| Autor: |
Bowe JE; Diabetes Research Group; Division of Diabetes & Nutritional Sciences; King's College London; London, UK., Foot VL; Diabetes Research Group; Division of Diabetes & Nutritional Sciences; King's College London; London, UK., Amiel SA; Diabetes Research Group; Division of Diabetes & Nutritional Sciences; King's College London; London, UK., Huang GC; Diabetes Research Group; Division of Diabetes & Nutritional Sciences; King's College London; London, UK., Lamb MW; Department of Surgery; University of California; Irvine, CA USA., Lakey J; Department of Surgery; University of California; Irvine, CA USA., Jones PM; Diabetes Research Group; Division of Diabetes & Nutritional Sciences; King's College London; London, UK., Persaud SJ; Diabetes Research Group; Division of Diabetes & Nutritional Sciences; King's College London; London, UK. |
| Abstrakt: |
This study was designed to determine the effects of 10 and 13 amino acid forms of kisspeptin on dynamic insulin secretion from mammalian islets since it is not clear from published data whether the shorter peptide is stimulatory while the longer peptide inhibits insulin release. Insulin secretion was measured by radioimmunoassay following perifusion of human, pig, rat and mouse isolated islets with kisspeptin-10 or kisspeptin-13 in the presence of 20 mM glucose. Both peptides stimulated rapid, reversible potentiation of glucose-stimulated insulin secretion from islets of all species tested. These data indicate that both kisspeptin-10 and kisspeptin-13, which is an extension of kisspeptin-10 by three amino acids, act directly at islet β-cells of various species to potentiate insulin secretion, and suggest that inhibitory effects reported in earlier studies may reflect differences in experimental protocols. |
