Specific Binding of Iodinated Growth Hormone to Rat Liver in Vivo*

Endocrinology ◽  
1978 ◽  
Vol 103 (4) ◽  
pp. 1190-1195 ◽  
Author(s):  
DANIEL TURYN ◽  
JUAN M. DELLACHA
1978 ◽  
Vol 12 (11) ◽  
pp. 1087
Author(s):  
M C POSTEL-VINAY ◽  
C KAYSER ◽  
B DESBUQUOIS

1985 ◽  
Vol 231 (2) ◽  
pp. 343-347 ◽  
Author(s):  
V A Zammit ◽  
C G Corstorphine

Specific binding of [2-14C] malonyl-CoA to rat liver mitochondria was measured at different temperatures and after various periods of time of exposure of the mitochondria to the ligand. Incubation of mitochondria at 37 degrees C in the absence of malonyl-CoA resulted in a decrease in their ability to bind malonyl-CoA at all concentrations tested (up to 55 microM). However, incubation of mitochondria in the presence of malonyl-CoA resulted in the loss of the binding only by a low-affinity component. By contrast, there was an increase in the binding that occurred at low, physiological, concentrations of malonyl-CoA. These differences in the response of the two binding components to incubation conditions were used to obtain quantitative data about their respective saturation kinetics. Evidence was obtained that, whereas the high-affinity component approached saturation hyperbolically with respect to malonyl-CoA concentration, the low-affinity component had sigmoidal characteristics. The concentrations of malonyl-CoA required to half-saturate the two components were 2-3 microM and 30 microM for the high- and low-affinity components respectively. Evidence was also obtained for the involvement of a temperature-dependent transition, that occurred at around 25 degrees C, in the modulation of malonyl-CoA binding to the mitochondria. The possible physiological roles of the two components of malonyl-CoA binding in relation to the regulation of overt carnitine palmitoyltransferase (CPT I) activity in vivo are discussed.


Development ◽  
1987 ◽  
Vol 100 (1) ◽  
pp. 13-22
Author(s):  
L. Dini ◽  
L. Conti-Devirgiliis ◽  
S. Russo-Caia

The number and distribution of galactose-specific binding sites were investigated in rat liver cells during perinatal development. Ligand binding to hepatocytes, macrophages and endothelial cells was followed with in vitro and in situ experiments by electron microscopy, using lactosylated bovine serum albumin adsorbed onto 5 nm colloidal gold particles as ligand. Binding capacity, starting at a late stage of fetal development, is very low both on the hepatocyte and on the macrophage surface, which show single particles statistically distributed. By contrast, bound particles are absent from fetal endothelial cells, which also lack the typical coated regions. In vivo, experiments at 37 degrees C show that endocytosis occurs to some extent in prenatal life. These results indicate that the expression of galactose-specific receptors' activity on the different liver cell types follows different developmental patterns, which are independently modulated.


Endocrinology ◽  
1982 ◽  
Vol 111 (1) ◽  
pp. 244-251 ◽  
Author(s):  
MARIE-CATHERINE POSTEL-VINAY ◽  
CHRISTINE KAYSER ◽  
BERNARD DESBUQUOIS

1988 ◽  
Vol 117 (4_Suppl) ◽  
pp. S138-S139
Author(s):  
U. Loos ◽  
J. STEINBORN ◽  
E. STEINBORN ◽  
F. S. KECK

1984 ◽  
Vol 224 (2) ◽  
pp. 535-540 ◽  
Author(s):  
L P Roguin ◽  
J M Delfino ◽  
N Vita ◽  
A C Paladini

Bovine somatotropin with an increasing number of its carboxylate groups modified by reaction with glycine methyl ester in the presence of a water-soluble carbodi-imide was tested for its activity in different bioassays. Only those derivatives which were known to be active in the body-weight-increase bioassay were able to compete with 125I-labelled bovine somatotropin for their specific binding sites in vivo. No difference was found in the rate of clearance of a poorly active derivative as compared with that of native somatotropin. In contrast, both active and inactive derivatives were found to be equally effective in displacing the tracer from its binding sites present in isolated cells and membrane preparations from rat liver. These results suggest that the liver somatogenic receptors studied in vitro are less discriminating than those detected in vivo.


2016 ◽  
Vol 65 (4) ◽  
pp. 447-454
Author(s):  
Motoyo Maruyama ◽  
Masahiko Fujisawa ◽  
Makoto Yokosuka ◽  
Toru R. Saito ◽  
Shin-ichi Hayama ◽  
...  

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