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Insulin is synthesized and secreted in the beta cells of the islets of Langerhans. Once insulin is synthesized, the beta cells are ready to release it in two different phases. As for the first phase, insulin release is triggered rapidly when the blood glucose level is increased.
Beta cells are the only site of insulin synthesis in mammals. [7] As glucose stimulates insulin secretion, it simultaneously increases proinsulin biosynthesis through translational control and enhanced gene transcription. [4] [8] The insulin gene is first transcribed into mRNA and translated into preproinsulin. [4]
Insulin was the first peptide hormone discovered. [17] Frederick Banting and Charles Best, working in the laboratory of John Macleod at the University of Toronto, were the first to isolate insulin from dog pancreas in 1921. Frederick Sanger sequenced the amino acid structure in 1951, which made insulin the first protein to be fully sequenced. [18]
The insulin receptor (IR) is a transmembrane receptor that is activated by insulin, IGF-I, IGF-II and belongs to the large class of receptor tyrosine kinase. [5] Metabolically, the insulin receptor plays a key role in the regulation of glucose homeostasis; a functional process that under degenerate conditions may result in a range of clinical manifestations including diabetes and cancer.
Insulin was first used as a medication in Canada by Charles Best and Frederick Banting in 1922. [85] [86] This is a chronology of key milestones in the history of the medical use of insulin. For more details on the discovery, extraction, purification, clinical use, and synthesis of insulin, see Insulin
Transcription of insulin is regulated by the binding of various transcription factors to the ~400 base pairs before the insulin transcription start site, called the "insulin regulatory sequence". [1] This sequence is made up of several distinct regions with different biochemical properties, each of which serve as binding sites for distinct ...
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