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Monoclonal antibody C3.1 is a platelet derived growth factor (PDGF) antagonist
Authors:R S Kawahara  B B Kennedy  T F Deuel
Affiliation:1. Department of Medicine, The Jewish Hospital of St. Louis, Washington University School of Medicine, 216 South Kingshighway Blvd., St. Louis, Missouri 63110 USA;2. Department of Biological Chemistry, The Jewish Hospital of St. Louis, Washington University School of Medicine, 216 South Kingshighway Blvd., St. Louis, Missouri 63110 USA;1. Department of Clinical Biochemistry, Ardabil University of Medical Sciences, Ardabil, Iran;2. Department of Nutrition, Khalkhal University of Medical Sciences, Khalkhal, Iran;3. Department of Anatomical Sciences, Ardabil University of Medical Sciences, Ardabil, Iran;4. Department of Plant Production and Genetics, University of Mohaghegh Ardabili, Iran;5. Department of Deutsch-Sprachen, Volkshochschule, Gütersloh, Germany;1. College of Pharmacy, Chung-Ang University, Seoul, 06974, Republic of Korea;2. Department of Global Innovative Drugs, Graduate School of Chung-Ang University, Seoul, 06974, Republic of Korea;3. Pohang Accelerator Laboratory, Pohang University of Science and Technology, Pohang, 790-784, Republic of Korea;1. State Key Laboratory of Cell Biology, Shanghai Institute of Biochemistry and Cell Biology, Center for Excellence in Molecular Cell Science, Chinese Academy of Sciences; University of Chinese Academy of Sciences, Shanghai 200031, China;2. Key Laboratory of Systems Health Science of Zhejiang Province, School of Life Science, Hangzhou Institute for Advanced Study, University of Chinese Academy of Sciences, Hangzhou, Zhejiang 310024, China;3. School of Life Science and Technology, ShanghaiTech University, Shanghai 201210, China
Abstract:A monoclonal antibody C3.1 raised against NR6 cells and partially purified PDGF receptor blocked PDGF stimulated [3H] thymidine incorporation in Swiss mouse 3T3 cells and immunoprecipitated a 180 kDa phosphoprotein from NR6 cells. The phosphoprotein bound to a C3.1 sepharose 4B affinity matrix and could be specifically eluted with PDGF but not by EGF or basic FGF. These preliminary results suggests that the ability of C3.1 to inhibit PDGF stimulated mitogenesis may be due to its direct or allosteric interaction at the PDGF receptor binding site.
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