Amylin (rat, mouse) (trifluoroacetate salt)

Amylin is a 37-residue peptide hormone secreted by pancreatic β-cells that reduces food intake, modifies glycogen synthesis, slows gastric emptying, and increases satiety.1,2,3,4 It binds to heteromeric complexes of human calcitonin receptor 2 (CTR2) with receptor activity-modifying protein (RAMP) 1 or 3 (IC50s = 7.86 and 6.35 nM, respectively).5 It also binds to mouse α-thyroid-stimulating hormone thyrotroph (α-TSH) cells (IC50 = 10.5 nM) and rat nucleus accumbens membrane preparations (Ki = 0.024 nM).4,5 In vitro, amylin (100 nM) inhibits insulin-induced, but not basal, glycogen synthesis in hepatocytes isolated from fasted rats.3 It also inhibits insulin-induced glycogen synthesis ex vivo in isolated soleus muscle from fasted rats.4 In vivo, amylin delays gastric emptying in rats (ED50 = 69 pmol) and decreases food intake in fasted mice (ED50 = 110 μg/kg).2,4 Unlike human amylin (Item No. 24274), rat amylin does not form fibrils and is not cytotoxic.6WARNING This product is not for human or veterinary use.

[1] LUTZ T A. Control of food intake and energy expenditure by amylin-therapeutic implications.[J]. International Journal of Obesity, 2009, 33 Suppl 1: S24-7. DOI: 10.1038/ijo.2009.13
[2] C M MACK. Davalintide (AC2307), a novel amylin-mimetic peptide: enhanced pharmacological properties over native amylin to reduce food intake and body weight[J]. International Journal of Obesity, 2009, 34 2: 385-395. DOI: 10.1038/ijo.2009.238
[3] A M GÓMEZ-FOIX  J J G  J E Rodriguez Gil. Anti-insulin effects of amylin and calcitonin-gene-related peptide on hepatic glycogen metabolism.[J]. Biochemical Journal, 1991, 276 ( Pt 3): 607-610. DOI: 10.1042/bj2760607
[4] WILLIAM VINE. Comparison of the in vitro and in vivo pharmacology of adrenomedullin, calcitonin gene-related peptide and amylin in rats[J]. European journal of pharmacology, 1996, 314 1: Pages 115-121. DOI: 10.1016/s0014-2999(96)00544-4
[5] G CHRISTOPOULOS. Multiple amylin receptors arise from receptor activity-modifying protein interaction with the calcitonin receptor gene product.[J]. Molecular Pharmacology, 1999, 56 1: 235-242. DOI: 10.1124/mol.56.1.235
[6] JANELLE GREEN . Full-length Rat Amylin Forms Fibrils Following Substitution of Single Residues from Human Amylin[J]. Journal of Molecular Biology, 2003, 326 4: Pages 1147-1156. DOI: 10.1016/s0022-2836(02)01377-3