The clearly elevated risk of mortality for the fetus necessitates intensive monitoring. Reduced glucose tolerance during pregnancy always requires treatment. In 3 % of persons with reduced glucose tolerance, the metabolic state deteriorates towards diabetes mellitus over a period of time. Hypoglycemia can, however, also be facilitated intentionally or unintentionally (factitious hypoglycemia). as a result of severe hepatic or renal failure, islet cell adenoma, or carcinoma. This condition is brought about by inhibition of gluconeogenesis, e.g. On the other hand, autonomous, non - regulated insulin secretion is generally the cause of hypoglycemia. Possible causes of this include destruction of the β‑cells (type I diabetes), reduced activity of the insulin or reduced pancreatic synthesis (type II), circulating antibodies to insulin, delayed release of insulin or the absence (or inadequacy) of insulin receptors. A too low concentration of free, biologically active insulin can lead to the development of diabetes mellitus.
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In this case, measurement of the concentration of serum insulin shows the quantity of free - and hence biologically active - hormone, whereas the determination of C‑peptide provides a measure of the patient's total endogenous insulin secretion.Ī disorder in insulin metabolism leads to massive influencing of a number of metabolic processes. For example, therapeutic administration of insulins of non - human origin can lead to the formation of anti‑insulin antibodies. in the tolbutamide test and glucagon test or in the evaluation of oral glucose tolerance tests or hunger provocation tests.Īlthough the adequacy of pancreatic insulin synthesis is frequently assessed via the determination of C‑peptide, it is still generally necessary to determine insulin. They are used to ascertain the glucose/insulin quotients and for clarification of questions concerning insulin secretion, e.g. Serum insulin determinations are mainly performed on patients with symptoms of hypoglycemia. The action of insulin is mediated by specific receptors and primarily consists of facilitation of the uptake of sugar by the cells of the liver, fatty tissue and musculature this is the basis of its hypoglycemic action. The amino acid sequence of insulin has remained surprisingly constant during evolution, with the result that prior to the development of genetically engineered human insulin it was possible to successfully use porcine or bovine insulin in the therapy of diabetes mellitus. Circulating insulin has a half‑life of 3‑5 minutes and is preferentially degraded in the liver, whereas inactivation or excretion of proinsulin and C‑peptide mainly takes place in the kidneys. About half of the insulin, but virtually none of the C‑peptide, is retained in the liver. Specific proteases cleave proinsulin to insulin and C‑peptide which pass into the bloodstream simultaneously.
Biosynthesis of the hormone takes place in the β‑cells of the islets of Langerhans in the form of single‑chain preproinsulin, which is immediately cleaved to give proinsulin. The insulin molecule consists of two polypeptide chains, the α‑chain with 21 and the β‑chain with 30 amino acids. Insulin is generally released in pulses, with the parallel glucose cycle normally about 2 minutes ahead of the insulin cycle. It is secreted by the B‑cells of the pancreas and passes into circulation via the portal vein and the liver. Insulin is a peptide hormone with a molecular weight of approximately 6000 daltons.
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