Heterogeneity of immunoreactive gastric inhibitory polypeptide in the plasma of newly diagnosed type 1 (insulin-dependent) diabetics. 1987

T Krarup, and J J Holst, and S Madsbad

The aim was to compare the three molecular forms of plasma immunoreactive gastric inhibitory polypeptide (IR-GIP) i.e. void volume (Vo), 8 and 5 kDa IR-GIP, found in type 1 diabetics with those found in normal subjects. Plasma from 6 non-fasting newly diagnosed ketotic type 1 diabetics obtained before and 1 h after a test meal given at start of insulin treatment, and before and 1 h after a test meal given after one and seven days of insulin treatment, respectively, was gel filtered and so was plasma from 6 normal subjects. The immunoreactivity in the effluents was measured with five different antisera. The elution positions of the three peaks were similar in controls and diabetics. With any given antiserum none of the components differed significantly as to amount of immunoreactivity between diabetics and controls, neither after the meals nor in the fasting state. The amount of Vo did not change in response to the meal, whereas the 8 and 5 kDa forms in the diabetics increased similarly to the increase in normals, also during ketosis. The Vo component did not differ significantly between diabetic and normal subjects, but it decreased significantly after start of insulin treatment. In the non-fasting, ketotic state before start of insulin treatment, no IR-GIP form was elevated significantly above normal postprandial levels. We conclude that the molecular forms of IR-GIP are similar in type 1 diabetics and normal subjects, but the molecular forms measured and their relative amounts vary according to which antiserum is used. The present study does not support that lack of insulin and ketosis markedly influence IR-GIP in plasma.

