Kyushu University Academic Staff Educational and Research Activities Database
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Hirohiko ISE Last modified date:2023.02.02

Associate Professor / Laboratory of Biomedical and Biophysical Chemistry
Department of Applied Molecular Chemistry
Institute for Materials Chemistry and Engineering

Graduate School
Undergraduate School

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 Reseacher Profiling Tool Kyushu University Pure
Academic Degree
Country of degree conferring institution (Overseas)
Field of Specialization
Cell biology, Biomaterials
Total Priod of education and research career in the foreign country
Research Interests
  • Regulation and elucidation of cellular function using carbohydrate-bearing polymers
    keyword : Cancer cell, glycochain, carbohydrate bearing polymer, cell function
Academic Activities
1. Beomju Hwang, Hirohiko Ise, Multimeric conformation of type III intermediate filaments but not the filamentous conformation exhibits high affinity to lipid bilayers, Genes Cells,, 25, 6, 413-426, 2020.04.
2. Hirohiko Ise ,Kumiko Matsunaga, Marie Shinohara, and Yasuyuki Sakai, Improved Isolation of Mesenchymal Stem Cells Based on Interactions between N-Acetylglucosamine-Bearing Polymers and Cell-Surface Vimentin, Stem Cells International,, 2019, 2019, 1-13, 2019.11.
3. Hirohiko Ise, Vimentin’s N-Acetylglucosamine-Binding Activity: Its Physiological Function, Trends Glycosci. Glycotechnol., 29, 169, E71-E79, 2017.09, Vimentin is known as a cytoskeletal protein that is expressed in mesenchymal and skeletal muscle tissues and plays an important role in the maintenance of the cytoplasmic architecture and cellular integrity. Moreover, vimentin is implicated in various cellular signal transduction pathways involved in cell proliferation and cell migration. Vimentin is highly expressed in lesion sites of various chronic diseases such as fibrosis, cancer, and autoimmune diseases. Vimentin’s high expression in various chronic diseases led to investigate its involvement in pathological mechanisms in chronic diseases. We recently reported that vimentin possesses N-acetyl-D-glucosamine (GlcNAc)-binding activity on cell surfaces. In this review, we describe vimentin’s GlcNAc-binding activity and discuss our hypothesis regarding its physiological relevance..
4. Hirohiko Ise, Sadanori Yamasaki, Kazuaki Sueyoshi, Yoshiko Miura, Elucidation of GlcNAc-binding properties of type III intermediate filament proteins, using GlcNAc-bearing polymers, Genes to Cells, 10.1111/gtc.12535, 22, 10, 900-917, 2017.10, Vimentin, desmin, glial fibrillary acidic protein (GFAP) and peripherin belong to type III intermediate filament family and are expressed in mesenchymal cells, skeletal muscle cells, astrocytes and peripheral neurons, respectively. Vimentin and desmin possess N-acetyl-d-glucosamine (GlcNAc)-binding properties on cell surfaces. The rod II domain of these proteins is a GlcNAc-binding site, which also exists in GFAP and peripherin. However, the GlcNAc-binding activities and behaviors of these proteins remain unclear. Here, we characterized the interaction and binding behaviors of these proteins, using various well-defined GlcNAc-bearing polymers synthesized by radical polymerization with a reversible addition-fragmentation chain transfer reagent. The small GlcNAc-bearing polymers strongly interacted with HeLa cells through vimentin expressed on the cell surface and interacted with vimentin-, desmin-, GFAP- and peripherin-transfected vimentin-deficient HeLa cells. These proteins present high affinity to GlcNAc-bearing polymers, as shown by surface plasmon resonance. These results show that type III intermediate filament proteins possess GlcNAc-binding activities on cell surfaces. These findings provide important insights into novel cellular functions and physiological significance of type III intermediate filaments..
5. Kim SJ, Ise H, Kim E, Goto M, Akaike T, Chung BH, Imaging and therapy of liver fibrosis using bioreducible polyethylenimine/siRNA complexes conjugated with N-acetylglucosamine as a targeting moiety, Biomaterials, 34, 6504-6514, 2013.09.
