinds of animal lectins.
The processing of N- and O-linked oligosaccharides in the Golgi apparatus occurs in highly divergent steps mediated by hundreds of glycosyltransferases, and the glycan structures thus produced differ in species and organs. Structurally diverse glycans are recognized by lectins, and lectin-mediated signaling sometimes causes several biological responses in the cells. To clarify the functional regulation of proteins mediated by sugar moieties, a genome-wide search of putative lectins was performed and new families of lectin-like receptors are being analyzed as a second topic of our research using biochemical, molecular biological, and cellular biological approaches.

3) Applied technology of designed cargo receptors on recombinant protein expression.
Based on knowledge of the quality control and cellular transport of glycoproteins, designed cargo receptors are applied to recombinant protein expression. To develop high-performance glycoprotein-based drugs, such an approach will enable us to create sugar chains at will and attach them to existing proteins, making them behave like new proteins.
1. N. Kawasaki, et al., Blood (2008) 111, 1972-1979.
2. Y. Kamiya, et al., J. Biol. Chem. (2008) 283, 1857-1861.
3. B. Nyfeler, et al., Blood (2008) 111, 1299-1301.
4. D. Yamaguchi, et al., Glycobiology (2007) 17, 1061-1069.
5. D. Nawa, et al., Glycobiology (2007) 117, 913-921.
6. N. Kawasaki, et al., J. Biochem. (2007) 141, 221-229.
7. K. Yamamoto, et al., Methods Mol. Biol. (2007) 381, 401-409.
8. M. Ito, et al., J. Exp. Med. (2006) 203, 289-295.
Other Activities
The Japanese Biochemical Society
The Japanese Society of Carbohydrate Research
The Pharmaceutical Society of Japan
The Japanese Society for Immunology
The Molecular Biology Society of Japan
The Japanese Society for Molecular Cell Biology of Macrophages
Future Plan
Our aim is to understand the sophisticated biological function of glycans, especially those attached to proteins, by analyzing the structure and function of sugar-recognizing
lectin molecules.
Messages to Students
Bioscience research areas are currently dramatically growing, and you have a chance to join and put your name in the history books.