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BACKGROUND Nonhuman monoclonal antibodies (MoAbs) of desired specificities have been studied in cancer treatment and tumor targeting with minimal success. Attempts of using humanized chimeric antibodies have not improved significantly their clinical applications. We have engaged in the development of human MoAbs by incorporating the in vitro immunization protocols to the nodal lymphocytes of cancer patients. Three human MoAbs thus generated were found to be strongly reactive with various human malignancies. The antigens recognized by the three antibodies were selected for immunochemical and biochemical characterizations. METHODS The antigens investigated were AgSK1, PA 1-2 and PA 3-1. The patterns of each antigen expression in various human cancer cell lines were studied by the immunocytochemical staining technique. The expression of AgSK1 in association with cellular proliferation was examined by the flow cytometry analysis. In studying the biochemical natures of these antigens, their sensitivities toward various chemical and physical treatments were determined. The antigens that were shown to be proteins were subjected to SDS-PAGE and Western blot for estimations of molecular weights. RESULTS The AgSK1 was detected in 10 human carcinoma cell lines but in none of the melanoma cell lines. This suggests that SK1 may be an epithelial or carcinoma marker. The phenotypic expressions of AgSK1 were shown to be associated with proliferation of carcinoma cells. Biochemically AgSK1 was a sialophycoprotein with an estimated molecular weight of 42-44 kilodaltons (kDa). HuMAb PA1-2 demonstrated a unique staining pattern at both the cytoplasmic and intercellular interface. The stained filamentlike structures extending from cell to cell indicated that Ag PA1-2 might play a role in cellular interactions. Biochemically, Ag PA1-2 appeared to be an asialocarbohydrate. The Ag PA3-1 was a cytoplasmic glycoprotein expressed by all 13 cell lines. The estimated molecular weights of PA3-1 were 164, 104, and 40 kDa. CONCLUSIONS Tumor-associated antigens recognized by the human MoAbs may be more relevant clinically than those recognized by the mouse immune system. Carcinoma-specific human MoAbs are desirable for cancer treatment and tumor localization.
H R Chang, and
K Koda, and
M E McKnight, and
M C Glassy
January 1982,
Springer seminars in immunopathology,
H R Chang, and
K Koda, and
M E McKnight, and
M C Glassy
January 1984,
Critical reviews in immunology,
H R Chang, and
K Koda, and
M E McKnight, and
M C Glassy
May 1989,
Nihon Ketsueki Gakkai zasshi : journal of Japan Haematological Society,
H R Chang, and
K Koda, and
M E McKnight, and
M C Glassy
April 1987,
Proceedings of the National Academy of Sciences of the United States of America,
H R Chang, and
K Koda, and
M E McKnight, and
M C Glassy
January 1983,
Ciba Foundation symposium,
H R Chang, and
K Koda, and
M E McKnight, and
M C Glassy
June 1983,
Biochemical Society transactions,
H R Chang, and
K Koda, and
M E McKnight, and
M C Glassy
January 1983,
Bulletin du cancer,
H R Chang, and
K Koda, and
M E McKnight, and
M C Glassy
May 1986,
Cancer research,
H R Chang, and
K Koda, and
M E McKnight, and
M C Glassy
January 1984,
Archiv fur Geschwulstforschung,
H R Chang, and
K Koda, and
M E McKnight, and
M C Glassy
March 1988,
Human cell,
