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Procoagulant properties of human MV3 melanoma cells
Geaquinto, D. L. A; Fernandes, R. S; Lima, L. G; Barja-Fidalgo, C; Monteiro, R. Q.
Afiliación
  • Geaquinto, D. L. A; Universidade Federal do Rio de Janeiro. Centro de Ciências da Saúde. Instituto de Bioquímica Médica. Rio de Janeiro. BR
  • Fernandes, R. S; Universidade Federal do Rio de Janeiro. Centro de Ciências da Saúde. Instituto de Bioquímica Médica. Rio de Janeiro. BR
  • Lima, L. G; Universidade Federal do Rio de Janeiro. Centro de Ciências da Saúde. Instituto de Bioquímica Médica. Rio de Janeiro. BR
  • Barja-Fidalgo, C; Universidade do Estado do Rio de Janeiro. Instituto de Biologia. Departamento de Farmacologia. Rio de Janeiro. BR
  • Monteiro, R. Q; Universidade Federal do Rio de Janeiro. Centro de Ciências da Saúde. Instituto de Bioquímica Médica. Rio de Janeiro. BR
Rev. bras. pesqui. méd. biol ; Braz. j. med. biol. res;41(2): 99-105, Feb. 2008. graf
Article en En | LILACS | ID: lil-474760
Biblioteca responsable: BR1.1
ABSTRACT
A correlation between cancer and prothrombotic states has long been described. More recently, a number of studies have focused on the procoagulant mechanisms exhibited by tumor cells. In the present study, we dissected the molecular mechanisms responsible for the procoagulant activity of MV3, a highly aggressive human melanoma cell line. It was observed that tumor cells strongly accelerate plasma coagulation as a result of i) expression of the blood clotting initiator protein, a tissue factor, as shown by flow cytometry and functional assays (factor Xa formation in the presence of cells and factor VIIa), and ii) direct activation of prothrombin to thrombin by cells, as evidenced by hydrolysis of the synthetic substrate, S-2238, and the natural substrate, fibrinogen. This ability was highly potentiated by the addition of exogenous factor Va, which functions as a co-factor for the enzyme factor Xa. In contrast, prothrombin activation was not observed when cells were previously incubated with DEGR-factor Xa, an inactive derivative of the enzyme. Moreover, a monoclonal antibody against bovine factor Xa reduced the prothrombin-converting activity of tumor cells. In conclusion, the data strongly suggest that MV3 cells recruit factor Xa from the culture medium, triggering an uncommon procoagulant mechanism.
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Texto completo: 1 Colección: 01-internacional Base de datos: LILACS Asunto principal: Protrombina / Tromboplastina / Cisteína Endopeptidasas / Trombina / Melanoma / Proteínas de Neoplasias Límite: Humans Idioma: En Revista: Braz. j. med. biol. res / Rev. bras. pesqui. méd. biol Asunto de la revista: BIOLOGIA / MEDICINA Año: 2008 Tipo del documento: Article País de afiliación: Brasil Pais de publicación: Brasil
Texto completo: 1 Colección: 01-internacional Base de datos: LILACS Asunto principal: Protrombina / Tromboplastina / Cisteína Endopeptidasas / Trombina / Melanoma / Proteínas de Neoplasias Límite: Humans Idioma: En Revista: Braz. j. med. biol. res / Rev. bras. pesqui. méd. biol Asunto de la revista: BIOLOGIA / MEDICINA Año: 2008 Tipo del documento: Article País de afiliación: Brasil Pais de publicación: Brasil