Cultures from adult rat liver cells I. Establishment of monolayer cell-cultures from normal liver

1971 ◽  
Vol 78 (2) ◽  
pp. 281-288 ◽  
Author(s):  
P. T. Iype
Keyword(s):  
Rat Liver ◽  
Cell Cultures ◽  
Normal Liver ◽  
Liver Cells ◽  
Monolayer Cell ◽  
Adult Rat ◽  
Rat Liver Cells

The assessment of glucagon binding in isolated intact neonatal and adult rat liver cells

1980 ◽  
Vol 301 (2) ◽  
pp. 191-192 ◽  
Author(s):  
V. Osterthun ◽  
T. Haas ◽  
F. Peters ◽  
M. Petry ◽  
I. Trautschold
Keyword(s):  
Rat Liver ◽  
Liver Cells ◽  
Adult Rat ◽  
Rat Liver Cells

Promotion of 3′-methyl-4-dimethylaminoazobenzene-initiated adult rat liver cells to malignant state by phenobarbital in culture

1986 ◽  
Vol 37 (5) ◽  
pp. 769-773 ◽  
Author(s):  
Masahiro Miyazaki ◽  
Yoshihiko Handa ◽  
Yasunori Suzuki ◽  
Jiro Sato
Keyword(s):  
Rat Liver ◽  
Liver Cells ◽  
Adult Rat ◽  
Rat Liver Cells ◽  
Malignant State

Expression of gamma-glutamyl transpeptidase in adult rat liver cells after transformation with SV40 virus

1984 ◽  
Vol 22 (1) ◽  
pp. 31-39 ◽  
Author(s):  
C. Lafarge-Frayssinet ◽  
S. Estrade ◽  
B. Rosa-Loridon ◽  
C. Frayssinet ◽  
R. Cassingena
Keyword(s):  
Rat Liver ◽  
Liver Cells ◽  
Gamma Glutamyl Transpeptidase ◽  
Sv40 Virus ◽  
Gamma Glutamyl ◽  
Adult Rat ◽  
Rat Liver Cells ◽  
Glutamyl Transpeptidase

The M1 subunit of rat liver ribonucleotide reductase appears to be modified by ubiquitination

1992 ◽  
Vol 70 (3-4) ◽  
pp. 215-223 ◽  
Author(s):  
Marianna Sikorska ◽  
Joanna Kwast-Welfeld ◽  
Tony Youdale ◽  
Robert Richards ◽  
James F. Whitfield ◽  
...  
Keyword(s):  
Rat Liver ◽  
Ribonucleotide Reductase ◽  
Reductase Activity ◽  
Normal Liver ◽  
Liver Cells ◽  
Synthetic Activity ◽  
M1 Protein ◽  
Rat Liver Cells ◽  
Molecular Masses ◽  
Morris Hepatoma

Using a combination of immunoblotting, double immunoprecipitation, immunoglobulin-affinity chromatography, and isoelectrofocusing, we have been able to identify a group of proteins that display CDP-reductase activity and contain antigenic epitopes recognized by anti-ribonucleotide reductase M1 subunit and anti-ubiquitin antibodies. In the cytoplasm of rat liver cells, we could detect a total of five proteins with molecular masses of 92, 89, 56, 45, and 37 kilodaltons which reacted with the anti-M1 subunit serum. All of them, except the 89-kilodalton protein (the nascent unmodified M1), were also recognized by the anti-ubiquitin antibody. In normal liver cells, all of the apparently ubiquitinated species of the M1 protein were found in the cytoplasm, but not in the nuclear envelope associated pool of the enzyme. However, we did not detect ubiquitinated M1 protein fragments in the cytoplasm of Morris hepatoma 5123tc. The level of the apparently ubiquitinated fragments of the M1 subunit increased in parallel to the DNA-synthetic activity of normal liver cells, suggesting that ubiquitination plays a key role in the regulation of the activity of the enzyme during the cell cycle.Key words: ribonucleotide reductase turnover, proteolysis, ubiquitin, DNA replication.

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