HOME > GCOE Organizing Members > Toyoshi Fujimoto MD, PhD

Toyoshi Fujimoto MD, PhDProfessor, Department of Molecular Cell Biology, Nagoya University Graduate School of Medicine
Specialized field
Anatomy and Cell Biology
Career Summary
- March, 1978
- Graduated from Kyoto University Faculty of Medicine
- April, 1978
- Assistant Professor, Department of Anatomy Kyoto University Faculty of Medicine
- February, 1982
- Associate Professor, Department of Anatomy
Kyoto University Faculty of Medicine - May, 1995
- Professor and Chairman
Department of Anatomy and Cell Biology
Gunma University School of Medicine - April, 1999-present
- Professor and Chairman
Department of Anatomy and Molecular Cell Biology
Nagoya University Graduate School of Medicine
Research Theme
Nano-scale analysis of lipid-based structures
Research Summary
Membrane microdomain (caveolae, rafts), lipid droplet, and autophagosome are formed based on the property of lipids, and thus we call them as lipid-based structures. Their abnormalities may lead to cancer, neurodegenerative diseases, obesity, liver steatosis, and other diseases. But the lipid-based structures are difficult to study by most conventional techniques. Our research goal is to develop a new ultrastructural technique to analyze the lipid-based structures. We have already established an electron microscopic method to visualize distribution of gangliosides at the nanometer scale, and are now trying to apply it to other membrane lipids to analyze their role in cancer invasion and autophagy. For lipid droplets, we showed previously that they are the platform of intracellular protein degradation processes, i.e., proteasomal and autophagic degradation. To extend the finding, we are now analyzing several candidate proteins that may be involved in the protein degradation process around the lipid droplet. By elucidating their functions at the cellular and the whole animal levels, we would like to understand their relationship with various diseases.
Principal Research Achievement
- Ohsaki Y et al. Lipid droplets are arrested in the ER membrane by tight binding of lipidated apolipoprotein B. J. Cell Sci. 121: 2415-2422 (2008)
- Fujita A et al. Gangliosides GM1 and GM3 in the living cell membrane form clusters susceptible to cholesterol depletion and chilling. Mol. Biol. Cell 18: 2812-2822 (2007)
- Ohsaki Y et al. Cytoplasmic lipid droplets are sites of convergence of proteasomal and autophagic degradation of apolipoprotein B. Mol. Biol. Cell 17: 2674-2683 (2006)
- Ozeki S et al. Rab18 localizes to lipid droplets and induces their close apposition to the endoplasmic reticulum-derived membrane. J. Cell Sci. 118: 2601-2611 (2005)
- Nomura R et al. Human coronavirus 229E binds to CD13 in raft and enters the cell through caveolae. J. Virol. 78: 8701-8708 (2004)
- Kogo H et al. Cell type-specific occurrence of caveolin-1alpha and -1beta in the lung caused by expression of distinct mRNAs. J. Biol. Chem. 279: 25574-25581 (2004)
- Tauchi-Sato K et al. The surface of lipid droplets is a phospholipid monolayer with a unique fatty acid composition. J. Biol. Chem. 277: 44507-44512 (2002)
- Torihashi S et al. Calcium oscillation linked to pacemaking of interstitial cell of Cajal; requirement of calcium influx and localisation of TRP4 in caveolae. J. Biol. Chem. 277: 19191-19197 (2002)
- Fujimoto T et al. Caveolin-2 is targeted to lipid droplets, a new ‘membrane domain’ in the cell. J. Cell Biol. 152: 1079-1085 (2001)
- Fujimoto T et al. Isoforms of caveolin-1 and caveolar structure. J. Cell Sci. 113: 3509-3517 (2000)
- Nomura R et al. Tyrosine phosphorylated caveolin-1: immunolocalization and molecular characterization. Mol. Biol. Cell 10: 975-986 (1999)
- Isshiki M et al. Endothelial Ca2+ waves preferentially originate at specific loci in caveolin-rich cell edges. Proc. Natl. Acad. Sci. USA. 95: 5009-5014 (1998)
- Saitou M et al. Occludin-deficient embryonic stem cells can differentiate into polarized epithelial cells bearing well-developed tight junctions. J. Cell Biol. 141: 397-408 (1998)
- Yamamoto-Hino M et al. Apical vesicles bearing inositol 1,4,5-trisphosphate receptors in the Ca2+ initiation site of ductal epithelium of submandibular gland. J. Cell Biol. 141: 135-142 (1998)
- Fujimoto K et al. Transmembrane phospholipid distribution revealed by freeze-fracture replica labeling. J. Cell Sci. 109: 2453-2460 (1996)
- Fujimoto T et al. Inositol 1,4,5-trisphosphate receptor-like protein in plasmalemmal caveolae is linked to actin filaments. J. Cell Sci. 108: 7-15 (1995)
- Fujimoto T. Calcium pump of the plasma membrane is localized in caveolae. J. Cell Biol. 120: 1147-1157 (1993)
- Fujimoto T et al. Localization of inositol 1,4,5-trisphosphate receptor-like protein in plasmalemmal caveolae. J. Cell Biol. 119: 1507-1513 (1992)
- Fujimoto T et al. Fodrin in the human polymorphonuclear leucocyte: redistribution induced by the chemotactic peptide. J. Cell Sci. 96: 477-484 (1990)
- Fujimoto T et al. Immunocytochemical studies of endothelial cells in vivo. I. The presence of desmin only, or of desmin plus vimentin, or vimentin only, in the endothelial cells of different capillaries of the adult chicken. J. Cell Biol. 103: 2775-2786 (1986)
Award
1988 Young Investigator Award
(The 8th International Congress on Histochemistry and Cytochemistry)
1996 Seto Award (The Society Award of The Japanese Society for Electron Microscopy)

