What it is
Amylin is a hormone of 37 amino acids made by the beta cells of the pancreas — the same cells that make insulin — and released together with it. UniProt's record for the human hormone (P10997) gives its structure:
- 37 amino acids: KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY;
- a disulfide bond — a bridge between two sulfur atoms — joining the cysteines at positions 2 and 7, which closes a small ring at the front of the chain;
- an amidated tyrosine at the end, a cap that is part of the active hormone.
It is cut from a longer precursor of 89 residues: a 22-residue signal sequence that steers the chain into the cell's secretion machinery, a short propeptide, the 37-residue hormone itself (residues 34–70), and a 16-residue propeptide at the end.
How it was found
Amylin was found in 1987, and the name it is often given in papers — islet amyloid polypeptide — says where. Two groups isolated it independently from the amyloid deposits that build up in the pancreatic islets of many people with type 2 diabetes: Cooper and colleagues reported it in PNAS (PMID 3317417) and Westermark and colleagues in The Lancet (PMID 2887903). Amyloid is a tangle of protein fibres; this one turned out to be made of a hormone nobody had yet described.
What it does
UniProt's function annotation, summarising the published literature, describes amylin as a glucoregulatory hormone — one that helps manage blood sugar — acting through amylin receptors. Those receptors are not a single protein: each is a calcitonin receptor paired with a partner called a RAMP (receptor-activity-modifying protein). Amylin can bind the calcitonin receptor on its own too, but less selectively.
The actions most often attributed to it work alongside insulin after a meal:
| Action | What it means |
|---|---|
| Slower stomach emptying | Food reaches the gut more gradually, so sugar enters the blood more slowly |
| Less glucagon after meals | Glucagon raises blood sugar; holding it back complements insulin |
| More fullness | Signals in the brain that reduce how much is eaten |
Those three actions are the ones the Symlin label lists for pramlintide, and they are the reason amylin became a starting point for weight-loss drug design.
Why every amylin drug is an altered copy
Human amylin clumps. The same property that put it in the amyloid deposits it was discovered in makes it awkward as a medicine. Pramlintide's label records the fix: proline in place of alanine at position 25 and serine at positions 28 and 29 — positions that copy the rat hormone, which does not form these deposits. The newer molecules in this library take the idea further:
- Pramlintide — approved 2005-03-16 (NDA 021332) as an add-on to mealtime insulin; every Symlin presentation is now listed as discontinued.
- Cagrilintide — a long-acting amylin analogue tested with semaglutide for weight loss.
- Eloralintide — a newer amylin-receptor agonist in trials.
Where it stands
openFDA's Drugs@FDA returns no application with amylin itself as the active ingredient (2026-10-02). PubMed returns 5,039 records for amylin, 203 tagged as randomised controlled trials — most of them about the analogues rather than the hormone. Amylin's place in this library is the one somatostatin and ghrelin hold: a hormone the body makes, recorded so the drugs built on it make sense.
Related reading
Amylin leaves the beta cell alongside insulin and C-peptide, and one of its jobs is holding back glucagon, the hormone that raises blood sugar. For how the GLP-1 drugs it is now being paired with are dosed and priced, GLP1 Ledger covers the medicines by name; this entry records only the hormone.