scholarly journals Phosphorylation of Ribosomal Proteins in Sarcoma 180 Tumor Cells

1972 ◽  
Vol 247 (17) ◽  
pp. 5345-5350
Author(s):  
Lawrence Bitte ◽  
David Kabat
Keyword(s):  
Tumor Cells ◽  
Ribosomal Proteins ◽  
Sarcoma 180

scholarly journals Upregulation of 5′-terminal oligopyrimidine mRNA translation upon loss of the ARF tumor suppressor

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Kyle A. Cottrell ◽  
Ryan C. Chiou ◽  
Jason D. Weber
Keyword(s):  
Protein Synthesis ◽  
Tumor Cells ◽  
Ribosomal Proteins ◽  
Human Cancer ◽  
Mrna Translation ◽  
Ribosome Profiling ◽  
Translational Efficiency ◽  
Gene Encoding ◽  
Terminal Oligopyrimidine ◽  
Ribosome Export

AbstractTumor cells require nominal increases in protein synthesis in order to maintain high proliferation rates. As such, tumor cells must acquire enhanced ribosome production. How the numerous mutations in tumor cells ultimately achieve this aberrant production is largely unknown. The gene encoding ARF is the most commonly deleted gene in human cancer. ARF plays a significant role in regulating ribosomal RNA synthesis and processing, ribosome export into the cytoplasm, and global protein synthesis. Utilizing ribosome profiling, we show that ARF is a major suppressor of 5′-terminal oligopyrimidine mRNA translation. Genes with increased translational efficiency following loss of ARF include many ribosomal proteins and translation factors. Knockout of p53 largely phenocopies ARF loss, with increased protein synthesis and expression of 5′-TOP encoded proteins. The 5′-TOP regulators eIF4G1 and LARP1 are upregulated in Arf- and p53-null cells.

scholarly journals ARF suppresses 5’-terminal oligopyrimidine mRNA translation

2020 ◽  
Author(s):  
Kyle A. Cottrell ◽  
Ryan C. Chiou ◽  
Jason D. Weber
Keyword(s):  
Protein Synthesis ◽  
Tumor Cells ◽  
Ribosomal Proteins ◽  
Human Cancer ◽  
Mrna Translation ◽  
Ribosome Profiling ◽  
Translational Efficiency ◽  
Gene Encoding ◽  
Terminal Oligopyrimidine ◽  
Ribosome Export

AbstractTumor cells require nominal increases in protein synthesis in order to maintain high proliferation rates. As such, tumor cells must acquire enhanced ribosome production. How many of the mutations in tumor cells ultimately achieve this aberrant production is largely unknown. The gene encoding ARF is the most commonly deleted gene in human cancer. ARF plays a significant role in regulating ribosomal RNA synthesis and processing, ribosome export into the cytoplasm, and global protein synthesis. Utilizing ribosome profiling, we show that ARF is a major suppressor of 5’-terminal oligopyrimidine mRNA translation. Genes with increased translational efficiency following loss of ARF include many ribosomal proteins and translation factors. Knockout of p53 caused a similar increase in 5’-TOP mRNA translation. The 5’-TOP regulators mTORC1, eIF4G1 and LARP1 are dysregulated in ARF and p53 null cells.

scholarly journals Evolution of sarcoma 180 in mice infected with Trypanosoma cruzi

1983 ◽  
Vol 78 (3) ◽  
pp. 237-244
Author(s):  
Fausto Edmundo Lima Pereira ◽  
William Assad Sassine ◽  
Dimith Chequer Bouhabib ◽  
Elton de Almeida Lucas
Keyword(s):  
Weight Gain ◽  
Trypanosoma Cruzi ◽  
Tumor Cells ◽  
Ascitic Fluid ◽  
Tumor Development ◽  
Sarcoma 180 ◽  
Tumor Inoculation ◽  
Time Intervals ◽  
Tumor Challenge ◽  
Ascites Formation

Mice infected with Trypanosoma cruzi were challenged with 2x10[raised to the power of 6] cells of sarcoma 180 (ascite tumor) by i.p. route, on day seven post infection. Tumor development was followed by evaluation of weight gain, by measurement of ascitic fluid produced and enumeration of tumor cells in ascitic fluid. Infected mice were more resitant to tumor development as demonstrated by reduction in ascites formation and by reduction in the number of tumor cells in ascitic fluid, at different time intervals after tumor challenge. The number of peritoneal cells exsudated after tumor inoculation was greater in infected mice than in controls. This increased resitance of mice infected with T. cruzi to tumor development could be due to the action of macrophages activated by the infection and by the action of endotoxins absorbed from the gut or produced by the own parasite.

β-lapachone enhancement of lipid peroxidation and superoxide anion and hydrogen peroxide formation by Sarcoma 180 ascites tumor cells

1979 ◽  
Vol 28 (6) ◽  
pp. 723-728 ◽  
Author(s):  
Roberto Docampo ◽  
Fernando S. Cruz ◽  
Alberto Boveris ◽  
Ramiro P.A. Muniz ◽  
Darci M.S. Esquivel
Keyword(s):  
Hydrogen Peroxide ◽  
Lipid Peroxidation ◽  
Tumor Cells ◽  
Superoxide Anion ◽  
Sarcoma 180 ◽  
Ascites Tumor ◽  
Peroxide Formation ◽  
Hydrogen Peroxide Formation

Molecular changes in cell surface membranes resulting from trypsinization of sarcoma 180 tumor cells

1976 ◽  
Vol 426 (4) ◽  
pp. 630-637 ◽  
Author(s):  
John W. Huggins ◽  
Robert W. Chestnut ◽  
Norman N. Durham ◽  
Kermit L. Carraway
Keyword(s):  
Cell Surface ◽  
Tumor Cells ◽  
Sarcoma 180 ◽  
Molecular Changes

scholarly journals Cytoxicity and Apoptotic Mechanism of Ruthenium(II) Amino Acid Complexes in Sarcoma-180 Tumor Cells

PLoS ONE ◽  
2014 ◽  
Vol 9 (10) ◽  
pp. e105865 ◽  
Author(s):  
Aliny Pereira Lima ◽  
Flávia Castro Pereira ◽  
Marcio Aurelio Pinheiro Almeida ◽  
Francyelli Mariana Santos Mello ◽  
Wanessa Carvalho Pires ◽  
...  
Keyword(s):  
Amino Acid ◽  
Tumor Cells ◽  
Sarcoma 180 ◽  
Amino Acid Complexes ◽  
Apoptotic Mechanism

AUTORADIOGRAPHIC STUDIES OF THE DISTRIBUTION OF 1-AMINOCYCLOPENTANE CARBOXYLIC ACID IN NORMAL AND CANCEROUS MICE

1962 ◽  
Vol 40 (1) ◽  
pp. 1111-1114 ◽  
Author(s):  
L. Berlinguet ◽  
Nicole Bégin ◽  
L. M. Babineau
Keyword(s):  
Bone Marrow ◽  
Amino Acid ◽  
Carboxylic Acid ◽  
Tumor Cells ◽  
Ehrlich Ascites Tumor ◽  
Sarcoma 180 ◽  
Ascites Tumor ◽  
Ehrlich Ascites

Normal and cancerous mice were injected with 1-aminocyclopentane C14-carboxylic acid and the distribution of the drug in the animals was studied by autoradiography. In normal mice, the amino acid is concentrated selectively by the pancreas and the bone marrow. In cancerous mice (Ehrlich ascites tumor and sarcoma-180), the tumor cells also intensively accumulate the amino acid.

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