6. Komura K, Ise H, Akaike T, Dynamic behaviors of vimentin induced by interaction with GlcNAc molecules. Glycobiology, Glycobiology, 22, 1741-1759, 2012.12.
7. Ise H, Goto M, Akaike T, Engulfment and clearance of apoptotic cells based on a GlcNAc-binding lectin-like property of surface vimentin., Glycobiology, 22, 788-805, 2012.06.
8. Minato A, Ise H, Goto M, Akaike T, Cardiac differentiation of embryonic stem cells by substrate immobilization of insulin-like growth factor binding protein 4 with elastin-like polypeptides, Biomaterials, 33, 515-523, 2012.01.
9. Kim SJ, Ise H, Goto M, Akaike T, Interactions of vimentin- or desmin-expressing liver cells with N-acetylglucosamine-bearing polymers, Biomaterials, 33, 2154-2164, 2012.03.
10. Ise M, Ise H, Shiba Y, Kobayashi S, Goto M, Takahashi M,, Akaike T, Ikeda U, Targeting N-acetylglucosamine-bearing polymer-coated liposomes to vascular smooth muscle cells., J Artif Organs., 14, 310-309, 2011.12.
11. Kim SJ, Ise H, Goto M, Komura K, Cho CS, Akaike T, Gene delivery system based on highly specific recognition of surface-vimentin with N-acetylglucosamine immobilized polyethylenimine., Biomaterials, 32, 3471-3480, 2011.05.
12. Ise H, Kobayashi S, Goto M, Sato T, Kawakubo M, Takahashi M,, Ikeda U, Akaike T, Vimentin and desmin possess GlcNAc-binding lectin-like properties on cell surfaces, Glycobiology, 20, 843-864, 2010.07.
13. Kobayashi S, Ise H, Takahashi M, Goto M, Akaike T, Ikeda U, Surface coating of bone marrow cells with N-acetylglucosamine for bone marrow implantation therapy., Biomaterials, 30, 574-582, 2009.02.
14. Aso S, Ise H, Takahashi M, Kobayashi S, Morimoto H, Izawa A, Goto M, Ikeda U, Effective uptake of N-acetylglucosamine-conjugated liposomes by cardiomyocytes in vitro., J. Control Release, 122, 189-198, 2007.09.
15. Misawa R, Ise H, Takahashi M, Morimoto H, Kobayashi E, Miyagawa S, Ikeda U, Development of liver regenerative therapy using glycoside-modified bone marrow cells., Biochem Biophys Res Commun., 342, 434-440, 2006.04.
16. Ise H, Nikaido T, Negishi N, Sugihara N, Suzuki F, Akaike T, Ikeda U, Effective hepatocyte transplantation using rat hepatocytes with low asialoglycoprotein receptor expression. , Am. J. Pathol. , 165, 501-510, 2004.09.
17. Ise H, Sugihara N, Negishi N, Nikaido T, Akaike T, Low Asialoglycoprotein Receptor Expression as Markers for Highly Proliferative Potential Hepatocytes., Biochem. Biophys. Res. Commun., 285, 172-182, 2001.08.
18. Ise H, Ferdous A, Sugihara N, Nikaido T, Negishi N, Akaike T, Separation of Mouse Hepatocytes of Distinct Biological Phenotypes Based on Their Asialoglycoprotein Receptor-mediated Binding Affinity to an Artificial Ligand. , Journal of Artificial Organs., 165, 501-510, 1999.07.
19. Ise H, Takashima S, Nagaoka M, Ferdous A, Akaike T, Analysis of cell viability and differential activity of mouse hepatocytes under 3D and 2D culture in agarose gel., Biotechnology Letters., 21, 209-213, 1999.01.
20. Nonaka H, Ise H, Sugihara N, Hirose S, Negishi N, Kondo Y, Akaike T, Development of Highly Functional Long-Term Culture Method of Liver Slice Embeded in Polymer Scaffold for Bioartificial Liver., Cell Transplantation , 12, 491-498, 2003.06.
21. Nagaoka M, Ise H, Akaike T, Immobilized E-cadherin model can enhance cell attachment and differentiation of primary hepatocytes but not proliferation., Biotechnology Letters , 24, 1857-1862, 2002.10.
22. Hirose S, Ise H, Uchiyama M, Cho CS, Akaike T, Regulation of Asialoglycoprotein Receptor Expression in the Proliferative State of Hepatocytes., Biochem. Biophys. Res. Commun. , 287, 675-681, 2002.10.
23. Yang J, Goto M, Ise H, Cho CS, Akaike T, Galactosylated alginate as a scaffold for hepatocytes entrapment. , Biomaterials, 23, 471-479, 2002.10.
24. Kakegawa T, Ise H, Sugihara N, Nikaido T, Negishi N, Akaike T, Tanaka E, Soluble Asialoglycoprotein Receptors Reflect the Apoptosis of Hepatocytes. , Cell Transplantation, 11, 407-415, 2002.09.
Educational Activities
Plan, teaching, and marking of the practice for under graduate students.
Teaching and guiding for the thesis for master degree and graduation.