Affiliations: [a] Morinaga Institute of Biological Science, Yokohama, Japan | [b] Department of Food Science and Technology, Faculty of Agriculture, Kyushu University, Fukuoka, Japan | [c] Department of Immunology, Medical Institute of Bioregulation, Kyushu University, Fukuoka, Japan
Note: [] Address reprint requests to: Dr. Masatoshi Kato, Morinaga Institute of Biological Science, 2-1-1 Shimosueyoshi, Tsurumi-ku, Yokohama 230, Japan.
Abstract: Histone H2B was demonstrated to be an immunoreactive material recognized by the human monoclonal antibody HB4C5, which had been already established to be specific for lung cancers. The inhibitory effect of histone H2B on the activity of HB4C5 antibody to immunostain the cytoplasmic antigen in lung adenocarcinoma tissue indicated that histone H2B at least had antigenic determinant comparable to the cytoplasmic antigen. A mouse anti-histone H2B monoclonal antibody could immunostain the cytoplasm of lung adenocarcinoma cells in sliced tissue sections in the same manner as the human monoclonal antibody HB4C5. Enzyme-linked immunosorbent assay of HB4C5 antibody on plastic immunoplates coated with histone H2B also showed specific reactivity of this antibody with histone H2B, and the reaction was effectively inhibited when extra histone H2B or mouse anti-histone H2B monoclonal antibody was added to the reaction mixture. These results consistently lead us to a conclusion that histone H2B possesses antigenicity to the human monoclonal antibody HB4C5.
Keywords: histone H2B, cancer marker, lung adenocarcinoma, human monoclonal antibody
