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Description

Amlintide (amylin) is a 37 amino acid peptide hormone that is closely related to calcitonin gene-related peptide (CGRP). Amylin was originally discovered as the main component of islet amyloid deposition in patients with type 2 diabetes. Amylin and CGRP share a receptor and are reported to have several similar biological actions. Amylin's major role is as a glucoregulatory hormone, and it is an important regulator of energy metabolism in health and disease. Other amylin actions have also been reported, such as on the cardiovascular system or on bone. Amylin acts principally in the circumventricular organs of the central nervous system and functionally interacts with other metabolically active hormones such as cholecystokinin, leptin, and estradiol. Amylin has been shown to have binding sites within the renal cortex in the area of the juxtaglomerular apparatus. Amylin has been shown to activate the rennin angiotensin aldosterone system. The amylin-based peptide, pramlintide, is used clinically to treat type 1 and type 2 diabetes. Pramlintide exhibits similar biologic activity to that of amylin. Clinical studies in obesity have shown that amylin agonists could also be useful for weight loss, especially in combination with other agents. Amylin is one of the few established gut/pancreatic hormones that has demonstrated durable, safe, tolerable, and clinically meaningful weight loss in humans.

Approval Year

PubMed

Sample Use Guides

In Vivo Use Guide
A rapid bolus of 50 ug of amlintide (synthetic human amylin) was injected in healthy subjects.
Route of Administration: Intravenous
In Vitro Use Guide
MCF-7 cells endogenously express human Amylin receptor CTR1 and CTR2. Stimulation of the receptor with Amylin results in the production of cAMP. The free, non-conjugated human Amylin results in an EC50 of 35.2±7.5 nM (r2=0.990), and the PEGylated human Amylin results in a EC50 of 30.8±6.7 nM (r=0.988)
Substance Class Protein
Protein Sub Type
Sequence Type COMPLETE
Record UNII
U3U3114NE1
Record Status Validated (UNII)
Record Version
Subunit 0

Structural Modifications