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Receptors on phaeochromocytoma cells for two members of the PP‐fold family — NPY and PP
Author(s) -
Schwartz Thue W.,
Sheikh Søren P.,
O'Hare Mairead M.T.
Publication year - 1987
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(87)81159-6
Subject(s) - fold (higher order function) , receptor , neuropeptide y receptor , chemistry , biochemistry , computer science , neuropeptide , programming language
Pancreatic polypeptide (PP) and neuropeptide Y (NPY) belong to a family of regulatory peptides which hold a distinct tertiary structure, the PP‐fold, even in dilute aqueous solution. High‐affinity receptors, specific for both PP and NPY, are described on the rat phaeochromocytoma cell line, PC‐12. The binding of [ 125 I‐Tyr 36 ]PP to PC‐12 cells was inhibited by concentrations of unlabeled PP which correspond to physiological concentrations of the hormone, 10 −11 ‐10 −9 mol/1. The affinity of the receptor for the neuropeptide, NPY, was 10 2 ‐times lower than that of the PP receptor. C‐terminal fragments of both PP (PP 24–36 ) and NPY (NPY 13–36 ) were between 10 2 ‐ and 10 3 ‐times less potent in displacing the radiolabeled 36‐amino‐acid peptides from their respective receptors. It is concluded that PC‐12 cells are suited for structure‐function studies of the PP‐fold peptides and studies on the cellular events following cellular binding of PP‐fold peptides.