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Plasminogen activator activity of metastatic variants from a murine fibrosarcoma; effect of thrombin in vitro
Author(s) -
Coen Daniele,
Bottazzi Barbara,
Bini Alessandra,
Conforti Maria Grazia,
Mantovani Alberto,
Mussoni Luciana,
Donati Maria Benedetta
Publication year - 1983
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.2910320111
Subject(s) - in vitro , plasminogen activator , fibrosarcoma , fibrin , microbiology and biotechnology , thrombin , enzyme , neoplasm , activator (genetics) , antiserum , chemistry , urokinase , ht1080 , cancer research , biology , biochemistry , pathology , immunology , endocrinology , medicine , platelet , receptor , antigen , genetics
In order to investigate the possible correlation between plasminogen activator (PA) activity and metastatic potential of tumour cells, we studied cultured cells from the murine fibrosarcoma mFS6 and from its two sublines M 4 and M 9 which differ markedly in their capacity to cause spontaneous metastases in the lung. PA activity was detected in all the sublines by an amidolytic method and was almost completely inhibited by treatment with anti‐urokinase antiserum. No significant differences were shown between mFS6, M 4 and M 9 . Moreover, molecular analysis of PA by SDS‐PAGE electrophoresis and fibrin overlay revealed in all the cell types a single species having a mol. wt. of approximately 48,000 daltons. Thrombin treatment dramatically inhibited the amidolytic activity of all cells, suggesting a role for this enzyme in the modulation of fibrin formation and dissolution within the primary neoplasm.