Frontier Research Institute for Interdisciplinary Sciences
Tohoku University

Life is sustained by proteins. Approximately 20,000 genes encoding proteins in the human genome have been identified to date, and it is believed that over 100,000 types of proteins are translated from these genes. Approximately 40% of these are predicted to be membrane or secreted proteins, and most are known to have at least one disulfide bond. Disulfide bonds are covalent bonds between the respective thiol groups of two cysteine residues in proteins. The formation of disulfide bonds, which play an important role in the conformational stability of proteins, occurs primarily in the endoplasmic reticulum, one of the cellular organelles. It is known that disulfide bond formation and cleavage (redox reaction) occur in the extracellular environment and mediate changes in protein function such as activity, ligand affinity, localization, and multimerization. Compared to internal redox, extracellular redox is still less understood.

I have so far elucidated one part of the redox network within the endoplasmic reticulum (intracellular). In the future, I will expand the scope of my research to understand extracellular redox. Currently, my research focuses on the relationship between extracellular redox and the defense system, and I aim to "understand the biological defense system via extracellular redox" through interdisciplinary research that integrates biochemistry, structural biology, cell biology, virology, computational science, organic chemistry, and pharmaceutical science.