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Measurement of plasminogen activator activity from human fibrosarcoma cells by a new microassay
Author(s) -
Rezaee M.,
Chen L.,
Kramer R. H.
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.2910400620
Subject(s) - fibrosarcoma , plasminogen activator , activator (genetics) , chemistry , medicine , pathology , biology , microbiology and biotechnology , cancer research , endocrinology , biochemistry , gene
Abstract Elevated levels of plasminogen activator (PA) activity have been correlated with neoplasia and may have an important role in tumor‐cell invasion and metastasis. We have developed a new caseinolytlc assay that uses an immunochemical approach to measure the activity of PA elaborated by malignant tumor cells. The highly sensitive assay consists in incubating a source of PA (viable tumor cells, cell extracts, or conditioned medium) with purified plasminogen in micro titer plates pre‐coated with a suitable protein substrate such as casein. Clearance of the immobilized protein substrate by PA‐generated plasmin is then measured by a technique based on the enzyme‐linked immunosorbent assay. In experiments using uro‐kinase as a source of PA, the assay displayed near linearity over several log units of urokinase activity and could detect is little as 10 −2 Ploug units of PA activity. Besides successfully measuring PA activity produced by the human HT1080 fibro‐sarcoma cell line, the assay permitted detection of significant plasminogen‐independent proteolytic activity generated by intact tumor cells cultured in direct contact with immobilized protein substrates.

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