An anti-carbohydrate monoclonal antibody inhibits cell-substratum adhesion of F9 embryonal carcinoma cells |
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| Authors: | S Nomoto H Muramatsu M Ozawa T Suganuma M Tashiro T Muramatsu |
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| Affiliation: | 1. Department of Biochemistry, Kagoshima University, School of Medicine, Kagoshima, 890 Japan;2. Department of Dermatology, Kagoshima University, School of Medicine, Kagoshima, 890 Japan;3. Department of Anatomy, Kagoshima University, School of Medicine, Kagoshima, 890 Japan;1. Department of Rheumatology and Immunology, Peking Union Medical College Hospital, Beijing, China;2. Department of Internal Medicine, Poznan University of Medical Sciences, Poznan, Poland;3. Department of Rheumatology and Connective Tissue Diseases, University Hospital No. 2, CM UMK, Bydgoszcz, Poland;4. First Affiliated Hospital of Zhengzhou University, Zhengzhou, China;5. Qilu Hospital of Shandong University, Jinan, China;6. Twoja Przychodnia Medyczne Centrum, Nowa Sól, Poland;7. The Third Affiliated Hospital of Sun Yat-sen University, Guangzhou, China;8. Tbilisi Heart and Vascular Clinic, Tbilisi, Georgia;9. National Pirogov Memorial Medical University, Vinnytsya, Ukraine;10. Bio-Thera Solutions, Guangzhou, China;11. Biogen International, Baar, Switzerland;12. Biogen Idec, Maidenhead, UK;1. Institute for Immunology, Tsinghua University, Beijing, China;2. Department of Basic Medical Sciences, School of Medicine, Tsinghua University, Beijing, China;3. Beijing Key Lab for Immunological Research on Chronic Diseases, Tsinghua University, Beijing, China;4. The Key Laboratory of Infection and Immunity, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China;5. The State Key Laboratory of Membrane Biology, Tsinghua-Peking Center for Life Sciences, School of Life Sciences, Tsinghua University, Beijing, China;1. Institute of Medical Microbiology and Hygiene, University of Freiburg Medical Center, 79104 Freiburg, Germany;2. Department of Internal Medicine IV, University of Freiburg Medical Center, 79106 Freiburg, Germany;3. Institute of Medical Microbiology and Hygiene, University of Mainz Medical Center, 55131 Mainz, Germany;4. International Max Planck Research School for Molecular and Cellular Biology, 79108 Freiburg, Germany;5. Faculty of Biology, 79104 Freiburg, Germany;6. BIOSS Center of Biological Signalling Studies, 79104 Freiburg, Germany;7. Laboratory of Transplantation Immunology, Departments of Biomedicine and Nephrology, University Hospital Basel, 4031 Basel, Switzerland;1. Peter Medawar Building for Pathogen Research, University of Oxford, Oxford OX2 3SY, UK;2. Reithera SRL (formerly Okairos SRL), Viale Città d’Europa 679, 00144 Rome, Italy;1. Division of Signaling and Gene Expression, La Jolla Institute for Allergy and Immunology, La Jolla, CA 92037, USA;2. Division of Vaccine Discovery, La Jolla Institute for Allergy and Immunology, La Jolla, CA 92037, USA;3. Department of Cancer Biology, The Scripps Research Institute, Jupiter, FL 33458, USA;4. Division of Cell Biology, La Jolla Institute for Allergy and Immunology, La Jolla, CA 92037, USA |
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| Abstract: | A monoclonal rat IgM antibody (4C9) raised against F9 embryonal carcinoma cells reacted with fucosyl residues in poly-N-acetyllactosamine-type large carbohydrates of these cells (embryoglycan). The chemical properties and distribution of the antigen resembled those of SSEA-1. The monoclonal antibody was found to inhibit cell-substratum adhesion of F9 cells: in the presence of the antibody, cells grew as spherical cell aggregates on plastic dishes. When the antibody was added to the already spread cells, they displayed the initial sign of rounding up within 3 h; the rounding process was largely completed within 6 h. After removal of the antibody, cells resumed their normal morphology. The antibody could act in the presence of 2,4-dinitrophenol. In serum-free medium, F9 cells spread on plastic dishes coated with fibronectin or with laminin, and the process was also inhibited by the antibody. Immuno-electronmicroscopy revealed that 4C9 antigen was diffusely distributed over the cell surface of F9 cells. The distribution of the antigen was not altered generally after culturing with the antibody for 6 h. Another monoclonal rat IgM antibody, which did not react with embryoglycan and resembled anti-Forssman, did not inhibit cell-substratum adhesion of F9 cells, in spite of its reactivity to the cells. Thus, a glycoprotein with fucosyl (poly)-N-acetyllactosamine structure appears to be involved in cell-substratum adhesion of F9 cells. |
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