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Y 1 and Y 2 receptors for neuropeptide Y
Author(s) -
Sheikh Søren P.,
Håkanson Rolf,
Schwartz Thue W.
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)80223-6
Subject(s) - neuropeptide y receptor , receptor , neuropeptide , chemistry , microbiology and biotechnology , biology , biochemistry
By using monoiodinated radioligands of both intact neuropeptide Y (NPY) and of a long C‐terminal fragment, NPY 13–36 , two subtypes of binding sites, which differ in affinity and specificity, have been characterized. The Y 1 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 ( K d ) of a few nanomolar but does not bind NPY 13–36 . The Y 2 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 NPY 13–36 . 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.