Premium
Characteristics of a breast cancer‐associated antigen defined by RCC‐1 antibody
Author(s) -
Tjandra J. J.,
Zalcberg J.,
Xing P.X.,
McKenzie I. F. C.
Publication year - 1990
Publication title -
immunology and cell biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.999
H-Index - 104
eISSN - 1440-1711
pISSN - 0818-9641
DOI - 10.1038/icb.1990.27
Subject(s) - antigen , epitope , antibody , monoclonal antibody , immunoperoxidase , breast cancer , neuraminidase , microbiology and biotechnology , cancer , chemistry , biology , immunology , medicine , biochemistry , enzyme
Summary This study reports the characterization of a breast cancer‐associated antigen identified by murine monoclonal antibody (MoAb) RCC‐1 (formerly called 24–17·1). Immunoperoxidase staining indicated that RCC‐1 recognized an antigen highly expressed in malignant tumours of breast origin, and no reactivity was noted with connective tissue, muscle or lymph nodes, which is an important consideration in its successful use in immunolymphoscintigraphy. The RCC‐1 was shown to consist of 94 000daiton disulfide‐bonded dimers which were shown to be different from the transferrin receptor. In addition, the antibody RCC‐1 did not react with components of human milk or with an antigenic peptide derived from the core protein of a mammary mucin. Chemical treatment and enzymatic digestion suggested that the epitope recognized by antibody RCC‐1 was protein as it was resistant to neuraminidase and periodate treatment but was sensitive to trypsin. The RCC‐1‐defined antigen detects a novel breast cancer associated antigen.