miR27a, a fine-tuning molecule, interacts with growth hormone (GH) signaling and ornithine decarboxylase (ODC) via targeting STAT5

Amino Acids ◽  
2021 ◽  
Author(s):  
Ajda Coker-Gurkan ◽  
Kadriye Koyuncu ◽  
Pinar Obakan Yerlikaya ◽  
Elif Damla Arisan
Keyword(s):  
Growth Hormone ◽  
Ornithine Decarboxylase ◽  
Fine Tuning

Growth hormone inhibition of lipogenesis in sheep adipose tissue: requirement for gene transcription and polyamines

1994 ◽  
Vol 142 (2) ◽  
pp. 235-243 ◽  
Author(s):  
C A Borland ◽  
M C Barber ◽  
M T Travers ◽  
R G Vernon
Keyword(s):  
Growth Hormone ◽  
Adipose Tissue ◽  
Fatty Acid ◽  
Ornithine Decarboxylase ◽  
Gene Transcription ◽  
Actinomycin D ◽  
Total Activity ◽  
Decarboxylase Activity ◽  
Polyamine Biosynthesis

Abstract The chronic inhibitory effect of growth hormone (GH) on lipogenesis in sheep adipose tissue explants was investigated in an in vitro tissue culture system. In the absence of other hormones, GH caused a decrease in the rate of lipogenesis after 6 h of culture. In contrast, when lipogenesis was stimulated by the presence of insulin plus dexamethasone, GH again decreased lipogenesis but after a lag of at least 12 h. Actinomycin D, an inhibitor of gene transcription, prevented the effect of GH on lipogenesis in both the absence and presence of insulin plus dexamethasone. Actinomycin D added to tissue previously incubated for 6 h in the presence of GH alone prevented further decline in lipogenesis over the next 5 h, suggesting that transcription of a short-lived mediator protein is required for the GH effect to occur. An increase in ornithine decarboxylase activity was detected in explants exposed to GH, reaching a peak after 12 h incubation; this was prevented by actinomycin D. Methylglyoxal bis-(guanylhydrazone), an inhibitor of polyamine biosynthesis, partially alleviated the effect of GH on lipogenesis; this was reversed by addition of spermidine. However, spermidine did not reverse the effects of actinomycin D, implicating a short-lived protein in addition to ornithine decarboxylase in the action of GH. In the absence of other hormones GH had no effect on either the expressed (initial) or total activity of acetyl-CoA carboxylase, but GH prevented the increase in both expressed and total activities of the enzyme induced by insulin plus dexamethasone. Varying lipolysis and fatty acid accumulation in adipose tissue by addition of adenosine deaminase plus indomethacin or bovine serum albumin to the culture medium had no effect on lipogenesis and these agents partly alleviated GH inhibition of lipogenesis. No effect of GH was found on the amount of glycerol released by cultured tissue. GH also had no effect on fatty acid esterification. Thus the chronic inhibitory effects of GH on lipogenesis involve a protein with a very short half-life. The effect also requires polyamines but does not appear to involve changes in fatty acid concentrations in the cell. In addition GH appears to inhibit lipogenesis and to antagonise insulin-stimulation of lipogenesis by different mechanisms. Journal of Endocrinology (1994) 142, 235–243

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.

Restriction fragment length polymorphisms at the ornithine decarboxylase locus associated with milk protein yield in Holsteins

1998 ◽  
Vol 65 (2) ◽  
pp. 341-345
Author(s):  
JIANBO YAO ◽  
SAMUEL E. AGGREY ◽  
DAVID ZADWORNY ◽  
URS KÜHNLEIN ◽  
J. FLAN HAYES
Keyword(s):  
Growth Hormone ◽  
Mammary Gland ◽  
Growth Factors ◽  
Candidate Genes ◽  
Ornithine Decarboxylase ◽  
Milk Production ◽  
Production Traits ◽  
Milk Production Traits ◽  
Gene Markers ◽  
Ample Evidence

Marker-assisted selection may provide the opportunity to make significant genetic gains in the improvement of economically important traits in livestock (Soller & Beckmann, 1983; Smith & Simpson, 1986). Implementation of this approach will first require identification of candidate genes or anonymous gene markers associated with the traits of interest. Candidate genes are those with a known relationship between physiological or biochemical processes and an economically important trait. In dairy cattle, genes associated with mammary gland growth, development and function are excellent candidate genes for milk production traits.The polyamines are low molecular mass polycations that influence cell proliferation and growth (Tabor & Tabor, 1984; Pegg, 1986). Ornithine decarboxylase (ODC, EC 4.1.1.17) catalyses the conversion of ornithine to putrescine, the rate-limiting step in polyamine biosynthesis (Pegg, 1986). The level of ODC is induced in quiescent cells exposed to a wide variety of stimuli such as growth hormone, corticosteroids, testosterone and growth factors (Tabor & Tabor, 1984). There is ample evidence that growth factors influence morphogenesis and differentiation of the mammary gland (Imagawa et al. 1994). Trophic hormones that are associated with lactation, such as prolactin and growth hormone, are also required to induce differentiation of bovine mammary epithelial cells (Huynh et al. 1991; Flint & Gardner, 1994), and both mitogenic and lactogenic effects of prolactin, insulin and hydrocortisone appear to be mediated through the polyamine pathway (Rillema et al. 1977; Bedford & Zadworny, 1990; Golden & Rillema, 1993). Strange et al. (1992) have shown that ODC is involved in synthesis of a milk component; ODC has elevated expression in the lactating mammary gland, which declines sharply after weaning. It is therefore possible that particular variants of ODC could be associated with increased mammary gland function and thus influence milk related traits.The objectives of the present study were to estimate allelic frequencies of ODC polymorphisms in Holstein bulls and to evaluate further the genotypic effects of ODC variants on milk production traits.

Role of ornithine decarboxylase in proliferation of prolactin-dependent lymphoma cells

1986 ◽  
Vol 64 (5) ◽  
pp. 381-386 ◽  
Author(s):  
Harry P. Elsholtz ◽  
Robert P. C. Shiu ◽  
Henry G. Friesen
Keyword(s):  
Growth Hormone ◽  
Cell Growth ◽  
Ornithine Decarboxylase ◽  
Human Growth Hormone ◽  
Normal Cell ◽  
Human Growth ◽  
Lymphoma Cells ◽  
Polyamine Biosynthesis ◽  
Nb2 Cells ◽  
Early Increase

Mitogenic stimulation of Nb2 lymphoma cells by lactogenic hormones (prolactin, human growth hormone) caused a dramatic early increase in ornithine decarboxylase (ODC) activity that achieved a maximal level by 6–8 h. A marked increase in ODC activity was also generated when cells which had reached a growth plateau were transferred to fresh medium that did not stimulate growth. Furthermore, low concentrations of human growth hormone (20 pg/mL) elicited a proliferative response, but did not cause a detectable early increase in ODC activity. The early peak of ODC activity thus appeared not to be directly involved in mediating lactogen-stimulated growth nor was it required to support the mitogenic response. However, prolonged suppression of ODC activity by DL-α-difluoromethylornithine (DFMO) (200 μM) attenuated the growth of Nb2 cells (50–60% inhibition), indicating that normal cell growth was dependent on ODC and polyamine biosynthesis. Under these conditions, putrescine, the enzyme product, or the polyamines spermidine and spermine restored normal cell growth when added at a concentration of 1 μM or greater. Nb2-SP cells, variants which proliferate in the absence of prolactin, were about two times more resistant to the growth suppressive effects of DFMO than prolactin-responsive Nb2 cells.

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