Studies of Insulin, Growth Hormone and Prolactin Binding: Tissue Distribution, Species Variation and Characterization

Posner, Barry I.; Kelly, Paul A.; Shiu, Robert P. C.; Friesen, Henry G.

doi:10.1210/endo-95-2-521

Cited by 596 publications

(195 citation statements)

References 11 publications

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“…As shown in an earlier study [2] , hGH, oPRL and to a lesser extent bGH inhibit the binding of [ 1251] bGH to liver membranes of female rats; the trations required for 50% inhibition are 2 X lo-' M for hGH, 3 X 1 O-' M for oPRL and 2.5 X 1 O-' M for bGH (tig.lA). It is of interest that, differing with earlier studies [2,4], the apparent affinity of oPRL for the hGH binding sites is slightly but consistently lower than the one of hGH; maximal inhibition achieved by oPRL is always inferior to the one obtained with hGH ( fig.lA). This difference which does not occur when [1251] oPRL is used as a ligand ( fig.2) suggests that, besides binding to the 'lactogenic' sites, hGH interacts with additional, 'growth hormone' binding sites.…”

Section: Resultsmentioning

confidence: 56%

Binding of human growth hormone to rat liver membranes: Lactogenic and somatotropic sites

Postel-Vinay¹

1976

FEBS Letters

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Section: Resultsmentioning

confidence: 56%

Binding of human growth hormone to rat liver membranes: Lactogenic and somatotropic sites

Postel-Vinay¹

1976

FEBS Letters

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“…present on nearly all cells (19), and the concentrations of receptors are about the same on nontarget cells as on classical targets such as liver, muscle, and fat cells. Theoretical predictions and experimental results indicate that receptor concentrations in vivo are sufficiently high (relative to receptor affinity and hormone concentrations) that the concentration of hormone bound to cells may be equal to or possibly 2 or 3 times the hormone concentration in plasma (20).…”

Section: Methodsmentioning

confidence: 99%

Insulin is ubiquitous in extrapancreatic tissues of rats and humans.

Rosenzweig¹,

Havránková²,

Brownstein³

et al. 1980

Proc. Natl. Acad. Sci. U.S.A.

118

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Insulin has been detected, at levels higher than those in plasma, in a broad range of extrapancreatic tissues in both rats and humans. Rat liver insulin was shown to be indistinguishable from genuine insulin by radioimmunoassay, Sephadex chromatography, bioassay, and antibody neutralization. Liver insulin (like brain insulin) was unchanged in ob/ob mice, in rats treated with streptozotocin, or in fasted rats, despite marked alterations in pancreatic secretion of insulin and in liver content of insulin receptors. Insulin was found in cultured human IM-9 lymphocytes and cultured fibroblasts at concentrations greater than 100 times the levels in the media. IM-9 lymphocyte insulin also was shown to be indistinguishable from genuine insulin, by the same criteria used for liver insulin. The insulin concentration in cultured human cells was unaffected by depletion of insulin from the culture medium or by addition of beef insulin to the medium. The data suggest that a part, if not all, of the extrapancreatic tissue insulin is independent of plasma insulin and may be synthesized by the tissues themselves.Recently, we demonstrated the presence of insulint in the brain in concentrations higher than in plasma (1). This brain insulin was indistinguishable from genuine insulin by multiple criteria, and its tissue concentration did not vary at all with extreme changes in plasma insulin (2). In the present study we show that insulin immunoreactivity is present in essentially all tissues of humans and rats as well as in cultured lymphocytes and fibroblasts at concentrations that are 2-100 times those present in the plasma or culture medium. The material is similar to (or identical with) genuine insulin by radioimmunoassay, gel filtration, bioassay, and antibody neutralization. The concentration of cellular insulin in vio changes little or not at all in response to extremes of hyperinsulinemia and hypoinsulinemia. MATERIALS AND METHODSTissue Preparations. Male Sprague-Dawley rats (250-300 g) fed ad lib were decapitated between 1400 and 1600 hr; "fasted rats" had been denied food for 50-72 hr before they were killed. Rats injected with streptozotocin (65 mg/kg intravenously) and control rats (injected with isotonic saline) were sacrificed 1 month after treatment. Obese (ob/ob) mice and their thin littermates (mixtures of ob/+ and +/+) of the C57BL65 strain were killed at 8-10 weeks of age. Organs and plasma were collected and stored as reported (1, 2).Human tissue samples, obtained either during operations or at autopsy within 3 hr after death, were frozen on dry ice prior to extraction. Whole blood (500 ml) from a fasting (overnight) normal human volunteer was separated into mononuclear and granulocytic fractions by a modification (3) of the method of The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U. S. C. §1734 solely to indicate this fact. 572Boyum (4). The cells were washed in phosphate-buffered salin...

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“…In the adult muscle, the signal was marked and homogenous not around the nuclei, but equally distributed throughout the muscle fibres. In the adult muscle, the GHR mRNA labeling was unexpected compared with the low specific GH binding observed in microsomial muscle preparations from other species [34,38].…”

Section: Discussionmentioning

confidence: 91%

Growth hormone receptor gene expression in the skeletal muscle of normal and double-muscled bovines during foetal development

Listrat

Hocquette²,

Picard³

et al. 2005

Reprod. Nutr. Dev.

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-The expression of the growth hormone receptor (GHR) gene was investigated in semitendinosus muscle during bovine foetal development in both normal and double-muscled Charolais foetuses which differ with respect to muscle development. Northern-blot analysis of foetal muscle RNA preparations with a GHR cDNA probe identified the 4.5 kb GHR mRNA as early as 130 days post-conception. In double-muscled animals, the expression of GHR mRNA increased from 130 to 210 days of gestation while it stayed stable in normal ones. It was significantly higher (P < 0.05) in double-muscled foetuses compared to normal ones from the second third of gestation. Northern-blot analysis of foetal muscle RNA preparations from both genotypes with a β-actin cDNA probe, revealed lower β-actin gene expression in double-muscled foetuses than in normal ones, suggesting a delay in the differentiation of muscle cells. In situ hybridisation revealed the localisation of specific GHR mRNA in muscle cells at all gestation stages analysed (130, 170, 210 days postconception) but not in connective tissue surrounding the muscle cells. At the adult stage, the hybridisation signal was also very high and observed in muscle cells only. These results show the ontogeny of GHR mRNA in bovine muscle and demonstrate a difference between normal and doublemuscled animals. muscle / bovine / receptor / growth hormone / in situ hybridisation

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Studies of Insulin, Growth Hormone and Prolactin Binding: Tissue Distribution, Species Variation and Characterization

Abstract: The specific binding of 125

Cited by 596 publications

References 11 publications

Binding of human growth hormone to rat liver membranes: Lactogenic and somatotropic sites

Binding of human growth hormone to rat liver membranes: Lactogenic and somatotropic sites

Insulin is ubiquitous in extrapancreatic tissues of rats and humans.

Growth hormone receptor gene expression in the skeletal muscle of normal and double-muscled bovines during foetal development

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