scholarly journals Ligand-induced translocation of insulin receptors in intact rat liver.

1982 ◽  
Vol 257 (18) ◽  
pp. 10852-10860 ◽  
Author(s):  
B Desbuquois ◽  
S Lopez ◽  
H Burlet
Keyword(s):  
Rat Liver ◽  
Insulin Receptors

scholarly journals Characterization of solubilized insulin receptors from rat liver microsomes. Existence of two receptor species with different binding properties

1986 ◽  
Vol 154 (2) ◽  
pp. 281-287 ◽  
Author(s):  
Rudiger KOCH ◽  
Arno DEGER ◽  
Hans-Martin JACK ◽  
Karl-Norbert KLOTZ ◽  
Dieter SCHENZLE ◽  
...  
Keyword(s):  
Rat Liver ◽  
Liver Microsomes ◽  
Insulin Receptors ◽  
Rat Liver Microsomes ◽  
Binding Properties

Insulin Binding Sites Induced in the Tetrahymena by Rat Liver Receptor Antibody

1984 ◽  
Vol 39 (1-2) ◽  
pp. 183-185 ◽  
Author(s):  
G. Csaba ◽  
P. Kovács ◽  
Ágnes Inczefi-Gonda
Keyword(s):  
Rat Liver ◽  
Concanavalin A ◽  
Binding Sites ◽  
Binding Capacity ◽  
Insulin Receptors ◽  
Insulin Binding ◽  
Receptor Antibody ◽  
Receptor Antibodies

Abstract Tetrahvmena cells treated with purified rabbit anti­ bodies to rat hepatocellular membrane exhibited a consider­ able increase in binding capacity on reexposure to the antibody 24 h later. Insulin binding was similarly enhanced by preexposure to the antibody, and vice versa, preex­ posure to insulin enhanced the later binding of rat liver receptor antibodies. This suggests that (1) the Tetrahymena and the rat possess similar insulin receptors, and (2) the receptor antibody is also able to induce imprinting for itself as well as for insulin. Concanavalin-A, noted for binding overlap with insulin, failed to induce imprinting either for insulin or for antibodies to receptors, whereas the latter did induce imprinting for Concanavalin-A.

Expression of insulin-like growth factor II (IGF-II) and IGF-II, IGF-I and insulin receptors mRNAs in isolated non-parenchymal rat liver cells

1992 ◽  
Vol 14 (1) ◽  
pp. 30-34 ◽  
Author(s):  
Frédérique Zindy ◽  
Eugenia Lamas ◽  
Sylvie Schmidt ◽  
André Kirn ◽  
Christian Brechot
Keyword(s):  
Growth Factor ◽  
Rat Liver ◽  
Insulin Receptors ◽  
Liver Cells ◽  
Insulin Like Growth Factor ◽  
Factor Ii ◽  
Igf I ◽  
Rat Liver Cells

Purification and properties of insulin receptors from rat liver membranes

1977 ◽  
Vol 77 (3) ◽  
pp. 981-988 ◽  
Author(s):  
Steven Jacobs ◽  
Yoram Shechter ◽  
Karen Bissell ◽  
Pedro Cuatrecasas
Keyword(s):  
Rat Liver ◽  
Insulin Receptors ◽  
Purification And Properties ◽  
Liver Membranes

scholarly journals Tyrosine phosphorylation of two cytosolic proteins of 50 kDa and 35 kDa in rat liver by insulin-receptor kinase in vitro

1987 ◽  
Vol 248 (1) ◽  
pp. 27-33 ◽  
Author(s):  
Y C Kwok ◽  
C C Yip
Keyword(s):  
Insulin Receptor ◽  
Rat Liver ◽  
Growth Factor Receptor ◽  
Insulin Receptors ◽  
Artificial Substrates ◽  
Receptor Kinase ◽  
Insulin Receptor Tyrosine Kinase ◽  
Cytosolic Proteins ◽  
Insulin Receptor Kinase

Insulin-receptor tyrosine kinase can phosphorylate a variety of artificial substrates in vitro. Its physiological substrate(s), however, remains unknown. In the present study, we show that immobilized insulin receptors phosphorylate tyrosine residues of two cytosolic proteins of 50 kDa and 35 kDa in rat liver. Phosphorylation of these two proteins required Mn2+- or Mg2+-ATP as the phosphate donor. Phosphorylation was time- and temperature-dependent. Furthermore, the rate of phosphorylation of the two proteins was related to the autophosphorylated state of the insulin receptor. The pI of the phosphorylated 50 kDa and 35 kDa proteins was 5.4 and 5.6 respectively. These proteins were present in low abundance. They were not related to each other, nor to the insulin receptor, as demonstrated by in-gel proteolytic digestion and by immunoprecipitation using antibodies produced against them. They were specific substrates for the insulin receptor kinase, since they were not phosphorylated by epidermal-growth-factor-receptor kinase. These observations suggest that the 50 kDa and 35 kDa cytosolic proteins may be endogenous substrates for the insulin-receptor kinase.

