Professor Hiroshi Nakada

Area and Subject Taught Immunochemistry
Research Theme(s) Cancer Cell Characteristics and Their Effect on Immune Mechanisms
Academic Degrees Doctor of Pharmacology, Kyoto University
Keywords for Research Field Tumor Immunology, Glycobiology, Mucin
Office Phone Number 81-75-705-1897

Research Overview

Currently, one in every two to three Japanese dies of cancer. It is said that the 21st century will be the age of the life sciences, and one of the most expected advances is the discovery of a cure for cancer. Cancer cells are foreign matter within our bodies, and it is supposed to be the job of the body's immune defense to eliminate this kind of matter. However, cancer cells use clever methods to weaken our immune reactions or even to turn our immune systems against us, allowing themselves to multiply and spread. My research aims to elucidate, at the molecular level, the mechanism by which immunological competence is reduced, to develop methods to halt this process, and to apply these methods to new treatments for cancer. The most common cancer cells are derived from epithelial cells. This type of cell generates a glycoprotein called mucin, which is secreted into the cancerous tissue and blood of the patient. It is now becoming clear that this substance acts on the immune cells (monocytes/macrophages, B cells, NK cells, dendritic cells) via a variety of receptors, inhibiting their functioning. This research is one of central post-genome issues, and we anticipate that new advances can be made by combining it with research at the genetic level.

Notable Publications and Works in the Last Three Years

  1. K.Nogimori, T.Hori, K.Kawaguchi, T.Fukui, S.Mii, H.Nakada, Y.Matsumoto, Y.Yamauchi, M.Takahashi, K.Furukawa, O.Tetsuya, K.Yokoi, Y.Hasegawa, K.Furukawa. Increased expression levels of ppGalNAc-T13 in lung cancers: Significance in the prognostic diagnosis. Int J Oncol. 49;1369-1376 (2016)
  2. Y. Mori, K. Akita, M. Yashiro, T. Sawada, K. Hirakawa, T. Murata, H.Nakada, Binding of Galectin-3, a β-Galactoside-binding Lectin, to MUC1 Protein Enhances Phosphorylation of Extracellular Signal-regulated Kinase 1/2 (ERK1/2) and Akt, Promoting Tumor Cell Malignancy. J Biol Chem. 290; 26125-26140 (2015)
  3. F.Oura, Y.Yajima, M.Nakata, K.Taniue, T. Akiyama, H.Nakada, K.Yamamoto, Y.Fujita-Yamaguchi. Susceptibility to proteases of anti-Tn-antigen MLS128 binding glycoproteins expressed in human colon cancer cells. Biosci Trends. 9; 49-55 (2015)