Growth Hormone Induction of Ornithine Decarboxylase in Rat Liver

Endocrinology ◽  
1970 ◽  
Vol 86 (6) ◽  
pp. 1414-1419 ◽  
Author(s):  
DIANE H. RUSSELL ◽  
SOLOMON H. SNYDER ◽  
VICENTE J. MEDINA
Keyword(s):  
Growth Hormone ◽  
Ornithine Decarboxylase ◽  
Rat Liver

scholarly journals Subcellular localization of ornithine decarboxylase in liver of control and growth-hormone-treated rats

1976 ◽  
Vol 157 (1) ◽  
pp. 33-39 ◽  
Author(s):  
B J Murphy ◽  
M E Brosnan
Keyword(s):  
Growth Hormone ◽  
Ornithine Decarboxylase ◽  
Rat Liver ◽  
Subcellular Fractionation ◽  
Decarboxylase Activity ◽  
Differential Centrifugation ◽  
Marker Enzymes ◽  
Aminotransferase Activity ◽  
Apparent Affinity ◽  
Hormone Administration

1. Ornithine-2-oxo acid aminotransferase activity was inhibited by amino-oxyacetate (10(-5) M). This permitted the measurement of ornithine decarboxylase in the presence of mitochondria by using the 14CO2-trapping technique. 2. Subcellular fractionation of rat liver by differential centrifugation, followed by the assay of ornithine decarboxylase in the presence of amino oxyacetate and of marker enzymes for each fraction, demonstrated that ornithine decarboxylase was located in the cytosol. 3. The greatly increased ornithine decarboxylase activity observed after growth-hormone administration was also found to be localized in the cytosol. 4. The Km of ornithine decarboxylase from rat liver for ornithine was 28 muM. Administration of growth hormone 4 h before death did not affect the apparent affinity of ornithine decarboxylase for ornithine.

The nuclear 3,5,3'-triiodothyronine receptor in human leukaemic cell lines

1984 ◽  
Vol 105 (3) ◽  
pp. 429-432 ◽  
Author(s):  
Juan Bernal ◽  
Leif C. Andersson
Keyword(s):  
Growth Hormone ◽  
Cell Line ◽  
Cell Lines ◽  
Rat Liver ◽  
Association Constant ◽  
Erythroid Differentiation ◽  
Leukaemic Cell ◽  
Cells In Culture ◽  
Gh Cells ◽  
High Concentrations

Abstract. The 3,5,3'-triiodothyronine (T3) receptor has been studied in a series of continuously growing human leukaemic cell lines. High concentrations of receptor were found in the erythroblastoid cell line K-562. T3 was bound to the nuclei of these cells with an association constant of 3.4 × 109 m−1, and capacity 104 fmol/100 μg DNA, or 8700 molecules/nucleus. This capacity is comparable to that of rat liver or growth hormone producing cells (GH cells) in culture, and suggests that the K-562 cell line could be a useful model for the study of T3 action on erythroid differentiation.

scholarly journals Pretranslational regulation of alpha 2u-globulin in rat liver by growth hormone.

1982 ◽  
Vol 257 (13) ◽  
pp. 7834-7838 ◽  
Author(s):  
A K Roy ◽  
B Chatterjee ◽  
W F Demyan ◽  
T S Nath ◽  
N M Motwani
Keyword(s):  
Growth Hormone ◽  
Rat Liver

scholarly journals A macromolecular inhibitor of the antizyme to ornithine decarboxylase

1982 ◽  
Vol 204 (3) ◽  
pp. 647-652 ◽  
Author(s):  
K Fujita ◽  
Y Murakami ◽  
S Hayashi
Keyword(s):  
Ornithine Decarboxylase ◽  
Rat Liver ◽  
Molecular Size ◽  
Antizyme Inhibitor ◽  
Heat Labile

A macromolecular factor that inhibits the activity of the antizyme to ornithine decarboxylase (ODC) was found in rat liver extracts. The factor, ‘antizyme inhibitor’, was heat-labile, non diffusable and of similar molecular size to ODC. The antizyme inhibitor re-activated ODC that had been inactivated by antizyme, apparently by replacing ODC in a complex with antizyme. Therefore the antizyme inhibitor can be used to assay the amount of inactive ODC-antizyme complex formed in vitro. When assayed by this method, the complex was shown to be eluted before ODC from a Sephadex G-100 column. Significant increase in ODC activity was observed when the antizyme inhibitor was added to crude liver extracts from rats that had been injected with 1,3-diaminopropane to cause decay of ODC activity, suggesting the presence of inactive ODC-antizyme complex in the extracts.

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