The specificity of binding of somatotropin (growth hormone) and prolactin to purified plasma membranes from rabbit liver

1984 ◽  
Vol 12 (2) ◽  
pp. 250-251
Author(s):  
CATHRYN F. LEAROYD ◽  
HILARY F. CADMAN ◽  
MICHAEL WALLIS
Keyword(s):  
Growth Hormone ◽  
Plasma Membranes ◽  
Rabbit Liver ◽  
Specificity Of Binding

scholarly journals The specificity of binding of growth hormone and prolactin to purified plasma membranes from pregnant-rabbit liver

1986 ◽  
Vol 236 (3) ◽  
pp. 657-663 ◽  
Author(s):  
C F Webb ◽  
H F Cadman ◽  
M Wallis
Keyword(s):  
Growth Hormone ◽  
Plasma Membranes ◽  
Human Growth ◽  
Rabbit Liver ◽  
Complex Nature ◽  
Binding Properties ◽  
Microsomal Preparation ◽  
Pregnant Rabbit ◽  
Specificity Of Binding ◽  
Triton X

The binding of 125I-labelled human growth hormone (hGH) to a purified plasma membrane preparation from the liver of pregnant rabbit, and to receptors solubilized from this fraction with Triton X-100, was dependent on time, temperature, the cations used and the receptor concentration. Solubilization did not affect the binding properties of the receptors at low concentrations of Triton X-100. Some somatogenic hormones, such as bovine GH, and some lactogenic hormones, such as ovine prolactin, displaced 125I-labelled hGH from purified plasma membranes and solubilized receptor preparations, but GHs and prolactins from various other species were rather ineffective. The results indicate that although there are binding sites for hGH in these pregnant rabbit liver membranes, few of these are specifically somatogenic or lactogenic. The binding properties of the purified plasma membranes are similar to those of a microsomal preparation studied previously, suggesting that the complex nature of the binding of hGH is not due to the heterogeneity of cellular membranes used to study binding, but is a property of the receptors associated with plasma membranes.

Growth Hormone and Prolactin Binding to Rabbit Liver Plasma Membranes

1981 ◽  
Vol 13 (09) ◽  
pp. 510-515 ◽  
Author(s):  
J. Fix ◽  
Paula Leppert ◽  
W. Moore
Keyword(s):  
Growth Hormone ◽  
Plasma Membranes ◽  
Rabbit Liver ◽  
Liver Plasma Membranes

Growth hormone receptors in hypothalamic and extra-hypothalamic tissues

1990 ◽  
Vol 5 (3) ◽  
pp. 231-238 ◽  
Author(s):  
R. A. Fraser ◽  
D. Attardo ◽  
S. Harvey
Keyword(s):  
Growth Hormone ◽  
Binding Sites ◽  
Plasma Membranes ◽  
Hormone Receptors ◽  
Cdna Probe ◽  
Rabbit Liver ◽  
Rabbit Brain ◽  
High Affinity ◽  
Age Related ◽  
Gh Receptors

ABSTRACT Central GH receptors (GHR) have been identified in hypothalamic and extra-hypothalamic tissues of rabbit and chicken brains. Plasma membranes of the rabbit brain demonstrated specific saturable high-affinity, low-capacity binding sites for 125I-labelled GH. RNA extracted from hypothalamic and extra-hypothalamic tissues of rabbit and chicken brains contained mRNA that hybridized with a cDNA probe for the rabbit liver GHR. This transcript was of a similar size to the major GHR mRNA moiety in rabbit liver. The expression of these moieties was age related, and higher in adult than in neonatal animals.

Phenobarbital Induction of Cytochrome P-450 and UDPGlucuronosyltransferase in Rabbit Liver Plasma Membranes

Enzyme ◽  
1982 ◽  
Vol 28 (1) ◽  
pp. 41-47 ◽  
Author(s):  
Jacques Magdalou ◽  
Bénédicte Antoine ◽  
Damrong Ratanasavanh ◽  
Gérard Siest
Keyword(s):  
Plasma Membranes ◽  
Rabbit Liver ◽  
Liver Plasma Membranes ◽  
Cytochrome P 450 ◽  
Phenobarbital Induction

scholarly journals Identification of a rabbit liver cytosolic binding protein for human growth hormone

1984 ◽  
Vol 221 (3) ◽  
pp. 617-622 ◽  
Author(s):  
S I Ymer ◽  
J L Stevenson ◽  
A C Herington
Keyword(s):  
Growth Hormone ◽  
Binding Affinity ◽  
Binding Protein ◽  
Physiological Role ◽  
Rabbit Liver ◽  
Precipitation Method ◽  
Affinity Column ◽  
Separation Procedure ◽  
Binding Characteristics ◽  
Membrane Bound

