Characterization of NPY receptor subtypes Y2 and Y7 in rainbow trout Oncorhynchus mykiss

Tomas A. Larsson; Earl T. Larson; Robert Fredriksson; J. Michael Conlon; Dan Larhammar

doi:10.1016/j.peptides.2005.10.008

Characterization of NPY receptor subtypes Y2 and Y7 in rainbow trout Oncorhynchus mykiss

Tomas A. Larsson
, Earl T. Larson
, Robert Fredriksson
, J. Michael Conlon
, Dan Larhammar

School of Biomedical Sciences

Uppsala University

Research output: Contribution to journal › Article › peer-review

31 Citations (Scopus)

Abstract

We report the cloning and pharmacological characterization of two neuropeptide Y (NPY) receptor subtypes, Y2 and Y7, in rainbow trout (Oncorhynchus mykiss). These subtypes are approximately 50% identical to each other and belong to the Y2 subfamily of NPY receptors. The binding properties of the receptors were investigated after expression in human HEK-293 EBNA cells. Both receptors bound the three zebrafish peptides NPY, PYYa, and PYYb, as well as porcine NPY and PYY, with affinities in the nanomolar range that are similar to mammalian Y2. The affinity of the truncated porcine NPY fragments, NPY 13-36 and NPY 18-36 was markedly lower compared to mammalian and chicken Y2. This suggests that mammalian and chicken Y2 are unique among NPY receptors in their ability to bind truncated peptide fragments. The antagonist BIIE0246, developed for mammalian Y2, did not bind either of the two rainbow trout receptors. Our results support the proposed expansion of this gene family by duplications before the gnathostome radiation. They also reveal appreciable differences in the repertoire and characteristics of NPY receptors between fish and tetrapods stressing the importance of lineage-specific gene loss as well as sequence divergence after duplication.

Original language	English
Pages (from-to)	1320-1327
Number of pages	8
Journal	Peptides
Volume	27
Issue number	6
DOIs	https://doi.org/10.1016/j.peptides.2005.10.008
Publication status	Published (in print/issue) - Jun 2006

Funding

We thank Theresa Larsdotter and Tatjana Haitina for technical help, Ingrid Lundell and Paula Sjödin for advice on the pharmacological analyses, Gunnar Jeserich (University of Osnabrück, Germany) for kindly providing the rainbow trout genomic phage library, and Svante Winberg and Tobias Backström for dissection of rainbow trout organs for mRNA extraction. This work was supported by grants from the Swedish Natural Science Research Council, Formas (The Swedish Research Council for Environment, Agricultural Sciences and Spatial Planning), the National Network for the Neurosciences (NNN) of the Swedish Strategic Funds (SSF), and Carl Trygger's Foundation.

Keywords

G-protein coupled receptor
NPY
Rainbow trout
Y2
Y7

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10.1016/j.peptides.2005.10.008

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title = "Characterization of NPY receptor subtypes Y2 and Y7 in rainbow trout Oncorhynchus mykiss",

abstract = "We report the cloning and pharmacological characterization of two neuropeptide Y (NPY) receptor subtypes, Y2 and Y7, in rainbow trout (Oncorhynchus mykiss). These subtypes are approximately 50\% identical to each other and belong to the Y2 subfamily of NPY receptors. The binding properties of the receptors were investigated after expression in human HEK-293 EBNA cells. Both receptors bound the three zebrafish peptides NPY, PYYa, and PYYb, as well as porcine NPY and PYY, with affinities in the nanomolar range that are similar to mammalian Y2. The affinity of the truncated porcine NPY fragments, NPY 13-36 and NPY 18-36 was markedly lower compared to mammalian and chicken Y2. This suggests that mammalian and chicken Y2 are unique among NPY receptors in their ability to bind truncated peptide fragments. The antagonist BIIE0246, developed for mammalian Y2, did not bind either of the two rainbow trout receptors. Our results support the proposed expansion of this gene family by duplications before the gnathostome radiation. They also reveal appreciable differences in the repertoire and characteristics of NPY receptors between fish and tetrapods stressing the importance of lineage-specific gene loss as well as sequence divergence after duplication.",

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AB - We report the cloning and pharmacological characterization of two neuropeptide Y (NPY) receptor subtypes, Y2 and Y7, in rainbow trout (Oncorhynchus mykiss). These subtypes are approximately 50% identical to each other and belong to the Y2 subfamily of NPY receptors. The binding properties of the receptors were investigated after expression in human HEK-293 EBNA cells. Both receptors bound the three zebrafish peptides NPY, PYYa, and PYYb, as well as porcine NPY and PYY, with affinities in the nanomolar range that are similar to mammalian Y2. The affinity of the truncated porcine NPY fragments, NPY 13-36 and NPY 18-36 was markedly lower compared to mammalian and chicken Y2. This suggests that mammalian and chicken Y2 are unique among NPY receptors in their ability to bind truncated peptide fragments. The antagonist BIIE0246, developed for mammalian Y2, did not bind either of the two rainbow trout receptors. Our results support the proposed expansion of this gene family by duplications before the gnathostome radiation. They also reveal appreciable differences in the repertoire and characteristics of NPY receptors between fish and tetrapods stressing the importance of lineage-specific gene loss as well as sequence divergence after duplication.

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Characterization of NPY receptor subtypes Y2 and Y7 in rainbow trout Oncorhynchus mykiss

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