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  • Electronic Resource  (2)
  • growth factors  (1)
  • liver metastasis  (1)
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  • Electronic Resource  (2)
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  • 1
    ISSN: 1573-7276
    Keywords: B16 melanoma ; c-met ; HGF/SF ; liver metastasis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Metastasis to the liver is a frequent event in clinical oncology, the molecular mechanisms of which are not fully understood. We have recently reported a consistent overexpression of c-met in B16 melanoma cells selected in vivo for enhanced liver metastatic ability. In this study we address the question as to whether constitutive activation of c-met is a necessary and sufficient condition for enhanced liver colonization B16 melanoma cells. Different levels of c-met expression and/or activation in B16 cells were achieved subcloning, or by c-DNA transfection with either HGF/SF or the oncogenic form of c-met (tpr-met). Metastatic ability of the different populations was then evaluated in vivo by the lung colonization (experimental metastasis) assay. Results indicate that c-met (but not tpr-met) activation in B16 melanoma cells may increase their liver colonizing potential, probably by enhancing motility and invasion in response paracrine interactions with its ligand. C-met expres sion per se, however, is not able to change the organ specificity of the cells. C-met activation appears instead to be required at later stages of liver colonization by B16 melanoma cells, in order to enhance their site-specific metastatic ability. © Rapid Science 1998
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 0730-2312
    Keywords: oncogenes ; growth factors ; phosphotyrosine ; autocriny ; stomach cancer ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Phosphotyrosine (P-Tyr) antibodies have been used to identify the phosphorylated forms of growth factor receptors and oncogene-coded tyrosine kinases. Western blot analysis of a gastric carcinoma cell line with P-Tyr antibodies revealed a tyrosine-phosphorylated protein of Mr 145,000 (P145). In addition, in vitro phosphorylation with (γ-32P)ATP of P-Tyr immunoprecipitates of the same cells resulted in labelling of this protein on tyrosine. P145 appears to be a transmembrane glycoprotein, with features suggestive of a growth factor receptor. However, the in vivo or in vitro addition of known growth factors did not affect P145 tyrosine phosphorylation. We now report that P145 is rapidly dephosphorylated in vivo when cells are exposed to low pH, a condition known to dissociate ligands from their receptors. The addition of serum-free medium, conditioned by the gastric carcinoma cells, fully restores the tyrosine phosphorylation lost with acid treatment. These data suggest that the activity responsible for P145 phosphorylation on tyrosine, whether intrinsic to P145 itself or due to an associated kinase, is stimulated by a factor secreted by the tumor cells themselves.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
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