UI MeSH Term Description Entries
D007328 Insulin A 51-amino acid pancreatic hormone that plays a major role in the regulation of glucose metabolism, directly by suppressing endogenous glucose production (GLYCOGENOLYSIS; GLUCONEOGENESIS) and indirectly by suppressing GLUCAGON secretion and LIPOLYSIS. Native insulin is a globular protein comprised of a zinc-coordinated hexamer. Each insulin monomer containing two chains, A (21 residues) and B (30 residues), linked by two disulfide bonds. Insulin is used as a drug to control insulin-dependent diabetes mellitus (DIABETES MELLITUS, TYPE 1). Iletin,Insulin A Chain,Insulin B Chain,Insulin, Regular,Novolin,Sodium Insulin,Soluble Insulin,Chain, Insulin B,Insulin, Sodium,Insulin, Soluble,Regular Insulin
D008297 Male Males
D008968 Molecular Conformation The characteristic three-dimensional shape of a molecule. Molecular Configuration,3D Molecular Structure,Configuration, Molecular,Molecular Structure, Three Dimensional,Three Dimensional Molecular Structure,3D Molecular Structures,Configurations, Molecular,Conformation, Molecular,Conformations, Molecular,Molecular Configurations,Molecular Conformations,Molecular Structure, 3D,Molecular Structures, 3D,Structure, 3D Molecular,Structures, 3D Molecular
D011863 Radioimmunoassay Classic quantitative assay for detection of antigen-antibody reactions using a radioactively labeled substance (radioligand) either directly or indirectly to measure the binding of the unlabeled substance to a specific antibody or other receptor system. Non-immunogenic substances (e.g., haptens) can be measured if coupled to larger carrier proteins (e.g., bovine gamma-globulin or human serum albumin) capable of inducing antibody formation. Radioimmunoassays
D001786 Blood Glucose Glucose in blood. Blood Sugar,Glucose, Blood,Sugar, Blood
D002096 C-Peptide The middle segment of proinsulin that is between the N-terminal B-chain and the C-terminal A-chain. It is a pancreatic peptide of about 31 residues, depending on the species. Upon proteolytic cleavage of proinsulin, equimolar INSULIN and C-peptide are released. C-peptide immunoassay has been used to assess pancreatic beta cell function in diabetic patients with circulating insulin antibodies or exogenous insulin. Half-life of C-peptide is 30 min, almost 8 times that of insulin. Proinsulin C-Peptide,C-Peptide, Proinsulin,Connecting Peptide,C Peptide,C Peptide, Proinsulin,Proinsulin C Peptide
D002850 Chromatography, Gel Chromatography on non-ionic gels without regard to the mechanism of solute discrimination. Chromatography, Exclusion,Chromatography, Gel Permeation,Chromatography, Molecular Sieve,Gel Filtration,Gel Filtration Chromatography,Chromatography, Size Exclusion,Exclusion Chromatography,Gel Chromatography,Gel Permeation Chromatography,Molecular Sieve Chromatography,Chromatography, Gel Filtration,Exclusion Chromatography, Size,Filtration Chromatography, Gel,Filtration, Gel,Sieve Chromatography, Molecular,Size Exclusion Chromatography
D003922 Diabetes Mellitus, Type 1 A subtype of DIABETES MELLITUS that is characterized by INSULIN deficiency. It is manifested by the sudden onset of severe HYPERGLYCEMIA, rapid progression to DIABETIC KETOACIDOSIS, and DEATH unless treated with insulin. The disease may occur at any age, but is most common in childhood or adolescence. Diabetes Mellitus, Brittle,Diabetes Mellitus, Insulin-Dependent,Diabetes Mellitus, Juvenile-Onset,Diabetes Mellitus, Ketosis-Prone,Diabetes Mellitus, Sudden-Onset,Diabetes, Autoimmune,IDDM,Autoimmune Diabetes,Diabetes Mellitus, Insulin-Dependent, 1,Diabetes Mellitus, Type I,Insulin-Dependent Diabetes Mellitus 1,Juvenile-Onset Diabetes,Type 1 Diabetes,Type 1 Diabetes Mellitus,Brittle Diabetes Mellitus,Diabetes Mellitus, Insulin Dependent,Diabetes Mellitus, Juvenile Onset,Diabetes Mellitus, Ketosis Prone,Diabetes Mellitus, Sudden Onset,Diabetes, Juvenile-Onset,Diabetes, Type 1,Insulin Dependent Diabetes Mellitus 1,Insulin-Dependent Diabetes Mellitus,Juvenile Onset Diabetes,Juvenile-Onset Diabetes Mellitus,Ketosis-Prone Diabetes Mellitus,Sudden-Onset Diabetes Mellitus
D005260 Female Females
D005749 Gastric Inhibitory Polypeptide A gastrointestinal peptide hormone of about 43-amino acids. It is found to be a potent stimulator of INSULIN secretion and a relatively poor inhibitor of GASTRIC ACID secretion. Glucose-Dependent Insulinotropic Peptide,Gastric-Inhibitory Polypeptide,Glucose Dependent Insulinotropic Peptide,Glucose-Dependent Insulin-Releasing Peptide,Glucose Dependent Insulin Releasing Peptide,Inhibitory Polypeptide, Gastric,Insulin-Releasing Peptide, Glucose-Dependent,Insulinotropic Peptide, Glucose-Dependent,Peptide, Glucose-Dependent Insulin-Releasing,Peptide, Glucose-Dependent Insulinotropic,Polypeptide, Gastric Inhibitory,Polypeptide, Gastric-Inhibitory

Related Publications

T Krarup, and J J Holst, and S Madsbad
January 1988, Acta medica Scandinavica,
T Krarup, and J J Holst, and S Madsbad
November 1978, Journal of clinical & laboratory immunology,
T Krarup, and J J Holst, and S Madsbad
August 1979, The Journal of clinical endocrinology and metabolism,
T Krarup, and J J Holst, and S Madsbad
February 1988, Endocrine reviews,
T Krarup, and J J Holst, and S Madsbad
December 1983, Australian and New Zealand journal of medicine,
T Krarup, and J J Holst, and S Madsbad
January 2012, Journal of Ayub Medical College, Abbottabad : JAMC,
T Krarup, and J J Holst, and S Madsbad
November 1984, Diabetologia,
Copied contents to your clipboard!