A specific growth hormone (GH) binding protein of Mr approx. 100000 has been demonstrated in the cytosolic fraction (200000g supernatant) of pregnant-rabbit liver by gel filtration techniques. This binding species was detectable by a standard charcoal separation procedure but not by the widely used poly(ethylene glycol) precipitation method. The GH binding protein had similar binding characteristics to those of classical membrane-bound GH receptors. The kinetics of association and dissociation, binding affinity (2.56×10(9)1/mol) and hormonal specificity have been established. There appears to be equal or greater amounts of GH binding protein in the cytosol than in the membrane fraction. The presence of the GH binding protein in rabbit liver cytosol was substantiated by its selective purification on a GH-Affigel 15 affinity column. This technique has resulted in a 200-300-fold purification with no substantial change in binding affinity. The ability of a concanavalin A-Sepharose affinity column to also bind the cytosolic binding protein indicates that, like the membrane-bound GH receptor, it is a glycoprotein. This is the first report of a cytosolic binding protein for GH and raises important questions regarding its potential physiological role in the mechanism of action of GH.

scholarly journals Effects of phenobarbital and rose bengal on the ATPases of plasma membranes of rat and rabbit liver

Gut ◽  
1972 ◽  
Vol 13 (11) ◽  
pp. 920-925 ◽  
Author(s):  
Y. Laperche ◽  
A. Launay ◽  
P. Oudea
Keyword(s):  
Rose Bengal ◽  
Plasma Membranes ◽  
Rabbit Liver

Growth hormone regulates cytosolic free calcium in rat fat cells by maintaining L-type calcium channels

1996 ◽  
Vol 270 (5) ◽  
pp. C1478-C1484 ◽  
Author(s):  
S. Gaur ◽  
H. Yamaguchi ◽  
H. M. Goodman
Keyword(s):  
Growth Hormone ◽  
Steady State ◽  
Plasma Membranes ◽  
Free Calcium ◽  
Fat Cells ◽  
Cytosolic Free Calcium ◽  
Fura 2 ◽  
Rat Adipocytes ◽  
Rat Fat Cells ◽  
Ca2 Channels

In freshly isolated individual rat adipocytes, cytosolic free Ca2+ concentration ([Ca2+]i) as measured with fura 2 slowly declined during incubation but was sustained, or even somewhat increased, by brief treatment with growth hormone (GH) at the beginning of a 3-h incubation period. GH-treated adipocytes were more permeable to Ca2+ than GH-deprived cells as indicated, using Mn2- as a surrogate and monitoring influx by the rate of quenching of fura 2 fluorescence. Blockage of Ca2- channels with 100 nM nimodipine lowered [Ca2+]i in GH-treated cells to the level seen in GH-deprived cells. Increases in [Ca2+]i or the rate of Mn2+ entry were twofold greater in GH-treated than in GH-deprived cells when extracellular K+ was increased to 30 mM. Similarly, the Ca2+ channel agonist BAY K 5552 or the diacylglycerol analogue 1,2-dioctanoyl-sn-glycerol increased [Ca2+]i more in GH-treated than in GH-deprived adipocytes. Ca(2+)-ATPase activity was two times higher in plasma membranes isolated from GH-treated than from GH-deprived cells. Continued synthesis of Ca(2+)-ATPase may depend on [Ca2+]i, since the effects of GH on [Ca2+]i and Ca(2+)-ATPase were blocked by a cycloheximide or verapamil. We suggest that voltage-sensitive L-type Ca2+ channels regulate steady-state [Ca2+]i in rat adipocytes and that GH maintains the number or functional integrity of these channels.

scholarly journals Purification of the 22000- and 20000-mol.wt. forms of human somatotropin and characterization of their binding to liver and mammary binding sites

1983 ◽  
Vol 214 (3) ◽  
pp. 885-892 ◽  
Author(s):  
J Closset ◽  
J Smal ◽  
F Gomez ◽  
G Hennen
Keyword(s):  
Mammary Gland ◽  
Binding Capacity ◽  
Chemical Characterization ◽  
Rabbit Liver ◽  
Partial Agonists ◽  
Affinity Constants ◽  
Pregnant Rabbit ◽  
Maximum Binding Capacity ◽  
Specificity Of Binding

Quantitative data concerning the binding of 22000-mol.wt. human somatotropin and its 20000-mol.wt. variant are described using pregnant-rabbit liver and mammary-gland receptors. The purification and the complete chemical characterization of both human somatotropin and its 20000-mol.wt. variant is also presented. Contamination of the 20000-mol.wt.-variant preparation by 22000-mol.wt. hormone was found to be 0.5% by weight as measured in radioimmunoassay using monoclonal antibody. Labelling of human somatotropin and its 20000-mol.wt. variant using the Iodogen method is described as well as the characterization of the binding to pregnant-rabbit liver and mammary-gland receptor preparations. The maximum binding capacity of the 125I-labelled human somatotropin was between 50 and 60% to liver particulate receptor, whereas that of the 20000-mol.wt. variant was 30%. The specificity of binding of both forms to rabbit hepatic and mammary-gland receptor was found to be similar for both proteins in the same system. The affinity constants and capacity were respectively 0.7 X 10(10)M-1 and 815 fmol/mg of protein for human somatotropin and 0.6 X 10(10)M-1 and 1.250 fmol/mg of protein for the 20000-mol.wt. variant. These data suggest that both proteins behave as partial agonists to the receptors studied.

Sign in / Sign up

Export Citation Format

Share Document