Transformation-dependent secretion of a low molecular weight protein by murine fibroblasts.
AUTOR(ES)
Gottesman, M M
RESUMO
A protocol has been devised to radiolabel proteins secreted by murine fibroblasts in vitro. A radiolabeled polypeptide of molecular weight 35,000 is released into medium in relatively large amounts by transformed cells and in much smaller amounts by nontransformed fibroblasts. This major excreted polypeptide (MEP) is found in the medium of spontaneously transformed mouse cells and in the medium of mouse cells transformed by a DNA tumor virus, RNA tumor viruses, or methylcholanthrene. The appearance of MEP appears to be well correlated with anchorage independence in these transformed cells. MEP can be localized within the cytoplasm of transformed but not untransformed cells by indirect immunofluorescence. The presence of MEP within murine fibroblasts or in their culture medium serves as a novel biochemical marker of transformation. A biological role for this protein has not been assigned.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=392645Documentos Relacionados
- Transformation-dependent expression of interleukin genes delivered by a recombinant parvovirus.
- Transformation-dependent increases in endogenous cytochalasin-like activity in chicken embryo fibroblasts infected by Rous sarcoma virus.
- Transformation-dependent alterations in the oligosaccharides of Prague C Rous sarcoma virus glycoproteins.
- Transformation-dependent activation of urokinase-type plasminogen activator by a plasmin-independent mechanism: involvement of cell surface membranes.
- Retinoblastoma protein and simian virus 40-dependent immortalization of human fibroblasts.