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Immunolocalization of collagenase in neoplastic epithelial cells
Author(s) -
Whitelock JM,
O'Grady RL,
Lyons JG
Publication year - 1989
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.1989.51
Subject(s) - collagenase , immunostaining , immunocytochemistry , antibody , biology , microbiology and biotechnology , fibroblast , western blot , cell culture , chemistry , enzyme , immunohistochemistry , pathology , in vitro , biochemistry , endocrinology , medicine , immunology , genetics , gene
Summary The distribution of interstitial collagenase in a rat mammary carcinoma model system has been studied by immunocytochemistry. Rabbit antibodies were raised against collagenase from neoplastic epithelial cells which were derived from an anaplastic, invasive, rat mammary carcinoma (BC1). Specificity of the antibodies was determined by Western blot analysis which showed reactivity with the inactive procollagenase from conditioned culture medium of BC1 cells as well as with purified, active BC1 collagenase. Anti‐BC1 collagenase antibodies did not recognize BC1 collagenase entrapped by the inhibitor, rat α‐2‐macroglobulin (α2M), or collagenase derived from TPA‐stimulated human fibroblasts. Anti‐human fibroblast collagenase antibodies did not recognize BC1 collagenase, suggesting that the human‐mesenchymal and rat‐epithelial enzymes are immunologically distinct molecules. Collagenase was immunolocalized intracellularly in BC1 cells cultured in the presence of monensin. Neither BC1 collagenase, α2M nor enzyme‐inhibitor complexes were demonstrated in or around invading tumours by immunostaining of tissue sections of rat mammary carcinomas.