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Biomarker for breast cancer chemoprevention: Antimalignin antibody
Author(s) -
Bogoch Samuel,
Bogoch Elenore S.
Publication year - 1993
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.240531148
Subject(s) - antibody , antigen , cancer , cytotoxic t cell , in vitro , monoclonal antibody , biomarker , breast cancer , malignant transformation , medicine , immunology , microbiology and biotechnology , biology , chemistry , cancer research , biochemistry
Recognin M has been isolated from MCF‐7 malignant mammary cells. It is a 10 kD cancer polypeptide antigen rich in glutamic and aspartic acids related to malignin isolated from glial brain tumors (Glu13, Asp9, His2). An IgM auto‐antibody against Recognin M, antimalignin, has been isolated from human serum, produced both as a mouse monoclonal antibody and in human form by challenge of human lymphocytes with the antigen in vitro . It has been isolated from malignant cells obtained at surgery and autopsy by elution and immunoabsorption to its immobilized purified antigen. Antimalignin antibody is cytotoxic to malignant cells in vitro in concentrations of picograms/cell. In a 20‐year study involving several hundred physicians and three independent laboratories in the U.S., and three hospitals and one laboratory in the U.K., we have found that the concentration of antimalignin in serum, in μg/ml, (1) of normal healthy non‐tumor‐bearing humans increases moderately each decade between the third and the seventh, as the risk of cancer increases (p < 0.001; N = 1972), (2) increases earlier and more markedly in as yet apparently unaffected members of high‐risk cancer families (p < 0.001; N = 1106), and (3) is markedly increased in concentration in human serum within weeks of the occurrence of malignant transformation and returns to normal within 3 months of successful treatment (p < 0.001; false positive and false negatives < 5% on first determination, < 1% on repeat determination; N = 600). Quantitative determination of serum antimalignin antibody is therefore of interest for use as a noninvasive biomarker to indicate successful results in breast cancer chemoprevention trials. In addition, purified antimalignin antibody (MTAG), due to its demonstrated specificity in fluorescent and other chromogen staining of cell membranes with exposed malignin epitopes, is applicable for use alone or as part of a battery of pre‐dysplasia or dysplasia‐based surrogate endpoint biomarkers in both individual and computerized cytometry.