Tag: Peptide hormone (51-amino-acid disulfide-linked dipeptide)

  • Insulin (Research)

    Peptide hormone (51-amino-acid disulfide-linked dipeptide)

    The pancreatic peptide hormone insulin; the foundational glucose-regulatory hormone and a research probe for metabolic and anabolic biology.

    Abstract

    Insulin (CAS 9004-10-8; A-chain 21 amino acids, B-chain 30 amino acids; total molecular weight approximately 5808 Da for human insulin) is the pancreatic peptide hormone discovered by Banting and Best in 1921 (Nobel Prize 1923) and synthesized as recombinant human insulin (Humulin) in 1982 by Genentech, the first FDA-approved recombinant pharmaceutical. Pharmacologically, insulin binds the insulin receptor (IR) and the IGF-1 receptor (IGF-1R) with substantially higher affinity for IR. Receptor binding triggers tyrosine kinase activation of IRS-1/2 and downstream PI3K-Akt signaling, regulating glucose uptake (GLUT4 translocation), glycogen synthesis, lipogenesis, and protein synthesis. Modern formulations include rapid-acting analogs (lispro, aspart, glulisine), regular insulin, intermediate (NPH), long-acting (glargine, detemir, degludec), and ultra-long-acting (degludec). Approved indications: type 1 diabetes (essential), type 2 diabetes (when oral agents fail). The principal safety risk is hypoglycemia, severe enough to cause neuronal injury or death; insulin is among the leading drug-related causes of medical emergency department visits. Recreational anabolic use has been documented but is associated with high acute mortality. Used as the canonical metabolic hormone in academic biology.

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