Thiol-Specific Biotinylation of the Insulin Receptor in Permeabilized Cells Enhances Receptor Function

Biochemistry ◽  
1995 ◽  
Vol 34 (26) ◽  
pp. 8357-8364 ◽  
Author(s):  
Michel Bernier ◽  
Orna Nadiv ◽  
Hemanta K. Kole
Keyword(s):  
Insulin Receptor ◽  
Receptor Function ◽  
Permeabilized Cells

Effects of hyperinsulinemia and hyperglycemia on insulin receptor function and glycogen synthase activation in skeletal muscle of normal man

Metabolism ◽  
1991 ◽  
Vol 40 (8) ◽  
pp. 830-835 ◽  
Author(s):  
Jens Friss Bak ◽  
Niels Møller ◽  
Ole Schmitz ◽  
Erik A. Richter ◽  
Oluf Pedersen
Keyword(s):  
Skeletal Muscle ◽  
Insulin Receptor ◽  
Glycogen Synthase ◽  
Receptor Function ◽  
Normal Man

O-7: Drosophila insulin receptor function is required for normal growth

2009 ◽  
Vol 104 (S 02) ◽  
pp. 13-13
Author(s):  
Robert S. Garofalo ◽  
Chi Chen ◽  
Mireya Marin ◽  
Yimin Ruan ◽  
Joseph Jack
Keyword(s):  
Insulin Receptor ◽  
Normal Growth ◽  
Receptor Function ◽  
Drosophila Insulin Receptor

Decreased muscle insulin receptor kinase correlates with insulin resistance in normoglycemic Pima Indians

1997 ◽  
Vol 273 (2) ◽  
pp. E276-E283 ◽  
Author(s):  
J. F. Youngren ◽  
I. D. Goldfine ◽  
R. E. Pratley
Keyword(s):  
Insulin Resistance ◽  
Insulin Receptor ◽  
Body Fat ◽  
Insulin Action ◽  
Enzyme Linked Immunosorbent Assay ◽  
Percent Body Fat ◽  
Receptor Function ◽  
Pima Indians ◽  
Insulin Receptor Tyrosine Kinase

Defects in insulin receptor tyrosine kinase activity are present in insulin-resistant non-insulin-dependent diabetes mellitus patients and certain nondiabetic individuals, both lean and obese. However, the relationship between insulin receptor function, insulin action, and obesity is unclear. To address this issue, we have employed a new and highly sensitive enzyme-linked immunosorbent assay to measure in vitro insulin-stimulated autophosphorylation of immunocaptured muscle insulin receptors in a group of 25 normoglycemic Pima Indians. Insulin action, determined during two-step euglycemic insulin clamps, varied widely in these subjects. Maximal in vitro insulin stimulation of insulin receptor autophosphorylation strongly correlated with both low (Mlow)- and high (Mhigh)-dose insulin-stimulated glucose disposal (r = 0.62 and 0.51, P < 0.002 and 0.011, respectively). Insulin receptor autophosphorylation was inversely related to percent body fat (r = -0.52, P < 0.009). After control for percent body fat, receptor autophosphorylation remained correlated with Mlow (partial r = 0.49, P < 0.025). These data therefore suggest that defects in insulin receptor function are major contributors to insulin resistance in both lean and obese normoglycemic Pima Indians.

Effects of high-fat diet on insulin receptor function in rat hippocampus and the level of neuronal corticosterone

Life Sciences ◽  
2011 ◽  
Vol 88 (13-14) ◽  
pp. 619-627 ◽  
Author(s):  
Wasana Pratchayasakul ◽  
Sasiwan Kerdphoo ◽  
Petnoi Petsophonsakul ◽  
Anchalee Pongchaidecha ◽  
Nipon Chattipakorn ◽  
...  
Keyword(s):  
Insulin Receptor ◽  
High Fat Diet ◽  
Rat Hippocampus ◽  
Receptor Function ◽  
High Fat

scholarly journals Insulin receptor function is inhibited by guanosine 5′-[γ-thio]triphosphate (GTP[S])

1990 ◽  
Vol 270 (2) ◽  
pp. 401-407 ◽  
Author(s):  
H W Davis ◽  
J M McDonald
Keyword(s):  
Insulin Receptor ◽  
G Proteins ◽  
Plasma Membranes ◽  
Insulin Receptors ◽  
Insulin Binding ◽  
Peptide Sequence ◽  
Receptor Kinase ◽  
Receptor Function ◽  
Gtp Binding ◽  
Insulin Receptor Kinase

The regulatory role of GTP-binding proteins (G-proteins) in insulin receptor function was investigated using isolated insulin receptors and plasma membranes from rat adipocytes. Treatment of isolated insulin receptors with 1 mM-guanosine 5′-[gamma-thio]triphosphate (GTP[S]) inhibited insulin-stimulated phosphorylation of the beta-subunit, histone Hf2b and poly(GluNa4,Tyr1) by 22%, 65% and 65% respectively. Phosphorylation of calmodulin by the insulin receptor kinase was also inhibited by 1 mM-GTP[S] both in the absence (by 88%) and in the presence (by 81%) of insulin. In the absence of insulin, 1 mM-GTP had the same effect on calmodulin phosphorylation as 1 mM-GTP[S]. However, when insulin was present, GTP was less effective than GTP[S] (41% versus 81% inhibition). Concentrations of GTP[S] greater than 250 microM are necessary to inhibit phosphorylation. Although these concentrations are relatively high, the effect of GTP[S] is not due to competition with [32P]ATP for the insulin receptor kinase since (1) other nucleotide triphosphates did not inhibit phosphorylation as much as did GTP[S] (or GTP) and (2) the Vmax of the ATP-dependent kinase reaction was decreased in the presence of GTP[S]. GTP[S] (1 mM) also inhibited insulin binding to isolated receptors and plasma membranes, by 80% and 50% respectively. Finally, an antibody raised to a peptide sequence common to the alpha-subunits of G-proteins Gs, Gi, Go and transducin detected G-proteins in plasma membranes but failed to detect them in the insulin receptor preparation. These results indicate that GTP inhibits insulin receptor function, but does so through a mechanism that does not require a conventional GTP-binding protein.

Sign in / Sign up

Export Citation Format

Share Document