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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Sheikh SP,Håkanson R,Schwartz TWdoi
10.1016/0014-5793(89)80223-6subject
Has Abstractpub_date
1989-03-13 00:00:00pages
209-14issue
1-2eissn
0014-5793issn
1873-3468pii
0014-5793(89)80223-6journal_volume
245pub_type
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