Ehrlich ascites tumor cells produce a transforming growth factor-beta (TGFbeta)-like activity but lack receptors with TGFbeta-binding capacity

Ehrlich ascites tumor cells incorporate [methyl-3H]thymidine into DNA independently of exogenous growth factors or fetal calf serum. Using an acid/ethanol extraction procedure we have obtained from these tumor cells a fraction that induces both the proliferation and the formation of cell foci by Swi...

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Bibliographic Details
Published in:Molecular and cellular biochemistry 1997-05, Vol.170 (1-2), p.153-162
Main Authors: Elexpuru, A, Martín-Nieto, J, Jimenez, A, Gómez, C, Villalobo, A
Format: Article
Language:English
Subjects:
3T3 Cells
Animals
Carcinoma, Ehrlich Tumor - physiopathology
Cell Adhesion - drug effects
Cell Division
Cell Line
Culture Media, Conditioned
DNA - biosynthesis
Epidermal Growth Factor - pharmacology
Insulin - pharmacology
Lung
Mice
Mink
Rats
Receptors, Transforming Growth Factor beta - analysis
Tissue Extracts - pharmacology
Transforming Growth Factor beta - biosynthesis
Transforming Growth Factor beta - metabolism
Transforming Growth Factor beta - pharmacology
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Summary:Ehrlich ascites tumor cells incorporate [methyl-3H]thymidine into DNA independently of exogenous growth factors or fetal calf serum. Using an acid/ethanol extraction procedure we have obtained from these tumor cells a fraction that induces both the proliferation and the formation of cell foci by Swiss 3T3 mouse fibroblasts in the presence of insulin; inhibits the proliferation of Mv1Lu mink lung epithelial cells; and stimulates the growth of NRK rat kidney fibroblasts in soft-agar in the presence of epidermal growth factor. An antibody against transforming growth factor-beta (TGFbeta) prevents both the tumor extract-induced proliferation of Swiss 3T3 fibroblasts and the tumor extract-induced proliferative arrest of Mv1Lu cells. The tumor cells secrete a TGF beta-like activity to the extracellular medium in a partially-activated form. However, authentic TGFbeta does not affect their proliferation, and no TGFbeta receptors were detected using [125I]TGFbeta as a ligand. Therefore, the absence of TGFbeta receptors with ligand-binding capacity in these tumor cells may bypass the negative control that this factor exerts on the proliferation of their normal cell counterparts.
ISSN:0300-8177