Insulin

Also known as: INS, P01308

**Mechanism of Action** Insulin (INS, UniProt P01308) is a peptide hormone that lowers blood glucose by binding to the insulin receptor (IR), a tyrosine kinase receptor. This triggers autophosphorylation and activation of downstream signaling cascades, primarily the PI3K/Akt pathway, which promotes translocation of GLUT4 transporters to the cell membrane in muscle and adipose tissue, facilitating glucose uptake. Additionally, insulin inhibits hepatic gluconeogenesis and glycogenolysis while stimulating glycogen synthesis, lipogenesis, and protein synthesis. **Key Research Findings** Insulin is one of the most extensively studied peptides, with over a century of research. Landmark studies (e.g., PubMed ID 456568) established its role in glucose homeostasis and its deficiency as the cause of diabetes mellitus. Recombinant human insulin (approved in 1982) revolutionized diabetes management, reducing immunogenicity compared to animal-derived insulins. Subsequent research has focused on insulin analogs (e.g., lispro, glargine) to optimize pharmacokinetics, and on understanding insulin resistance mechanisms in type 2 diabetes. **Clinical Relevance** Insulin is a cornerstone therapy for type 1 diabetes and advanced type 2 diabetes. Approved formulations include rapid-acting, short-acting, intermediate-acting, and long-acting analogs, enabling individualized glycemic control. Its use reduces hyperglycemia-related complications (e.g., nephropathy, retinopathy) but requires careful monitoring to avoid hypoglycemia. Ongoing research explores novel delivery systems (e.g., inhaled, oral) and closed-loop artificial pancreas technologies. For research purposes only — not medical advice.

Key data

Mechanism of action

Insulin decreases blood glucose concentration. It increases cell permeability to monosaccharides, amino acids and fatty acids. It accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver

Research & studies

Frequently asked questions

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