scholarly journals Metabolic turnover of human c-rasH p21 protein of EJ bladder carcinoma and its normal cellular and viral homologs.

1984 ◽  
Vol 4 (8) ◽  
pp. 1647-1652 ◽  
Author(s):  
L S Ulsh ◽  
T Y Shih
Keyword(s):  
Bladder Carcinoma ◽  
Half Life ◽  
P21 Protein ◽  
Metabolic Turnover ◽  
Ras Genes ◽  
Murine Sarcoma Virus ◽  
Sarcoma Virus ◽  
Processed Products ◽  
Murine Sarcoma ◽  
P21 Proteins

The EJ bladder carcinoma oncogene is activated by a point mutation in the c-rasH proto-oncogene at the 12th amino acid codon. In an attempt to understand the mechanism of oncogenic activation, a comparative study was undertaken to examine the metabolic turnover and subcellular localization of the p21 protein encoded by the EJ oncogene, the viral oncogene, and its normal cellular homolog. Pulse-labeling experiments indicated that both c-ras p21 proteins were synthesized by a very similar pathway, as was observed for the viral p21 protein of Harvey murine sarcoma virus. The pro-p21 proteins were detected in free cytosol, and the processed products were associated with plasma membrane. The intracellular half-life of p21 proteins was determined by pulse-labeling and chasing in the presence of excess unlabeled methionine. Although both p21 proteins of EJ and the normal c-ras genes which are not phosphorylated have a half-life of 20 h, the viral p21 protein of Harvey murine sarcoma virus which includes a phosphorylated form is much more stable in cells, having a half-life of 42 h, apparently due to phosphorylation.

Metabolic turnover of human c-rasH p21 protein of EJ bladder carcinoma and its normal cellular and viral homologs

1984 ◽  
Vol 4 (8) ◽  
pp. 1647-1652
Author(s):  
L S Ulsh ◽  
T Y Shih
Keyword(s):  
Bladder Carcinoma ◽  
Half Life ◽  
P21 Protein ◽  
Metabolic Turnover ◽  
Ras Genes ◽  
Murine Sarcoma Virus ◽  
Sarcoma Virus ◽  
Processed Products ◽  
Murine Sarcoma ◽  
P21 Proteins

The EJ bladder carcinoma oncogene is activated by a point mutation in the c-rasH proto-oncogene at the 12th amino acid codon. In an attempt to understand the mechanism of oncogenic activation, a comparative study was undertaken to examine the metabolic turnover and subcellular localization of the p21 protein encoded by the EJ oncogene, the viral oncogene, and its normal cellular homolog. Pulse-labeling experiments indicated that both c-ras p21 proteins were synthesized by a very similar pathway, as was observed for the viral p21 protein of Harvey murine sarcoma virus. The pro-p21 proteins were detected in free cytosol, and the processed products were associated with plasma membrane. The intracellular half-life of p21 proteins was determined by pulse-labeling and chasing in the presence of excess unlabeled methionine. Although both p21 proteins of EJ and the normal c-ras genes which are not phosphorylated have a half-life of 20 h, the viral p21 protein of Harvey murine sarcoma virus which includes a phosphorylated form is much more stable in cells, having a half-life of 42 h, apparently due to phosphorylation.

scholarly journals Nucleotide sequence of the two rat cellular rasH genes.

1986 ◽  
Vol 6 (5) ◽  
pp. 1706-1710 ◽  
Author(s):  
M Ruta ◽  
R Wolford ◽  
R Dhar ◽  
D Defeo-Jones ◽  
R W Ellis ◽  
...  
Keyword(s):  
Amino Acids ◽  
Nucleotide Sequence ◽  
Coding Region ◽  
3T3 Cells ◽  
Ras Gene ◽  
P21 Protein ◽  
Murine Sarcoma Virus ◽  
Sarcoma Virus ◽  
Nih 3T3 ◽  
Murine Sarcoma

We present the nucleotide sequence of the coding region of the rat c-rasH-1 gene and a partial sequence analysis of the rat c-rasH-2 gene. By comparing these sequences with the Harvey murine sarcoma virus ras gene, we predict that the p21 protein encoded by the Harvey virus differs from the cellular c-rasH-1-encoded p21 at only two amino acids; those at positions 12 and 59. Alterations at each of these positions may play a role in activating the viral p21 protein. The c-rasH-2 gene is likely to be a nonfunctional pseudogene because it lacks introns, cannot be activated to transform NIH 3T3 cells, and differs in sequence from both c-rasH-1 and v-rasH at several base pair positions.

scholarly journals Characterization and developmental expression of a Drosophila ras oncogene.

