What is Insulin, Fasting, Serum?
Insulin is a 51-amino acid peptide hormone synthesised as preproinsulin by pancreatic beta cells of the islets of Langerhans, processed through cleavage of the signal peptide and C-peptide to form the mature two-chain disulphide-linked insulin molecule. It is co-secreted with equimolar amounts of C-peptide — a clinically important distinction, as C-peptide persists longer in circulation (half-life approximately 35 minutes vs insulin 5–10 minutes) and is not removed by hepatic first-pass metabolism, making C-peptide a more reliable index of endogenous insulin secretion when hepatic extraction is a variable. Insulin secretion has two phases: a rapid first-phase release of pre-formed granules within 2–5 minutes of glucose stimulation, and a slower second-phase synthesis-dependent release over 60–90 minutes. Fasting insulin reflects basal insulin secretion — the minimal level required to suppress hepatic glucose output (gluconeogenesis and glycogenolysis) and prevent lipolysis between meals, in the absence of postprandial stimulation. In insulin resistance states, the pancreatic beta cells compensate for reduced insulin receptor sensitivity by secreting proportionally more insulin to maintain euglycaemia — fasting hyperinsulinaemia develops before fasting glucose rises, making fasting insulin the earliest biochemical marker of insulin resistance in individuals with preserved beta cell compensatory capacity.