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FEBS Lett. 1989 Mar 13;245(1-2):209-14.

Y1 and Y2 receptors for neuropeptide Y.

Author information

1
Laboratory for Molecular Endocrinology, Rigshospitalet, Copenhagen, Denmark.

Abstract

By using monoiodinated radioligands of both intact neuropeptide Y (NPY) and of a long C-terminal fragment, NPY13-36, two subtypes of binding sites, which differ in affinity and specificity, have been characterized. The Y1 type of binding site, characterized on a human neuroblastoma cell line, MC-IXC, and a rat pheochromocytoma cell line, PC-12, binds NPY with a dissociation constant (Kd) of a few nanomolar but does not bind NPY13-36. The Y2 type of binding site, characterized on porcine hippocampal membranes and on another human neuroblastoma cell line, SMS-MSN, is of higher affinity and binds both NPY and NPY13-36. None of the binding sites distinguish between NPY and the homologous peptide YY (PYY). It is concluded that NPY/PYY-binding sites occur in two subtypes which may represent two types of physiological receptors.

PMID:
2538360
DOI:
10.1016/0014-5793(89)80223-6
[Indexed for MEDLINE]
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