scholarly journals Analysis of insulin receptor phosphorylation sites in intact rat liver cells by two-dimensional phosphopeptide mapping. Predominance of the tris-phosphorylated form of the kinase domain after stimulation by insulin

1991 ◽  
Vol 275 (1) ◽  
pp. 15-21 ◽  
Author(s):  
T Issad ◽  
J M Tavaré ◽  
R M Denton
Keyword(s):  
Insulin Receptor ◽  
Rat Liver ◽  
Insulin Receptors ◽  
Kinase Domain ◽  
Two Dimensional ◽  
Tyrosine Residues ◽  
C Terminus ◽  
Rat Liver Cells ◽  
Wheat Germ Lectin ◽  
Dimensional Mapping

1. Insulin receptors were partially purified from rat liver by chromatography on wheat-germ-lectin-Sepharose. Incubation with [gamma-32P]ATP in the presence of insulin resulted in increased phosphorylation of the beta-subunit on both tyrosine and serine residues. Two-dimensional mapping of tryptic peptides showed that, in agreement with previous studies using preparations of receptors from other sources, the tyrosine residues involved were the three tyrosines in the kinase domain (corresponding to tyrosines 1158, 1162 and 1163 of the human receptor) plus two tyrosines close to the C-terminus (corresponding to tyrosines 1328 and 1334). 2. The effects of insulin on the phosphorylation of receptors within intact rat liver cells were determined by incubating cells in the presence of [32P]Pi for 50 min and then with or without insulin for a further 10 min. The labelled receptors were then rapidly isolated by sequential use of wheat-germ-lectin-Sepharose chromatography and immuno-isolation using a monoclonal antibody to the C-terminal end of the beta-subunit. 3. Insulin was found to increase overall phosphorylation of the receptor nearly 3-fold. Two-dimensional mapping was then carried out in combination with phosphoamino acid analysis. This revealed that the pattern of phosphorylation of the receptors in cells incubated in the absence and presence of insulin exhibited a number of marked differences from that observed in previous studies on intact cells, which had been restricted to cells expressing very high levels of insulin receptors such as certain hepatoma-derived cells or cells transfected with insulin receptor cDNA. The differences in the effects of insulin included a larger increase in the proportion of receptors being phosphorylated on the three tyrosine residues of the kinase domain, no apparent phosphorylation of the two tyrosine residues close to the C-terminus and no increase in either threonine or overall serine phosphorylation. 4. The receptors appeared to be phosphorylated on a number of different serine residues in cells incubated in the absence of insulin. Evidence for both increases and decreases in the phosphorylation of specific serine residues on addition of insulin was obtained. 5. It is concluded that care should be taken when extrapolating findings on the phosphorylation of the insulin receptor within cultured cells to more physiological situations.

scholarly journals Disulfide bonds within the α-subunit of insulin receptors in rat liver and brain membranes

FEBS Letters ◽  
1987 ◽  
Vol 214 (1) ◽  
pp. 107-110
Author(s):  
Munehiko Nagao ◽  
Choitsu Sakamoto ◽  
Takashi Matozaki ◽  
Shigeaki Baba
Keyword(s):  
Rat Liver ◽  
Disulfide Bonds ◽  
Insulin Receptors ◽  
Α Subunit ◽  
Brain Membranes

Antiserum to liver insulin receptor hyperpolarizes rat muscle

1983 ◽  
Vol 244 (1) ◽  
pp. C58-C60 ◽  
Author(s):  
K. Zierler ◽  
E. M. Rogus
Keyword(s):  
Skeletal Muscle ◽  
Insulin Receptor ◽  
Rat Liver ◽  
Rabbit Antiserum ◽  
Insulin Receptors ◽  
Metabolic Effects ◽  
Metabolic Responses ◽  
Maximum Effect ◽  
Half Maximum ◽  
Rat Muscle

Antibodies to insulin receptors have been reported to have some insulinlike metabolic effects. If insulin-induced electrical hyperpolarization of skeletal muscle is part of the transduction chain between receptor and certain metabolic responses, then receptor antiserum should hyperpolarize. The Jacobs antiserum (rabbit antiserum against rat liver insulin receptor) hyperpolarized rat caudofemoralis muscle. Maximum effect, about 4.5 mV, occurred at 1:10,000 dilution, half maximum at about 1:40,000. Maximum effect of antiserum was only as great as half maximum hyperpolarization by insulin on this muscle. 2-Deoxyglucose uptake was also stimulated by antiserum but required greater concentration than for hyperpolarization, and the stimulation was only by about one-third the maximum effect of insulin.

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