## Abstract The properties of 121‐6 cells were characterized. This cell line is transformed by ts‐121, a temperature‐sensitive mutant of polyoma virus. Both the morphology and saturation density of the 121‐6 cells were affected by temperature; i.e. at 39° C, the cells grew to monolayer sheets and r
Cell cycle dependence of transformation expression in mouse cells transformed by a thermosensitive mutant (Ts-121) of polyoma virus
✍ Scribed by Yasuhiro S. Okada; Akira Hakura
- Publisher
- John Wiley and Sons
- Year
- 1979
- Tongue
- English
- Weight
- 675 KB
- Volume
- 100
- Category
- Article
- ISSN
- 0021-9541
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✦ Synopsis
Abstract
Change in division capability as a phenotypic expression of cellular transformation was investigated by using one of the temperature‐sensitive (ts) mutants of the polyoma virus‐transformed cell line, the 121‐6‐5 cells of BALB/3T3. When contact ‐inhibited cells were treated with hyaluronidase at 39°C, a single round of cell division was induced after which cell growth was inhibited by cell density. However, if the cells were incubated at 35°C, after the enzyme treatment, density‐inhibition block disappeared and the cells entered a second division. This indicates that the release of cells from density‐inhibition depends on the low temperature incubation. The ability of cells to complete a second division was examined by shifting the cells from 39°C to 35°C during different phases of the first division cycle after the enzyme‐treatment. A 6‐hour incubation of S phase cells at 35°C resulted in a second cycle of division, while the 24‐hour incubation of G1 cells at 35°C did not induce a second round of division. These results suggest that expression of the transformed phenotype in 121‐6‐5 cells is clearly dependent upon both the temperature and the phase of the division cycle.
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Abbreviations: ECM, extracellular matrix; SV40, simian virus 40; a-SMA, a-smooth cells were isolated from a single animal to develop homogeneous muscle actin; TGF-b1, transforming growth factor b1; PCR, polymerase chain reaction.
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