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C-peptide Is a stable fragment of endogenously produced proinsulin that is "cleaved" from it during insulin production. It consists of 31 amino acid residues, is located between the alpha and beta chains of proinsulin and is biologically inactive. Once the insulin molecule is synthesized in the pancreatic beta cells, the C-peptide is released into the bloodstream along with insulin. Insulin is inactive before the C-peptide is removed, which allows the pancreas to store insulin as a prohormone. It should be noted that although the number of C-peptide and insulin molecules produced during secretion is the same, the equilibrium concentration of C-peptide in the blood is approximately 5 times the molar concentration of insulin, which is related to the different rate of their elimination from the blood.
C-peptide concentration decreases:
Determining the level of C-peptide allows us to assess the level of insulin secretion. C-peptide determination has a number of advantages over insulin determination: The half-life of C-peptide in the blood is longer than that of insulin, so C-peptide levels are more stable than insulin concentrations. Determination of C-peptide makes it possible to assess insulin secretion even when taking exogenous insulin, as well as in the presence of autoantibodies to insulin, which is important in the examination of patients with type 1 diabetes.
C-peptide levels change according to changes in endogenous insulin concentration. The ratio of these parameters may change in the setting of liver and kidney disease because insulin is metabolized primarily in the liver while C-peptide metabolism and excretion are mediated by the kidneys. Accordingly, the determination of this indicator may be the main, in case of impaired liver function, adequate interpretation of changes in insulin concentration in the blood.
Monitoring of C-peptide levels is especially important in patients after surgical treatment of insulinoma; Elevated levels of C-peptide in the blood indicate metastases or tumor recurrence.
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