proinsulin
Sign in to saveProinsulin is the prohormone precursor to insulin made in the beta cells of the Pancreatic Islets, specialized regions of the pancreas. In humans, proinsulin is encoded by the INS gene. The pancreatic islets only secrete between 1% and 3% of proinsulin intact. However, because proinsulin has a longer half life than insulin, it can account for anywhere from 5–30% of the insulin-like structures circulating in the blood. There are higher concentrations of proinsulin after meals and lower levels when a person is fasting. Additionally, while proinsulin and insulin have structural differences, proin
Key facts
- Protein.caption
- Insulin undergoes extensive posttranslational modification along the production pathway. Production and secretion are largely independent; prepared insulin is stored awaiting secretion. Both C-peptide and mature insulin are biologically active. Cell components and proteins in this image are not to scale.
- Protein.image
- Insulin path.svg
- Protein.width
- 220px
- Protein.HGNCid
- 6081
- Protein.Symbol
- INS
- Protein.EntrezGene
- 3630
- Protein.OMIM
- 176730
- Protein.RefSeq
- NM_000207
- Protein.UniProt
- P01308
- Protein.Chromosome
- 11
- Protein.Arm
- p
- Protein.Band
- 15.5
- Protein.Name
- insulin
via Wikipedia infobox
Article
8 sectionsContents
- Structure
- Synthesis and Post-translational Modification
- Immunogenicity
- Medical Relevance
- [[Diabetes mellitus|Diabetes Mellitus]]
- [[Neonatal diabetes mellitus|Neonatal Diabetes Mellitus]]
- See also
- References
Proinsulin is the prohormone precursor to insulin made in the beta cells of the Pancreatic Islets, specialized regions of the pancreas. In humans, proinsulin is encoded by the INS gene. The pancreatic islets only secrete between 1% and 3% of proinsulin intact. However, because proinsulin has a longer half life than insulin, it can account for anywhere from 5–30% of the insulin-like structures circulating in the blood. There are higher concentrations of proinsulin after meals and lower levels when a person is fasting. Additionally, while proinsulin and insulin have structural differences, proinsulin does demonstrate some affinity for the insulin receptor. Due to the relative similarities in structure, proinsulin can produce between 5% and 10% of the metabolic activity similarly induced by insulin.
Proinsulin is the final single chain protein structure secreted by cells before cleavage into mature insulin. Proinsulin was discovered by Professor Donald F. Steiner of the University of Chicago in 1967.