An NCI-designated Comprehensive Cancer Center
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Yoko Fujita-Yamaguchi, Ph.D.

Professor Emeritus, Diabetes & Metabolism Research Institute
Research Focus
  • Insulin & IGF signaling
  • Antibody therapeutics
  • Cancer
Appointments
Director, City of Hope-Japan Scientific & Educational Exchange Program; Adjunct Professor, Department of Molecular and Cellular Biology
Other Languages Spoken
  • Japanese

Selected Publications related to Insulin and IGF-I receptors

  • Fujita-Yamaguchi, Y., Choi, S., Sakamoto, Y. and Itakura, K. (1983)  Purification of insulin receptor with full binding activity.  J.Biol.Chem., 258:5045-5049
  • Kasuga, M., Fujita-Yamaguchi, Y., Blithe, D.L., and Kahn, C.R. (1983) Tyrosine-specific protein kinase activity is associated with the purified insulin receptor.  Proc.Natl. Acad.Sci., USA, 80:2137-2141.  
  • Fujita-Yamaguchi, Y. (1984) Characterization of purified insulin receptor subunits. J.Biol.Chem. 259:1206-1211.
  • LeBon, T. R., Jacobs, S., Cuatrecasas, P., Kathuria, S. and Fujita-Yamaguchi, Y. (1986) Purification of insulin-like growth factor (IGF)-I receptor from human placental membranes.  J.Biol.Chem., 261:7685-7689.  
  • Fujita-Yamaguchi, Y., LeBon, T., Tsubokawa, M., Henzel, W., Kathuria, S., Koyal, D., and Ramachandran, J. (1986)  Comparison of insulin-like growth factor (IGF)-I receptor and insulin receptor purified from human placental membranes.  J.Biol.Chem., 261:16727-16731.  
  • Ullrich, A., Gray, A., Tam, A.W., Yang-Feng, T., Tsubokawa, M., Collins, C., Henzel, W., LeBon, T., Kathuria, S., Chen, E., Jacobs, S., Francke, U., Ramachandran, J. and Fujita-Yamaguchi, Y.  (1986)  Insulin like growth factor I receptor primary structure:  Comparison with insulin receptor suggests structural determinants define functional specificity.  EMBO J. 5:2503-2512.  
  • Li, S.-L., Yan, P.-F., Paz, I.B., and Fujita-Yamaguchi, Y.  (1992)  Human insulin receptor β subunit transmembrane/cytoplasmic domain expressed in a baculovirus expression system:  Purification, characterization, and polylysine effects on the protein tyrosine kinase activity.  Biochemistry 31:12455-12462.
  • Yan, P.F., Li, S.-L., Liang, S.-J., Giannini, S., and Fujita-Yamaguchi, Y.  (1993) The role of C-terminal and acidic domains in the activity and stability of human insulin receptor protein tyrosine kinase studied by purified deletion-mutants of the β subunit.  J. Biol. Chem. 268:22444-22449.


Selected Publications related to antibody therapeutics and diagnostics

  • Fujita-Yamaguchi, Y. Production of Single-Chain Variable-Fragments against Carbohydrate Antigens. (2014) Antibodies 3, 155-168.

 

  • Fujita-Yamaguchi, Y. (2013) Renewed interest in basic and applied research involving monoclonal antibodies against an oncofetal Tn-antigen. J Biochem.152, 103-105.

 

  • Yuasa, N., Ogawa, H., Koizumi, T., Tsukamoto, K., Matsumoto-Takasaki, A., Asanuma, H., Nakada, H.,  and  Fujita-Yamaguchi, Y. (2012) Construction and expression of anti-Tn-antigen-specific single chain antibody genes from hybridoma producing MLS128 monoclonal antibody.  J Biochem. 151, 371-381.

 

  • Kusada, Y, Morizono, T., Matsumoto-Takasaki, A., Sakai, K., Sato, S., Asanuma, H.,Takayanagi, A., and Fujita-Yamaguchi, Y.  (2008) Construction and characterization of  single-chain antibodies against human insulin-like growth factor-1 Receptor from hybridomas producing 1H7 and 3B7 monoclonal antibody.  J. Biochem. 143, 9-19.

 

  • Li, S.-L., Liang, S.-J., Guo, N., Wu, A. M., and Fujita-Yamaguchi, Y. (2000) Single chain antibodies against human insulin-like growth factor-I receptor: Expression, purification, and effect on tumor growth. Cancer Immunol Immunother., 49, 243-252.

Selected Publications related to MLS128 anti-Tn antigen mAb and its colon cancer-specific receptor

  • Morita, N., Yajima, Y., Asanuma, H., Nakada, H., and Fujita-Yamaguchi, Y. (2009) Inhibition of cancer cell growth by anti-Tn monoclonal antibody MLS128. Biosci. Trends. 3, 32-37

 

  • Zamri, N., Masuda, N., Oura, F., Yajima, Y., Nakada, H., and Fujita-Yamaguchi, Y.(2012) Effects of two monoclonal antibodies, MLS128 against Tn-antigen and 1H7 against insulin-like growth factor-I receptor, on the growth of colon cancer cells. Biosci Trends., 6, 303-312.

 

  • Zamri, N., Masuda, N., Oura, F., Kabayama, K., Yajima, Y., Nakada,  H., Yamamoto, K., and Fujita-Yamaguchi, Y. (2013) Characterization of anti-Tn-antigen MLS128 binding proteins involved in inhibiting the growth of human colorectal cancer cells. Biosci Trend, 7, 221-229.

 

  • Oura, F., Yajima, Y., Nakata, M., Taniue, K., Akiyama, T., Nakada, H., Yamamoto, K., and Fujita-Yamaguchi, Y. (2015) Susceptibility to proteases of anti-Tn-antigen MLS128 binding glycoproteins expressed in human colon cancer cells. Biosci Trends. 9, 49-55.

Selected Publications related to sequence of SHA

  • Fujita, Y., Oishi, K., Suzuki, K., and Imahori, K. (1975) Purification and properties of anti-B hemagglutinin produced by Streptomyces sp.  Biochemistry 14:4465-4470.

 

  • Fujita-Yamaguchi, Y., Oishi, K., Suzuki, K., and Imahori, K. (1982) Studies on carbohydrate-binding to a lectin purified from Streptomyces sp.  Biochim.Biophys.Acta., 701:86-92.  

 

  • Bagramyan, K., Hong, T.B.,Murad, J.P., Fujita-Yamaguchi, Y., and Kalkum, M.  Mass spectrometric resurrection of SHA, a L-rhamnose and β-D-galactose binding lectin from the lost strain Streptomyces 27S5. 63rd American Society for Mass Spectrometry (ASMS) Conference, ThP307, Saint Louis, 31 May - 4 June, 2015.
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