Detection of compounds in serum inhibiting insulin binding to erythrocyte receptors. 1988

N Ribarac-Stepić, and K Kovacina, and M Zamaklar, and M Devecerski
Institute for Nuclear Sciences Boris Kidric, Faculty of Medicine, Belgrade, Yugoslavia.

The erythrocytes were used as a model system to study insulin receptors in diabetic patients with highly increased insulin resistance. The specific binding of 125I-insulin to erythrocytes of these patients was markedly reduced. When erythrocytes prepared from non-diabetic subjects were exposed to serum of these patients, the decrease of insulin binding was reproduced. The binding of insulin showed a displacement curve that is parallel to the control values over the same range of hormone concentration, even in the case when control erythrocytes were preincubated with serum of diabetics with increased insulin resistance. These results indicate the presence of certain component in blood plasma of examined patients which alters insulin binding to receptors. The developed assay provides an efficient method for detection and identification of substances presented in the serum which can influence the binding of insulin to the specific sites as well as its biological effects.

UI MeSH Term Description Entries
D007333 Insulin Resistance Diminished effectiveness of INSULIN in lowering blood sugar levels: requiring the use of 200 units or more of insulin per day to prevent HYPERGLYCEMIA or KETOSIS. Insulin Sensitivity,Resistance, Insulin,Sensitivity, Insulin
D007457 Iodine Radioisotopes Unstable isotopes of iodine that decay or disintegrate emitting radiation. I atoms with atomic weights 117-139, except I 127, are radioactive iodine isotopes. Radioisotopes, Iodine
D011972 Receptor, Insulin A cell surface receptor for INSULIN. It comprises a tetramer of two alpha and two beta subunits which are derived from cleavage of a single precursor protein. The receptor contains an intrinsic TYROSINE KINASE domain that is located within the beta subunit. Activation of the receptor by INSULIN results in numerous metabolic changes including increased uptake of GLUCOSE into the liver, muscle, and ADIPOSE TISSUE. Insulin Receptor,Insulin Receptor Protein-Tyrosine Kinase,Insulin Receptor alpha Subunit,Insulin Receptor beta Subunit,Insulin Receptor alpha Chain,Insulin Receptor beta Chain,Insulin-Dependent Tyrosine Protein Kinase,Receptors, Insulin,Insulin Receptor Protein Tyrosine Kinase,Insulin Receptors
D003924 Diabetes Mellitus, Type 2 A subclass of DIABETES MELLITUS that is not INSULIN-responsive or dependent (NIDDM). It is characterized initially by INSULIN RESISTANCE and HYPERINSULINEMIA; and eventually by GLUCOSE INTOLERANCE; HYPERGLYCEMIA; and overt diabetes. Type II diabetes mellitus is no longer considered a disease exclusively found in adults. Patients seldom develop KETOSIS but often exhibit OBESITY. Diabetes Mellitus, Adult-Onset,Diabetes Mellitus, Ketosis-Resistant,Diabetes Mellitus, Maturity-Onset,Diabetes Mellitus, Non-Insulin-Dependent,Diabetes Mellitus, Slow-Onset,Diabetes Mellitus, Stable,MODY,Maturity-Onset Diabetes Mellitus,NIDDM,Diabetes Mellitus, Non Insulin Dependent,Diabetes Mellitus, Noninsulin Dependent,Diabetes Mellitus, Noninsulin-Dependent,Diabetes Mellitus, Type II,Maturity-Onset Diabetes,Noninsulin-Dependent Diabetes Mellitus,Type 2 Diabetes,Type 2 Diabetes Mellitus,Adult-Onset Diabetes Mellitus,Diabetes Mellitus, Adult Onset,Diabetes Mellitus, Ketosis Resistant,Diabetes Mellitus, Maturity Onset,Diabetes Mellitus, Slow Onset,Diabetes, Maturity-Onset,Diabetes, Type 2,Ketosis-Resistant Diabetes Mellitus,Maturity Onset Diabetes,Maturity Onset Diabetes Mellitus,Non-Insulin-Dependent Diabetes Mellitus,Noninsulin Dependent Diabetes Mellitus,Slow-Onset Diabetes Mellitus,Stable Diabetes Mellitus
D004910 Erythrocyte Membrane The semi-permeable outer structure of a red blood cell. It is known as a red cell 'ghost' after HEMOLYSIS. Erythrocyte Ghost,Red Cell Cytoskeleton,Red Cell Ghost,Erythrocyte Cytoskeleton,Cytoskeleton, Erythrocyte,Cytoskeleton, Red Cell,Erythrocyte Cytoskeletons,Erythrocyte Ghosts,Erythrocyte Membranes,Ghost, Erythrocyte,Ghost, Red Cell,Membrane, Erythrocyte,Red Cell Cytoskeletons,Red Cell Ghosts
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D001665 Binding Sites The parts of a macromolecule that directly participate in its specific combination with another molecule. Combining Site,Binding Site,Combining Sites,Site, Binding,Site, Combining,Sites, Binding,Sites, Combining
D001667 Binding, Competitive The interaction of two or more substrates or ligands with the same binding site. The displacement of one by the other is used in quantitative and selective affinity measurements. Competitive Binding

Related Publications

N Ribarac-Stepić, and K Kovacina, and M Zamaklar, and M Devecerski
January 1983, Proceedings of the European Dialysis and Transplant Association. European Dialysis and Transplant Association,
N Ribarac-Stepić, and K Kovacina, and M Zamaklar, and M Devecerski
September 1985, American journal of veterinary research,
N Ribarac-Stepić, and K Kovacina, and M Zamaklar, and M Devecerski
March 1999, Polskie Archiwum Medycyny Wewnetrznej,
N Ribarac-Stepić, and K Kovacina, and M Zamaklar, and M Devecerski
January 1994, Ukrainskii biokhimicheskii zhurnal (1978),
N Ribarac-Stepić, and K Kovacina, and M Zamaklar, and M Devecerski
September 1984, Biochemical and biophysical research communications,
N Ribarac-Stepić, and K Kovacina, and M Zamaklar, and M Devecerski
January 1982, Journees annuelles de diabetologie de l'Hotel-Dieu,
N Ribarac-Stepić, and K Kovacina, and M Zamaklar, and M Devecerski
January 1988, Acta diabetologica latina,
N Ribarac-Stepić, and K Kovacina, and M Zamaklar, and M Devecerski
January 1981, Progress in clinical and biological research,
N Ribarac-Stepić, and K Kovacina, and M Zamaklar, and M Devecerski
January 1982, Journees annuelles de diabetologie de l'Hotel-Dieu,
N Ribarac-Stepić, and K Kovacina, and M Zamaklar, and M Devecerski
October 1983, Indian journal of biochemistry & biophysics,
Copied contents to your clipboard!