scholarly journals Infection of chick limb bud presumptive chondroblasts by a temperature-sensitive mutant of Rous sarcoma virus and the reversible inhibition of their terminal differentiation in culture.

1983 ◽  
Vol 3 (8) ◽  
pp. 1518-1526 ◽  
Author(s):  
D Boettiger ◽  
R Soltesz ◽  
H Holtzer ◽  
M Pacifici
Keyword(s):  
Rous Sarcoma Virus ◽  
Limb Bud ◽  
Temperature Sensitive ◽  
Permissive Temperature ◽  
Nonpermissive Temperature ◽  
Sensitive Mutant ◽  
Temperature Sensitive Mutant ◽  
Rous Sarcoma ◽  
Sarcoma Virus ◽  
Infected Cells

Stage 21 to 22 chicken embryo limb bud cells were infected with a temperature-sensitive mutant of Rous sarcoma virus and were grown in culture. Although control, uninfected cells yielded definitive chondroblasts (by day 4) which initiated the synthesis of the cartilage-characteristic proteoglycan, the transformed cells grown at the permissive temperature failed to do so. These effects were fully reversible after a shift to the nonpermissive temperature. In addition, infected cells at the nonpermissive temperature expressed traits of terminal chondrogenic maturation 2 to 3 days earlier than parallel, uninfected cells. Thus, Rous sarcoma virus-induced transformation reversibly blocks terminal limb bud cell chondrogenesis in culture, at the nonpermissive temperature, viral infection may also induce intracellular or extracellular conditions which favor or accelerate the process of chondrogenic cell maturation.

Infection of chick limb bud presumptive chondroblasts by a temperature-sensitive mutant of Rous sarcoma virus and the reversible inhibition of their terminal differentiation in culture

1983 ◽  
Vol 3 (8) ◽  
pp. 1518-1526
Author(s):  
D Boettiger ◽  
R Soltesz ◽  
H Holtzer ◽  
M Pacifici
Keyword(s):  
Rous Sarcoma Virus ◽  
Limb Bud ◽  
Temperature Sensitive ◽  
Permissive Temperature ◽  
Nonpermissive Temperature ◽  
Sensitive Mutant ◽  
Temperature Sensitive Mutant ◽  
Rous Sarcoma ◽  
Sarcoma Virus ◽  
Infected Cells

Stage 21 to 22 chicken embryo limb bud cells were infected with a temperature-sensitive mutant of Rous sarcoma virus and were grown in culture. Although control, uninfected cells yielded definitive chondroblasts (by day 4) which initiated the synthesis of the cartilage-characteristic proteoglycan, the transformed cells grown at the permissive temperature failed to do so. These effects were fully reversible after a shift to the nonpermissive temperature. In addition, infected cells at the nonpermissive temperature expressed traits of terminal chondrogenic maturation 2 to 3 days earlier than parallel, uninfected cells. Thus, Rous sarcoma virus-induced transformation reversibly blocks terminal limb bud cell chondrogenesis in culture, at the nonpermissive temperature, viral infection may also induce intracellular or extracellular conditions which favor or accelerate the process of chondrogenic cell maturation.

Aggregation properties of chondrocytes infected with a temperature-sensitive mutant of Rous sarcoma virus

1980 ◽  
Vol 43 (1) ◽  
pp. 407-417
Author(s):  
A. Tanaka ◽  
A. Kaji
Keyword(s):  
Normal Level ◽  
Rous Sarcoma Virus ◽  
Cell Aggregation ◽  
Temperature Sensitive ◽  
Permissive Temperature ◽  
Sensitive Mutant ◽  
Temperature Sensitive Mutant ◽  
Rous Sarcoma ◽  
Sarcoma Virus ◽  
Level Of Aggregation

Aggregation capacity of chicken embryo chondrocytes decreases when transformed by Rous sarcoma viruses. Cell-to-cell aggregation capacity of chondrocytes infected with a T class temperature-sensitive mutant (tsNY68) (with the temperature-sensitive lesion at the src gene) of Rous sarcoma virus is dependent upon the temperature at which these cells are grown. When grown at the permissive temperature (36 degrees C), where the transforming gene is expressed, aggregation capacity was lower than normal while infected cells grown at the non-permissive temperature (41.5 degrees C) had similar capacity to aggregate to that of normal chondrocytes. However, after a prolonged period of culture (10 days), chondrocytes transformed by wild type SR-RSV regained the normal level of aggregation capacity. Cells transformed by tsNY68 and incubated at the permissive temperature for 10 days also regained the normal level of aggregation capacity. It appears therefore that RSV-transformed chondrocytes first become less adhesive but during long-term cultivation they regain their property to aggregate. The decrease of aggregation capacity due to T class mutants of RSV at 36 degrees C is dependent on constant maintenance of protein synthesis because addition of cycloheximide restored the aggregation capacity even at the permissive temperature.

Transformation of chicken embryo retinal melanoblasts by a temperature-sensitive mutant of rous sarcoma virus

Cell ◽  
1977 ◽  
Vol 11 (4) ◽  
pp. 881-890 ◽  
Author(s):  
Kate Roby ◽  
John Brumbaugh ◽  
Judy Biehl ◽  
Howard Holtzer ◽  
David Boettiger
Keyword(s):  
Rous Sarcoma Virus ◽  
Chicken Embryo ◽  
Temperature Sensitive ◽  
Sensitive Mutant ◽  
Temperature Sensitive Mutant ◽  
Rous Sarcoma ◽  
Sarcoma Virus

Phosphorylation of talin at tyrosine in Rous sarcoma virus-transformed cells

1987 ◽  
Vol 7 (1) ◽  
pp. 371-378
Author(s):  
J E DeClue ◽  
G S Martin
Keyword(s):  
Rous Sarcoma Virus ◽  
Peptide Mapping ◽  
Temperature Sensitive ◽  
Permissive Temperature ◽  
Sensitive Mutant ◽  
Tyrosine Residues ◽  
Rous Sarcoma ◽  
Sarcoma Virus ◽  
Chicken Embryo Fibroblasts ◽  
In Cells

The cytoskeletal protein talin was found to undergo enhanced phosphorylation at tyrosine residues in chicken embryo fibroblasts following transformation by Rous sarcoma virus. An increase in the tyrosine phosphorylation of talin was also observed within 6 h in cells infected by the temperature-sensitive mutant tsNY68 after a shift from the nonpermissive to the permissive temperature. The overall extent of phosphorylation was 0.07 mol of phosphate per mol of talin and was not appreciably altered by transformation. In uninfected cells talin was shown to be phosphorylated at multiple sites by tryptic peptide mapping. Following transformation most of these sites remained phosphorylated, to the same or to a lesser extent, while novel, phosphotyrosine-containing phosphopeptides appeared. Talin was phosphorylated at tyrosine in cells infected by Rous sarcoma virus mutants which induce altered or partial transformation morphologies; thus the increased phosphorylation of talin at tyrosine occurred irrespective of the morphology induced. Transformation by Y73 also induced elevated levels of phosphotyrosine in talin, whereas transformation by the avian erythroblastosis and Fujinami sarcoma viruses did not.

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