Amylin inhibits glucose-induced insulin secretion in a dose-dependent manner. Study in the perfused rat pancreas.
Islet amyloid polypeptide (IAPP), also called amylin, has been localized in the B-cell secretory granule and is co-secreted with insulin. We have investigated the effect of synthetic amidated rat amylin on the insulin release evoked by 9 mM glucose in the isolated, perfused rat pancreas. Amylin, in a range of 75 nM-75 pM, significantly inhibited this insulin response in a dose-dependent manner. The correlation between the logarithm of amylin concentrations and the percentages of inhibition was highly significant (r = 0.98, P < 0.01). The lowest effective amylin concentration tested (75 pM) is within the range of amylin levels reported for the effluent of the perfused rat pancreas. Finally, pre-infusion of the rat pancreas with a high amylin concentration (75 nM) did not alter the insulin response to glucose, thus excluding a toxic effect of amylin on the B-cell. These observations support the concept that amylin plays a role in the control of insulin secretion.
Dégano
P
P
Hospital Puerta de Hierro, Universidad Autónoma de Madrid, Spain.
Silvestre
R A
RA
Salas
M
M
Peiró
E
E
Marco
J
J
D000682:Amyloid / Q000494:pharmacology*; D000818:Animals; D004305:Dose-Response Relationship, Drug; D005947:Glucose / Q000494:pharmacology; D066298:In Vitro Techniques; D007328:Insulin / Q000378:metabolism*; D000078790:Insulin Secretion; D058228:Islet Amyloid Polypeptide; D007515:Islets of Langerhans / Q000187:drug effects* / Q000378:metabolism; D008297:Male; D051381:Rats; D017208:Rats, Wistar
D000682:Amyloid; D007328:Insulin; D058228:Islet Amyloid Polypeptide; D005947:Glucose