Galanin-induced inhibition of insulin secretion from rat islets: effects of rat and pig galanin and galanin fragments and analogues
| Autor: | Bo Ahrén, Sören Gregersen, Ülo Langel, Gilberto Fisone, Tamas Bartfai, K. Hermansen |
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| Rok vydání: | 1991 |
| Předmět: |
Male
endocrine system medicine.medical_specialty Swine medicine.medical_treatment Molecular Sequence Data Neuropeptide Galanin receptor Galanin Biology Islets of Langerhans Internal medicine Insulin Secretion medicine Animals Insulin Amino Acid Sequence Receptor Pancreatic hormone Pharmacology Pancreatic islets digestive oral and skin physiology Rats Inbred Strains Peptide Fragments Rats Endocrinology medicine.anatomical_structure nervous system Liberation Female Peptides hormones hormone substitutes and hormone antagonists |
| Zdroj: | European journal of pharmacology. 203(1) |
| ISSN: | 0014-2999 |
| Popis: | The 29-amino acid neuropeptide galanin occurs in intrapancreatic nerves and inhibits insulin secretion. To study the structure-activity relations of galanin, we examined the effects of pig and rat galanin, three galanin fragments (galanin-(1-11), galanin-(1-16) and rat galanin-(17-29) and four galanin analogues ([Ala2]pig galanin, [Ala2]rat galanin, [D-Trp2]rat galanin and [D-Trp2]galanin-(1-16] on glucose-stimulated insulin secretion from isolated rat islets. Pig and rat galanin and galanin-(1-11) equipotently inhibited glucose-stimulated (8.3 mM) insulin secretion at and above 10(-7) M (P less than 0.05), whereas galanin-(1-16), inhibited insulin secretion at 10(-6) M (P less than 0.01). In contrast, the C-terminal rat galanin-(17-29) and the galanin analogues did not influence insulin secretion. Thus, rat and pig galanin are equipotent in inhibiting glucose-stimulated insulin secretion from rat islets. The active site resides in the N-terminal part of the molecule. Furthermore, the binding of galanin to its receptor depends on structural characteristics governed by the N-terminal position and in particular by the Trp2 residue. |
| Databáze: | OpenAIRE |
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