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Insulin is a peptide hormone made by pancreatic beta cells and encoded by the INS gene; it is central to glucose homeostasis and anabolic metabolism.
Insulin is a peptide hormone produced by pancreatic beta cells in the islets of Langerhans. Encoded by the human INS gene, it is the body’s main anabolic hormone, regulating metabolism of carbohydrates, fats, and proteins. Insulin promotes glucose uptake into liver, fat, and skeletal muscle cells and supports conversion of absorbed glucose into glycogen and fats, while high circulating insulin strongly inhibits liver glucose production. It is secreted in response to elevated blood glucose and suppressed when glucose is low, helping maintain glucose homeostasis alongside glucagon. Structurally, human insulin is a heterodimer made of an A-chain and a B-chain linked by disulfide bonds (with an additional intrachain disulfide bond in the A-chain). It is synthesized as an inactive precursor, preproinsulin, then processed to proinsulin and cleaved to remove the C-peptide, producing mature insulin that is stored in secretory granules and released upon metabolic signals. Insulin is released from beta cells in two phases (a rapid first phase and a sustained second phase), and its deficiency or impaired activity leads to diabetes (type 1 from autoimmune beta-cell destruction and type 2 from less pronounced beta-cell dysfunction plus insulin resistance).
Insulin is a peptide hormone made by pancreatic beta cells and encoded by the INS gene; it is central to glucose homeostasis and anabolic metabolism.
Human insulin consists of A- and B-chains linked by disulfide bonds; it is synthesized as preproinsulin/proinsulin and processed to remove C-peptide before secretion.
Insulin secretion occurs in two phases in response to blood glucose, and reduced insulin activity contributes to diabetes (type 1 and type 2).
A peptide hormone produced by pancreatic beta cells that regulates carbohydrate, fat, and protein metabolism and lowers blood glucose by promoting cellular glucose uptake.
The human gene that encodes insulin, located on chromosome 11.
The two peptide chains of insulin that are linked by disulfide bonds to form the active hormone.
Covalent bonds between cysteine residues that connect insulin chains and stabilize insulin’s structure.
The inactive 110-amino-acid precursor of insulin that is translated into the rough endoplasmic reticulum and processed to proinsulin.
The folded intermediate form of insulin that contains the C-peptide and is packaged for further processing in secretory granules.
The middle segment removed from proinsulin during processing to produce mature insulin.
Beta-cell insulin release occurs first rapidly (about 10 minutes) and then more slowly and sustainedly (peaking after 2–3 hours).
A form of diabetes caused by autoimmune destruction of insulin-producing beta cells, leading to absolute insulin deficiency.
A form of diabetes involving insulin resistance and impaired beta-cell function, often associated with disrupted islet biology and increased glucagon activity.
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