This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Copyright Permission Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by OKITA, M. Articles by KASUGA, M. Search for Related Content PubMed PubMed Citation Articles by OKITA, M. Articles by KASUGA, M.

Brain Peptide YY Receptors: Highly Conserved Characteristics throughout Vertebrate Evolution^*

Second Department of Internal Medicine, Kobe University School of Medicine Kobe, Japan

Address all correspondence and requests for reprints to: Dr. Akio Inui, Second Department of Internal Medicine, Kobe University School of Medicine, Kusunoki-cho 7-5-1, Chuo-ku, Kobe 650, Japan.

Abstract

We have shown previously that peptide YY (PYY) receptors are uniquely distributed in various mammalian brains and also have identified the receptor from porcine hippocampal membranes as a protein of 50,000 mol wt. To extend these observations, both the characteristics of PYY-receptor interaction and the structure of the receptor have been examined and compared with those of its sister peptide, neuropeptide Y (NPY), in the brains of various vertebrates including mammals (human, dog, guinea pig, rat, and mouse), birds (chicken), reptiles (snapping turtle), amphibians (bullfrog), and fish (yellowtail fish). The affinities and relative potencies of PYY as well as NPY receptors for pancreatic polypeptide (PP) family peptides were about the same in all species examined except for chickens. PYY and NPY bound to both the PYY and NPY receptors with high affinities, but porcine and avian PPs did not. In chicken brain, however, PYY, NPY, porcine PP, and avian PP all bound to the receptors with high affinity. Analysis of the equilibrium binding data for PYY receptors produced curvilinear Scatchard plots in all of the species, suggesting the existence of high and low affinity binding sites. Affinity cross-linking using disuccinimidyl suberate followed by electrophoretic analysis of ligandreceptor complexes characterized the molecular size of PYY and NPY receptors. [¹²⁵I]PYY was cross-linked to a protein of 50,000 mol wt without sulfhydryl-bonded subunits on mammalian hippocampal membranes. A receptor protein with the same mol wt was identified in other brain areas, including hypothalamus and pituitary. PYY receptors in other vertebrate brains were similar in size to those of mammalian species except in chicken brain, where a receptor protein of 67,000 mol wt was observed. In addition, we also have demonstrated that the NPY receptor is a monomeric 50,000 and 55,000 mol wt protein in mammalian and fish brains, respectively. These findings indicate that brain PYY and NPY receptors in most vertebrate species from fish to man are pharmacologically and structurally similar and have been well conserved over a period of evolution of 400 million yr. The divergence of the receptors observed in chicken brain may reflect some change in their function. (Endocrinology 129: 2512–2520, 1991)

Footnotes

^* This work was supported in part by Ministry of Education, Science, and Culture of Japan Grant-in-Aid for Special Project Research 01570642.

Received June 4, 1991.

This article has been cited by other articles:

				J. Y.-L. Yu, C.-H. Pon, H.-C. Ku, C.-T. Wang, and Y.-H. Kao A preprogalanin cDNA from the turtle pituitary and regulation of its gene expression Am J Physiol Regulatory Integrative Comp Physiol, April 1, 2007; 292(4): R1649 - R1656. [Abstract] [Full Text] [PDF]

				S. J. Wimalawansa and S. J. Wimalawansa Purification and Biochemical Characterization of Neuropeptide Y(2) Receptor J. Biol. Chem., August 4, 1995; 270(31): 18523 - 18530. [Abstract] [Full Text] [PDF]