A comparison of actions of neuropeptide Y (NPY) agonists and antagonists at NPY Y1 and Y2 receptors in anaesthetized rats
Autor: | Erica K. Potter, M.J Moriarty, Margaret A Smith-White |
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Rok vydání: | 1998 |
Předmět: |
Agonist
medicine.medical_specialty medicine.drug_class Recombinant Fusion Proteins Peptide Biology Pancreatic Polypeptide Peptides Cyclic Cellular and Molecular Neuroscience Endocrinology Salmon In vivo Internal medicine mental disorders medicine Animals Humans Pancreatic polypeptide Anesthesia Neuropeptide Y Protein Precursors Rats Wistar Receptor Pancreatic hormone chemistry.chemical_classification Dose-Response Relationship Drug Endocrine and Autonomic Systems Heart Vagus Nerve General Medicine Neuropeptide Y receptor Peptide Fragments humanities Rats Receptors Neuropeptide Y Neurology chemistry Peptide YY Synapses Female |
Zdroj: | Neuropeptides. 32:109-118 |
ISSN: | 0143-4179 |
DOI: | 10.1016/s0143-4179(98)90025-7 |
Popis: | The pancreatic polypeptide family includes three members, neuropeptide Y (NPY), peptide YY (PYY) and pancreatic polypeptide (PP), with sequence homology between members and species varying from approximately 50 to 80%. Some of these peptides were compared in the mammalian cardiovascular system for activity mediated by actions on pre- (Y 2 ) and post-junctional (Y 1 ) NPY receptors. NPY and PYY, with sequence homology of 67% have similar actions on Y 1 and Y 2 receptors. Rat pancreatic polypeptide (rPP) with sequence homology of approximately 50% is inactive at both. This study reports that the chimeric peptide, hPP 1–11 /NPY 12–36 and the truncated peptide NPY 2–36 show similar activity to NPY mediated through both receptor types in vivo, while salmon PYY (sPYY), with 81% homology to NPY, has improved potency at both receptor subtypes. NPY 3–36 has equal activity with NPY on actions mediated through Y 2 receptors, but significantly reduced activity mediated through Y 1 receptors. Two NPY antagonists were also examined: PYX2 was inactive in vivo and 1229U91 showed potent, long-lasting activity on Y 1 receptor-mediated effects. |
Databáze: | OpenAIRE |
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