Receptor binding profiles of NPY analogues and fragments in different tissues and cell lines

• Published in: Peptides (New York, N.Y. : 1980) N.Y. : 1980), 1995, Vol.16 (8), p.1389-1394
• Main Authors: Wieland, H.A., Willim, K., Doods, H.N.
• Format: Article
• Language: English
• Subjects: Adipose Tissue - metabolism; Animals; Cell Line; Cerebral Cortex - metabolism; Dogs; Hippocampus - metabolism; History of medicine; History, 15th Century; Humans; In Vitro Techniques; Kidney - metabolism; Kinetics; Male; Neuropeptide Y (NPY); Neuropeptide Y - analogs & derivatives; Neuropeptide Y - chemistry; Neuropeptide Y - metabolism; NPY receptor subtypes; Peptide Fragments - chemistry; Peptide Fragments - metabolism; Rabbits; Rats; Receptors, Neuropeptide Y - metabolism; Species selectivity; Species Specificity; Y 1, Y 2 subtype selectivity
• ISSN: 0196-9781; 1873-5169
• DOI: 10.1016/0196-9781(95)02028-4

To investigate receptor selectivity and possible species selectivity of a number of NPY analogues and fragments, receptor binding studies were performed using cell lines and membranes of several species. NPY displays 4–25-fold higher affinity for the Y 2 receptor than for the Y 1 receptor. The affinity of [Leu 31,Pro 34]NPY is 7–60-fold higher for the Y 1 receptor when compared with the Y 2 subtype. Species selectivity within the Y 2 receptors is demonstrated by PYY(3–36), NPY(2–36), NPY(22–36), and NPY(26–36). It is shown that NPY(22–36) is species selective for the human Y 2 subtype ( K i of 0.3 n M) compared with the rabbit and rat Y 2 receptor ( K i of 2 and 10 n M, respectively). PYY(3–36) displays highest affinity for the human and rabbit Y 2 subtype ( K i of 0.03 and 0.17 n M). The screening of NPY analogues and fragments revealed that highest affinity for the human Y 2 receptor is shown by NPY(2–36) and PYY(3–36). In addition, PYY(3–36) and NPY(2–36) are not only subtype selective, but also species selective.