A core protein epitope of the polymorphic epithelial mucin detected by the monoclonal antibody SM‐3 is selectively exposed in a range of primary carcinomas

Anne Girling, Jirina Bartkova, Joy Burchell, Sandra Gendler, Cheryl Gillett, Joyce Taylor‐Papadimitriou

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Abstract

The monoclonal antibody (MAb) SM‐3, which was raised to chemically deglycosylated milk mucin, reacts with an epitope present on the core protein of this mucin which we have referred to as PEM (polymorphic epithelial mucin). Although this mucin is abundantly expressed by both the lactating breast and breast carcinomas, the antibody SM‐3 shows very little or no reactivity on the former but does react with 92% of breast carcinomas. Furthermore, SM‐3 stains primary carcinomas of the lung, colon and ovary, but on the corresponding normal tissue the epitope is expressed at a much reduced level or not at all. These results indicate that an epitope masked in the normal mucin is exposed in the mucin produced by tumour cells, perhaps due to aberrant glycosylation. An extensive immunohistochemical study of other normal tissues reveals that the majority show only weak focal staining with SM‐3 or none at all, the distal tubules and collecting ducts of the kidney, and sebaceous glands being the only normal tissues studied to show homogeneously positive staining.

Original languageEnglish (US)
Pages (from-to)1072-1076
Number of pages5
JournalInternational Journal of Cancer
Volume43
Issue number6
DOIs
StatePublished - Jun 15 1989

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ASJC Scopus subject areas

  • Oncology
  • Cancer Research

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