| Autor: |
M C, Michel, W, Gaida, A G, Beck-Sickinger, H A, Wieland, H, Doods, H, Dürr, G, Jung, G, Schnorrenberg |
| Rok vydání: |
1992 |
| Předmět: |
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| Zdroj: |
Molecular pharmacology. 42(4) |
| ISSN: |
0026-895X |
| Popis: |
Previous attempts to classify neuropeptide Y receptor subtypes suffered from relying only on carboxyl-terminal analogs and fragments of neuropeptide Y. We have tested the potency and affinity of chemically different compounds, i.e., centrally truncated analogs of neuropeptide Y, in three Y1-like (Ca2+ mobilization in HEL cells, blood pressure increases in pithed rats, and 125I-neuropeptide Y binding in SK-N-MC cells) and two Y2-like (125I-neuropeptide Y binding to rabbit kidney membranes and presynaptic inhibition in rat vas deferens) model systems of neuropeptide Y receptors. Our data confirm the concept of two major subclasses of neuropeptide Y receptors, with some centrally truncated neuropeptide Y analogs having high affinity for Y2-like and low affinity for Y1-like neuropeptide Y receptors. Some of the truncated neuropeptide Y analogs are antagonists at Y1-like receptors and (possibly partial) agonists at Y2-like receptors. Our data also indicate that amino acid residues distal from the amino- and carboxyl-terminal ends of the peptide may subtype-selectively affect affinity and intrinsic efficacy of peptide agonists at neuropeptide Y receptors. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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