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Characterization of a novel neuroglandular antigen (NGA) expressed on abnormal human melanocytes
Author(s) -
Sikora L. K. J.,
Demetrick D. J.,
Dixon W. T.,
Jerry L. M.,
Pinto A.,
Urbanski S. J.,
Temple W.
Publication year - 1987
Publication title -
international journal of cancer
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.475
H-Index - 234
eISSN - 1097-0215
pISSN - 0020-7136
DOI - 10.1002/ijc.2910390203
Subject(s) - antigen , monoclonal antibody , antibody , melanoma , microbiology and biotechnology , glycoprotein , staining , immunohistochemistry , biology , chemistry , pathology , immunology , medicine , cancer research
Abstract Murine monoclonal antibodies (MAbs) were produced with reactivity to human malignant melanoma. Six MAbs, 3 of the IgGI (LS113, LS140, LS152) and 3 of the IgG2a (LS59, LS62, LS76) subclasses, were selected for their binding, with an identical pattern of reactivity, to a novel melanoma‐associated antigen. As characterized by the enzyme‐linked immunosorbent assay (ELISA), these MAbs were found to be positive on n‐octyl‐β‐D‐glucopyranoside extracts of all 10 melanoma cell lines tested and on extracts of 22 metastatic melanoma tumors. The antibodies had minimal reaction with a panel of 14 normal adult tissue extracts. A degree of crossreactivity was observed with 50% of 39 non‐melanoma tumor extracts. The results obtained with the ELISA on cell line and tissue extracts were duplicated using the ABC method of peroxidase staining. The pattern of cross‐reactivity, as demonstrated by the intense staining of paraffin‐embedded and frozen tissue sections of normal, benign and malignant tissues, defines the recognized protein as a neuroglandular antigen (NGA). Immunoadsorbents made with the antibodies were used to purify the antigen shed from cultured melanomas. All 6 MAbs recognized this purified antigen while 5 other antimelanoma antibodies did not react with it. On gel electrophoresis this antigen is a highly glycosylated glycoprotein with a protein core of 21 kDa.