J. Dolais-Kitabgi

Learn More
The effects of neurotensin on insulin and somatostatin release were examined in isolated pancreatic islets prepared from 3-4 days rats, and maintained in culture for 48 h before use. In the presence of 12 mM glucose, glucagon (50-2,000 ng/ml, i.e. 14-560 nM) caused a 2-fold increase in insulin and somatostatin release. Neurotensin (150 ng/ml, i.e., 100 nM)(More)
The effects of neurotensin on the release of insulin, glucagon, and somatostatin were investigated in isolated pancreatic islets prepared from 3- to 4-day-old rats and maintained in culture for 48 h before use. Islets were incubated for 20 and 60 min in the presence of 3 or 23 mM glucose with or without neurotensin. In 20-min incubations at 3 mM glucose,(More)
Antibodies against peptides corresponding to sequences in the C-terminus of the insulin receptor beta-subunit were used to approach the putative role of this receptor domain in signal generation. Two sequences were chosen and correspond to peptide C1, comprising amino acids 1309-1326, and peptide C2, comprising amino acids 1294-1317. The two antibodies(More)
The role of the insulin receptor carboxyl-terminal domain in regulation of insulin signal transduction was studied with antipeptide antibodies against the sequence 1321-1338, which contains two autophosphorylation sites, tyrosine 1328 and tyrosine 1334. The antibodies were introduced by electroporation in murine fibroblasts transfected with an expression(More)
Anti-peptide antibodies directed against a highly-conserved sequence of the insulin receptor tyrosine kinase domain have been used to study the relationship between this specific region and kinase activation. Antibodies have been prepared by the injection into a rabbit of a synthetic peptide (P2) corresponding to residues 1110-1125 of the proreceptor. The(More)
A mutation substituting a valine for phenylalanine at residue 382 in the insulin receptor alpha-subunit has been found in two sisters with a genetic form of extreme insulin resistance. This receptor mutation impairs the ability of the hormone to activate autophosphorylation of solubilized receptors and phosphorylation of substrates (Accili, D., Mosthaf, L.,(More)
The effect of the hypoglycaemic biguanide, metformin, on insulin binding and insulin action was investigated in rat hepatocyte monolayers. The binding of insulin was not modified in cultured cells exposed for 24 or 48 h to metformin at concentrations ranging from 1 mumol/l to 1 mmol/l, and no effect could be detected on insulin-induced down regulation.(More)
For the insulin receptor and the EGF receptor it is believed that ligand occupancy results in interactions within the heterotetrameric alpha 2 beta 2 insulin receptor or between monomeric EGF receptors. These interactions then activate the intracellular receptor tyrosine kinase which induces receptor autophosphorylation and phosphorylation of cellular(More)
The pancreatic content of somatostatin, insulin, and glucagon and the hypothalamic content of somatostatin were examined inob/ob mice at various ages and in goldthioglucose-obese mice. The total pancreatic content of somatostatin was increased inob/ob mice compared to controls: 92 ng vs 75 ng (a 22% increase) at 2 months of age; 208 ng vs 131 ng (a 60%(More)
This paper describes the properties of rabbit polyclonal antibodies directed against purified human insulin receptor which strongly stimulate the intrinsic tyrosine kinase activity. The stimulatory effect of the antibodies on the kinase activity was obtained on the insulin receptor autophosphorylation as well as on the kinase activity towards a synthetic(More)