hormone secreted by the β cells of the islets of Langerhans, specific groups of cells in the pancreas. Insufficiency of insulin in the body results in diabetes. Insulin was one of the first products to be manufactured using genetic engineering.
In general, insulin acts to reduce extracellular (including blood plasma) levels of glucose by interacting in some way yet unknown with various cell membranes. In adipose (fatty) tissue it facilitates the cellular uptake of glucose and its subsequent conversion to fatty acids, and it inhibits the breakdown of fatty acids to simpler compounds. In muscle it again facilitates the transport of glucose into cells and in addition stimulates its conversion to glycogen. It also increases protein synthesis in muscle. In the liver, insulin facilitates glucose catabolism and its conversion to glycogen and inhibits its synthesis from simpler compounds.
Frederick G. Banting, Charles H. Best, and J. J. R. Macleod were the first to obtain, from extracts of pancreas (1921–22), a preparation of insulin that could serve to replace a deficiency of the hormone in the human body. The complete amino acid sequence of the insulin molecule was described in the early 1950s; insulin was the first protein to be sequenced entirely. This pioneering work was confirmed from 1963 to 1966, when several groups reported laboratory synthesis of biologically active insulin. The three-dimensional structure of the crystalline hormone was published in 1969.
Insulin has been shown to be a protein consisting of two polypeptide chains (see peptide), one of 21 amino acid residues and the other of 30, joined by two disulfide bridges (see cysteine). The two chains are synthesized in the β cells as part of one continuous polypeptide chain called proinsulin; a 32-amino acid sequence (the connecting peptide) is subsequently split out of the proinsulin molecule by an enzyme resembling trypsin to yield active insulin.
Many, but not all, of the symptoms of diabetes can be controlled by the administration of insulin. The forms of insulin available early in the 20th cent. had to be injected frequently because they were quick-acting. Later modifications gave the insulin solution a more prolonged action so that hypodermic injections could be made less frequently. Some now control their insulin levels via a small, portable insulin pump. In certain cases of mild diabetes, oral medications that stimulate production of insulin can be taken in lieu of insulin. See glucagon.
Insulin is a hormone that is made in the beta cells of the pancreas and plays a critical role in the use of glucose (sugar) in the body. In the...
A peptide hormone with a molecular weight of 5808, containing two chains. Source: FAO (2002)...
Polypeptide hormone (see peptide) that regulates blood glucose levels. Secreted by the islets of Langerhans (see Langerhans, islets of) in the panc