Monoclonal antibody to the human insulin receptor, but not insulin, stimulates S6 kinase via human insulin receptors mutated at three major tyrosine autophosphorylation sites

1992 ◽  
Vol 48 (3) ◽  
pp. 324-335 ◽  
Author(s):  
Chin K. Sung
Keyword(s):  
Monoclonal Antibody ◽  
Insulin Receptor ◽  
Human Insulin ◽  
Insulin Receptors ◽  
S6 Kinase ◽  
Human Insulin Receptor ◽  
Tyrosine Autophosphorylation

Functional activation of mutant human insulin receptor by monoclonal antibody

The Lancet ◽  
1996 ◽  
Vol 347 (9015) ◽  
pp. 1586-1590 ◽  
Author(s):  
A Krook ◽  
M.A Soos ◽  
S O'Rahilly ◽  
A Krook ◽  
M.A Soos ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Insulin Receptor ◽  
Human Insulin ◽  
Human Insulin Receptor

Turnover of insulin receptors in cells transfected with human insulin receptor cDNA

1989 ◽  
Vol 17 (1) ◽  
pp. 197-198
Author(s):  
ROSALIND H. GANDERTON ◽  
JONATHAN WHITTAKER ◽  
KENNETH SIDDLE
Keyword(s):  
Insulin Receptor ◽  
Human Insulin ◽  
Insulin Receptors ◽  
Human Insulin Receptor ◽  
Receptor Cdna ◽  
In Cells

Human insulin receptor radioimmunoassay: applicability to insulin-resistant states

1989 ◽  
Vol 257 (3) ◽  
pp. E451-E457 ◽  
Author(s):  
V. Pezzino ◽  
V. Papa ◽  
V. Trischitta ◽  
A. Brunetti ◽  
P. A. Goodman ◽  
...  
Keyword(s):  
Insulin Receptor ◽  
Human Insulin ◽  
Insulin Receptors ◽  
Insulin Resistant ◽  
Human Insulin Receptor ◽  
Igf I ◽  
Rabbit Polyclonal Antibody ◽  
Specific Activities ◽  
Triton X ◽  
Major Target

A radioimmunoassay of the human insulin receptor was developed employing a potent rabbit polyclonal antibody to the human insulin receptor and a highly purified human placental insulin receptor preparation. The receptor, obtained by sequential affinity chromatography with insulin receptor monoclonal antibody-agarose and wheat germ agglutinin-agarose, was radiolabeled with 125I-Bolton-Hunter reagent at specific activities of 2,100-3,300 Ci/mmol. Over 75% of this ligand was immunoprecipitable with the polyclonal antireceptor antibody and remained immunoprecipitable for greater than 45 days. The assay was sensitive to unlabeled receptor concentrations as low as 0.2 ng/0.5 ml; unlabeled insulin did not cross-react and unlabeled insulin-like growth factor (IGF)-I receptor cross-reacted weakly. The radioimmunoassay was applicable to the measurement of insulin receptors in tissues and cells that were extracted by solubilization in 1% Triton X-100; no purification of the extracted receptor was necessary. Of the three major target tissues for insulin action studied, liver had the highest concentration of receptors (47.6 ng/mg protein); fat and muscle had lower levels. Other studies with the radioimmunoassay indicated that insulin receptors were decreased both in monocytes from obese hyperinsulinemic subjects and in fibroblasts from patients with leprechaunism.

scholarly journals Catalysis of serine and tyrosine autophosphorylation by the human insulin receptor.

1992 ◽  
Vol 89 (17) ◽  
pp. 7885-7889 ◽  
Author(s):  
K. Baltensperger ◽  
R. E. Lewis ◽  
C. W. Woon ◽  
P. Vissavajjhala ◽  
A. H. Ross ◽  
...  
Keyword(s):  
Insulin Receptor ◽  
Human Insulin ◽  
Human Insulin Receptor ◽  
Tyrosine Autophosphorylation
Sign in / Sign up

Export Citation Format

Share Document