1985 ◽  
Vol 5 (4) ◽  
pp. 885-889 ◽  
Author(s):  
B Mozer ◽  
R Marlor ◽  
S Parkhurst ◽  
V Corces
Keyword(s):  
Developmental Expression ◽  
Ras Oncogene ◽  
Coding Region ◽  
Ras Gene ◽  
Amino Acid Homology ◽  
Ras Genes ◽  
Human Counterpart ◽  
Murine Sarcoma Virus ◽  
Sarcoma Virus ◽  
Murine Sarcoma

We cloned a Drosophila melanogaster ras gene (Dmras64B) on the basis of its homology to the ras oncogen from Harvey murine sarcoma virus. This gene mapped at chromosomal position 64B on the left arm of the third chromosome. Sequencing of Dmras64B revealed extensive amino acid homology with the proteins encoded by the human and Saccharomyces cerevisiae ras genes. The coding region of the Drosophila gene is interrupted by two introns located in different positions with respect to its human counterpart. Dmras64B encodes three different RNAs (1.6, 2.1, and 2.6 kilobases long) that are constantly expressed throughout the development of the fly.

Nucleotide sequence of the two rat cellular rasH genes

1986 ◽  
Vol 6 (5) ◽  
pp. 1706-1710
Author(s):  
M Ruta ◽  
R Wolford ◽  
R Dhar ◽  
D Defeo-Jones ◽  
R W Ellis ◽  
...  
Keyword(s):  
Amino Acids ◽  
Nucleotide Sequence ◽  
Coding Region ◽  
3T3 Cells ◽  
Ras Gene ◽  
P21 Protein ◽  
Murine Sarcoma Virus ◽  
Sarcoma Virus ◽  
Nih 3T3 ◽  
Murine Sarcoma

We present the nucleotide sequence of the coding region of the rat c-rasH-1 gene and a partial sequence analysis of the rat c-rasH-2 gene. By comparing these sequences with the Harvey murine sarcoma virus ras gene, we predict that the p21 protein encoded by the Harvey virus differs from the cellular c-rasH-1-encoded p21 at only two amino acids; those at positions 12 and 59. Alterations at each of these positions may play a role in activating the viral p21 protein. The c-rasH-2 gene is likely to be a nonfunctional pseudogene because it lacks introns, cannot be activated to transform NIH 3T3 cells, and differs in sequence from both c-rasH-1 and v-rasH at several base pair positions.

Characterization and developmental expression of a Drosophila ras oncogene

1985 ◽  
Vol 5 (4) ◽  
pp. 885-889
Author(s):  
B Mozer ◽  
R Marlor ◽  
S Parkhurst ◽  
V Corces
Keyword(s):  
Developmental Expression ◽  
Ras Oncogene ◽  
Coding Region ◽  
Ras Gene ◽  
Amino Acid Homology ◽  
Ras Genes ◽  
Human Counterpart ◽  
Murine Sarcoma Virus ◽  
Sarcoma Virus ◽  
Murine Sarcoma

We cloned a Drosophila melanogaster ras gene (Dmras64B) on the basis of its homology to the ras oncogen from Harvey murine sarcoma virus. This gene mapped at chromosomal position 64B on the left arm of the third chromosome. Sequencing of Dmras64B revealed extensive amino acid homology with the proteins encoded by the human and Saccharomyces cerevisiae ras genes. The coding region of the Drosophila gene is interrupted by two introns located in different positions with respect to its human counterpart. Dmras64B encodes three different RNAs (1.6, 2.1, and 2.6 kilobases long) that are constantly expressed throughout the development of the fly.

Myeloproliferative virus, a cloned murine sarcoma virus with spleen focus-forming properties in adult mice.

1980 ◽  
Vol 33 (2) ◽  
pp. 573-582 ◽  
Author(s):  
W Ostertag ◽  
K Vehmeyer ◽  
B Fagg ◽  
I B Pragnell ◽  
W Paetz ◽  
...  
Keyword(s):  
Adult Mice ◽  
Murine Sarcoma Virus ◽  
Sarcoma Virus ◽  
Murine Sarcoma

Functional organization of the Harvey murine sarcoma virus genome.

1980 ◽  
Vol 35 (1) ◽  
pp. 76-92 ◽  
Author(s):  
E H Chang ◽  
J M Maryak ◽  
C M Wei ◽  
T Y Shih ◽  
R Shober ◽  
...  
Keyword(s):  
Functional Organization ◽  
Virus Genome ◽  
Murine Sarcoma Virus ◽  
Sarcoma Virus ◽  
Murine Sarcoma
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