NEUROPEPTIDE-Y (NPY), AN ENDOGENOUS PRESYNAPTIC MODULATOR OF ADRENERGIC NEUROTRANSMISSION IN THE RAT VAS-DEFERENS - STRUCTURAL AND FUNCTIONAL-STUDIES

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dc.contributor.authorDONOSO, V
dc.contributor.authorSILVA, M
dc.contributor.authorSTPIERRE, S
dc.contributor.authorHUIDOBROTORO, JP
dc.date.accessioned2025-01-23T19:24:51Z
dc.date.available2025-01-23T19:24:51Z
dc.date.issued1988
dc.description.abstractThe role of neuropeptide tyrosine (NPY) on adrenergic neurotransmission was assessed in the rat vas deferens transmurally stimulated with square pulses of 0.15 or 15 Hz. Nanomoles of NPY inhibited the electrically-induced contractions on the prostatic half but not on the prostatic half but not on the epididymal end of the ductus. NPY was at least 200-fold more potent than norepinephrine or adenosine to produce an equivalent inhibition. Complete amino acid sequence of NPY is required for full agonist activity; deletion of tyrosine at the amino terminus, i.e., NPY fragment 2-36 was 3-fold less potent than the native peptide. NPY fragment 5-36, 11-36 or 25-36 were proportionally less potent than NPY. Avian pancreatic polypeptide was inactive. The presynaptic nature of the NPY acitivity was established measuring the outflow of 3H-norepinephrine from the adrenergic varicosities of the vas deferens electrically stimulated. In this assay, NPY was more potent than NPY 2-36 or NPY fragment 5-36. No inhibitory action of NPY was detected in K+ depolarized tissues. The inhibitory effect of NPY on the rat vas deferens neurotransmission was not significantly modified by yohimbine, theophylline or naloxone, indicating that the effect of NPY is not due to the activation of alpha2-adrenoceptors, adenosine receptors or opiate receptors respectively. Picrotoxin or apamin did not modify the inhibitory potency of NPY; verapamil or methoxyverapamil significantly reduced its potency. The inhibitory action of NPY is best explained through the activation of presynaptic NPY receptors that regulate norepinephrine release via a negative feedback mechanism. Structure activity studies give support to the notion of NPY receptors.
dc.fuente.origenWOS
dc.identifier.eissn1873-5169
dc.identifier.issn0196-9781
dc.identifier.urihttps://repositorio.uc.cl/handle/11534/99408
dc.identifier.wosidWOS:A1988P113200017
dc.issue.numero3
dc.language.isoen
dc.pagina.final553
dc.pagina.inicio545
dc.revistaPeptides
dc.rightsacceso restringido
dc.subject.ods03 Good Health and Well-being
dc.subject.ods02 Zero Hunger
dc.subject.odspa03 Salud y bienestar
dc.subject.odspa02 Hambre cero
dc.titleNEUROPEPTIDE-Y (NPY), AN ENDOGENOUS PRESYNAPTIC MODULATOR OF ADRENERGIC NEUROTRANSMISSION IN THE RAT VAS-DEFERENS - STRUCTURAL AND FUNCTIONAL-STUDIES
dc.typeartículo
dc.volumen9
sipa.indexWOS
sipa.trazabilidadWOS;2025-01-12
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