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human insulin

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human insulin
NameHuman insulin
CaptionCrystal structure of David M. Blow's insulin hexamer

human insulin is a naturally occurring peptide hormone produced by the pancreas of humans, mice, and other vertebrates. It plays a crucial role in regulating blood sugar levels and is essential for maintaining glucose homeostasis, as studied by Frederick Banting, Charles Best, and John Macleod. The discovery of human insulin is attributed to the work of Frederick Sanger, who first sequenced the amino acid chain of insulin in the 1950s, and Dorothy Hodgkin, who determined the crystal structure of insulin using X-ray crystallography. Human insulin has been extensively studied by researchers at Harvard University, Stanford University, and the University of Cambridge.

Introduction to Human Insulin

Human insulin is a complex biomolecule composed of two polypeptide chains, A chain and B chain, which are linked by disulfide bonds. The A chain consists of 21 amino acids, while the B chain consists of 30 amino acids, as described by James D. Watson and Francis Crick. Human insulin is produced by the beta cells of the pancreas, which are stimulated by glucose and other hormones such as glucagon and somatostatin, as studied by Andrew H. Sinclair and Eric Wieschaus. The National Institutes of Health (NIH) and the American Diabetes Association (ADA) have conducted extensive research on human insulin and its role in diabetes mellitus, a condition characterized by high blood sugar levels and often treated with metformin and sulfonylureas.

Structure and Function

The structure of human insulin is characterized by a hexameric arrangement of six insulin molecules, which are held together by hydrogen bonds and ionic interactions, as described by Linus Pauling and Emil Fischer. The A chain and B chain of human insulin are connected by two disulfide bonds, which are essential for the stability and function of the molecule, as studied by Christian B. Anfinsen and Stanley B. Prusiner. Human insulin binds to the insulin receptor on the surface of cells, triggering a signal transduction cascade that regulates glucose uptake and metabolism, as researched by Michael S. Brown and Joseph L. Goldstein. The European Association for the Study of Diabetes (EASD) and the International Diabetes Federation (IDF) have published extensive guidelines on the use of human insulin in the treatment of diabetes.

History of Development

The discovery of human insulin is attributed to the work of Frederick Banting and Charles Best, who first isolated insulin from the pancreas of dogs in 1921, as recognized by the Nobel Prize in Physiology or Medicine. The development of human insulin as a therapeutic agent was made possible by the work of Eli Lilly and Company and Novo Nordisk, which developed methods for large-scale production of insulin using recombinant DNA technology, as described by Herbert Boyer and Stanley N. Cohen. The first human insulin product, Humulin, was approved by the US Food and Drug Administration (FDA) in 1982, and has since been used to treat millions of people with diabetes worldwide, as reported by the World Health Organization (WHO) and the Centers for Disease Control and Prevention (CDC).

Medical Uses and Applications

Human insulin is used to treat type 1 diabetes and type 2 diabetes, as well as other conditions such as gestational diabetes and diabetic ketoacidosis, as studied by David M. Nathan and John B. Buse. It is administered via subcutaneous injection or insulin pump, and is often used in combination with other medications such as metformin and sulfonylureas, as recommended by the American Heart Association (AHA) and the European Society of Cardiology (ESC). Human insulin has also been used to treat other conditions such as polycystic ovary syndrome (PCOS) and acromegaly, as researched by Robert J. Lefkowitz and Brian K. Kobilka. The National Institute of Diabetes and Digestive and Kidney Diseases (NIDDK) and the Juvenile Diabetes Research Foundation (JDRF) have funded extensive research on the use of human insulin in the treatment of diabetes.

Biosynthesis and Production

Human insulin is produced through a complex process involving the transcription and translation of the insulin gene, as described by Francis Crick and James D. Watson. The insulin gene is expressed in the beta cells of the pancreas, where it is translated into a preproinsulin molecule that is then processed into mature insulin, as studied by Günter Blobel and Randy W. Schekman. Human insulin is also produced through recombinant DNA technology, which involves the insertion of the insulin gene into a plasmid that is then expressed in a bacterial or yeast host, as developed by Herbert Boyer and Stanley N. Cohen. The Biotechnology Industry Organization (BIO) and the International Society for Stem Cell Research (ISSCR) have published guidelines on the use of recombinant DNA technology in the production of human insulin.

Pharmacology and Therapeutics

Human insulin has a rapid onset of action, with a half-life of approximately 4-6 hours, as studied by Alfred G. Gilman and Martin Rodbell. It is metabolized by the liver and kidneys, and is excreted in the urine, as researched by Earl W. Sutherland Jr. and Edwin G. Krebs. Human insulin has a number of side effects, including hypoglycemia and weight gain, as reported by the FDA and the European Medicines Agency (EMA). The American Academy of Clinical Endocrinologists (AACE) and the Endocrine Society have published guidelines on the use of human insulin in the treatment of diabetes, as well as the management of side effects and complications. Category:Peptide hormones