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Little is known of the changes occurring in the liver during pregnancy and lactation. The ratios of liver weight and liver protein to body weight are increased in pregnant rats [Bokelmann & Scheringer, 1932], and more of the maternal protein is apportioned to the liver in pregnant rats than in non-pregnant controls [Poo, Lew & Addis, 1939; Poo, Lew, Lee & Addis, 1940]. The total nucleic acid content is considerably raised, both deoxyribonucleic and ribonucleic acids taking part [Davidson & Waymouth, 1944]. There is an increase of the ascorbic acid content of the livers of mice and rats during pregnancy [Kennaway & Kennaway, 1944; Kennaway & Tipler, 1947]. The arginase content of the liver of rats is normal during pregnancy but increased during lactation [Folley & Greenbaum, 1947].
Since during pregnancy and lactation the maternal organism has to provide the material for a very rapid protein synthesis, considerable changes in
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SUMMARY
Rat liver when treated with bovine growth hormone produced a humoral factor ('sulphation factor') which stimulated cartilage growth directly; the results indicate that this humoral factor differs from growth hormone.
Perfusion of rat liver and incubation of rat liver slices with bovine growth hormone stimulated the production of 'sulphation factor' as measured by the uptake of 35S into rat cartilage. The liver required a long exposure to the hormone before the 'sulphation factor' was produced and was still capable of 'sulphation factor' production after growth hormone treatment had ceased.
The age and condition of the animal influenced the time necessary for growth hormone to act on the liver and the persistence of its effects. Disruption of liver slices by freezing and thawing, and by homogenization, destroyed their ability to produce 'sulphation factor' on addition of growth hormone.
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adipose tissue ( Grala et al . 2010 ). Studies on rodents and humans suggest that the lipolytic effect of acyl ghrelin may occur in muscle tissue ( Barazzoni et al . 2005 , Vestergaard et al . 2011 ). In different adipose tissues and in the liver, acyl
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al . 1998 ). Further, there is evidence that ZAG directly promotes lipid utilisation, possibly by the upregulation of mitochondrial uncoupling proteins ( Bing et al . 2002 ). ZAG has been identified in various organs, including the liver, breast
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1995 , Reinecke & Collet 1998 ). IGF-I is mainly produced in liver – the principal source of circulating (endocrine) IGF-I – under the influence of growth hormone (GH). IGF-I released from the liver into the circulation acts on a variety of target
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SUMMARY
A single intraperitoneal injection of 2 μg. d-aldosterone monoacetate/g. body weight produced a rapid, but temporary, uncoupling of oxidative phosphorylation in mouse liver mitochondria. This resulted in low P:O ratios in male and female animals of 1·21 and 1·52, respectively. The P:O ratio of females remained somewhat lower than the control levels but there was a progressive improvement in oxidative phosphorylation during the first 24 hr. after the injection leading to P: O ratios similar to those in the controls. Experiments in vitro showed that the uncoupling effects of aldosterone were related to its concentration in the reaction medium. Aldosterone added to fresh rat liver mitochondria, at concentrations of 10−10, 10−7 and 10−4m inhibited phosphorylation by 9·5, 77·1 and 95·1% and lowered P:O ratios to 2·46, 1·66 and 0·41, respectively. These changes in oxidative phosphorylation were not related to alteration in ATPase activity and were independent of mitochondrial electrolyte concentration.
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Abstract
Cirrhosis of the liver, a condition characterised by hepatocyte regeneration, is also associated with elevated insulin levels and insulin resistance. In animal models hepatic regeneration is associated with increased IGFBP-1 gene expression. Insulin is known to be an inhibitor of IGFBP-1 gene expression and circulating insulin levels in man demonstrate a negative correlation with IGFBP-1 levels. To further our understanding of the regulation of IGFBP-1 in cirrhosis we have studied steady state levels of IGFBP-1 mRNA in human liver from three groups of patients: Group 1, tissue obtained at the time of harvesting donor liver for orthotopic liver transplantation (n=4); group 2, patients undergoing major liver resection with no histological evidence of chronic liver disease (n=4); and group 3, patients undergoing orthotopic transplantation for chronic liver failure (n=9). Simultaneous samples of serum were taken at the time of surgery in some patients and in these patients IGFBP-1 mRNA levels were related to circulating levels of IGFBP-1 and insulin.
IGFBP-1 mRNA was detectable in all the human liver samples with the greatest levels seen from the normal livers of group 2 patients. Insulin levels were elevated in the cirrhotic group 3 patients compared to a normal range as were IGFBP-1 levels. There was no relationship between circulating levels of IGFBP-1 and IGFBP-1 gene expression.
In conclusion, IGFBP-1 mRNA is present in human adult liver at the time of surgery and also in cirrhotic liver despite high levels of insulin suggesting that there are factors other than insulin regulating IGFBP-1 gene expression.
Journal of Endocrinology (1994) 141, 377–382
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SUMMARY
The binding characteristics of corticosterone by rat liver were studied by a displaceable binding technique. The binding of corticosterone to protein fractionated by gel filtration and density gradient centrifugation has been carried out as a preliminary determination of the nature of the binding sites. The results were analysed and showed three types of binding sites for corticosterone with the characteristic association constants at 0° of K 1 = 1·2 × 1010, K 2 = 1 × 108 and K 3 = 1 × 104 1./mole. Percentage displacement of corticosterone from the nuclear fraction did not differ significantly from that from tissue or the mitochondrial-microsomal fraction. The K 1 and K 2 sites persisted in separated buffer-soluble fractions but were destroyed on mild heating leaving only the K 3 sites.
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ABSTRACT
We have compared circulating and hepatic somatomedin (SM) activity in rats with diabetes or malnutrition of varying severity. Somatomedin activity was measured by the hypophysectomized rat costal cartilage bioassay. In both moderate diabetes and moderate malnutrition, mean serum SM activity was not significantly lower than normal (79 ± 13% (s.e.m.) and 95 ± 11% vs normal controls respectively). In contrast, liver perfusate SM activity was significantly reduced in both groups (51 ± 12% for moderate diabetes and 44 ± 12% for moderate malnutrition). Liver extract SM activity was also significantly decreased in both moderate diabetes and malnutrition (74 ± 4% and 75 ± 6% vs normal controls respectively). In severe diabetes and malnutrition, both liver and serum activities were low, consistent with previous reports. Our studies showed that liver SM activity fell in response to metabolic stress before a decrease in circulating levels occurred, supporting the concept that the liver regulates serum SM activity and growth in diabetes and malnutrition.
J. Endocr. (1984) 101, 257–261
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The mode of uptake of l-[125I]thyroxine by freshly isolated rat liver parenchymal cells was studied by a rapid centrifugation technique. Using conditions for measuring initial rates of uptake, uptake by liver cells was not saturable when exposed to hormone concentrations in the incubation medium ranging from 2 pmol/l to 10 μmol/l. The Arrhenius plot was linear from 2 to 37°C; the temperature coefficient was 1·4. The uptake of l-[125I]thyroxine by liver cells was 35% when compared with that of l-[125I]tri-iodothyronine. In the presence of 2·8% bovine serum albumin the rate of uptake of l-[125I]thyroxine by liver cells was reduced by 90%. These results suggest that l-[125I]thyroxine enters the rat liver parenchymal cell by simple diffusion and only the free hormone crosses the plasma membrane.
