Cloning of a neuropeptide Y/peptide YY receptor from the atlantic cod: the Yb receptor

Arvidsson, Ann-Kristin; Wraith, Amanda; Jönsson‐Rylander, Ann‐Cathrine; Larhammar, Dan

doi:10.1016/s0167-0115(98)00051-2

Cited by 26 publications

(11 citation statements)

References 20 publications

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“…Thus, the Y1 sites in any tissue are much more prone to be inactivated by a variety of agents than that of Y2 receptors. Previous studies have shown that the Y1 receptor is involved in the regulation of hyperphagia, vasoconstriction of vascular smooth muscles, proliferation of neuronal precursors, as well as potentiating noradrenaline-evoked vasoconstriction post-junctional and decreasing ethanol tolerance [39, 40]. Furthermore, the hY1 receptor is highly expressed in human primary breast cancer and Ewing’s sarcoma, suggesting that this receptor represents an important diagnostic and therapeutic target for these types of cancer [41, 42].…”

Section: The Characteristics Of Human Npy Receptorsmentioning

confidence: 99%

A Promising Therapeutic Target for Metabolic Diseases: Neuropeptide Y Receptors in Humans

et al. 2017

Cell Physiol Biochem

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Human neuropeptide Y (hNPY) is one of the most widely expressed neurotransmitters in the human central and peripheral nervous systems. It consists of 36 highly conserved amino acid residues, and was first isolated from the porcine hypothalamus in 1982. While it is the most recently discovered member of the pancreatic polypeptide family (which includes neuropeptide Y, gut-derived hormone peptide YY, and pancreatic polypeptide), NPY is the most abundant peptide found in the mammalian brain. In order to exert particular functions, NPY needs to bind to the NPY receptor to activate specific signaling pathways. NPY receptors belong to the class A or rhodopsin-like G-protein coupled receptor (GPCR) family and signal via cell-surface receptors. By binding to GPCRs, NPY plays a crucial role in various biological processes, including cortical excitability, stress response, food intake, circadian rhythms, and cardiovascular function. Abnormal regulation of NPY is involved in the development of a wide range of diseases, including obesity, hypertension, atherosclerosis, epilepsy, metabolic disorders, and many cancers. Thus far, five receptors have been cloned from mammals (Y1, Y2, Y4, Y5, and y6), but only four of these (hY1, hY2, hY4, and hY5) are functional in humans. In this review, we summarize the structural characteristics of human NPY receptors and their role in metabolic diseases.

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Section: The Characteristics Of Human Npy Receptorsmentioning

confidence: 99%

A Promising Therapeutic Target for Metabolic Diseases: Neuropeptide Y Receptors in Humans

et al. 2017

Cell Physiol Biochem

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“…Several other NPY receptors have been cloned in sub-mammalian species. For example, NPY zYa, NPY zYb and NPY zYc receptors from the zebra fish, 90,91 the NPY Yb receptor from Atlantic cod 92 and unclassified NPY receptors from Lymnaea stagnalis 93 and Drosophila melanogaster. 94 The NPY cod, NPY Yb=zYb and NPY zYc receptors display NPY Y 1 -like pharmacology while the NPY zYa subtype seems to have a pharmacological profile closer to the NPY Y 5 receptor.…”

Section: Npy Receptor Subtypesmentioning

confidence: 99%

Appetite suppression based on selective inhibition of NPY receptors

Chamorro

Della‐Zuana

et al. 2002

Int J Obes

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AIM:The aim of this review is to critically assess available evidence that blockade of the actions of NPY at one of the five NPY receptor subtypes represents an attractive new drug discovery target for the development of an appetite suppressant drug. RESULTS: Blockade of the central actions of NPY using anti-NPY antibodies, antisense oligodeoxynucleotides against NPY and NPY receptor antagonists results in a decrease in food intake in energy-deprived animals. These results appear to show that endogenous NPY plays a role in the control of appetite. The fact that NPY receptors exist as at least five different subtypes raises the possibility that the actions of endogenous NPY on food intake can be adequately dissociated from other effects of the peptide. Current drug discovery has produced a number of highly selective NPY receptor antagonists which have been used to establish the NPY Y 1 receptor subtype as the most critical in regulating short-term food intake. However, additional studies are now needed to more clearly define the relative contribution of NPY acting through the NPY Y 2 and NPY Y 5 receptors in the complex sequence of physiological and behavioral events that underlie the long-term control of appetite. CONCLUSIONS: Blockade of the NPY receptor may produce appetite-suppressing drugs. However, it is too early to state with certainty whether a single subtype selective drug used alone or a combination of NPY receptor selective antagonists used in combination will be necessary to adequately influence appetite regulation.

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“…Porcine NPY, p[Leu31,Pro34]NPY, the series of amino terminally truncated pig NPY peptides pNPY , pNPY 13236 , pNPY [18][19][20][21][22][23][24][25][26][27][28][29][30][31][32][33][34][35][36] , pNPY [25][26][27][28][29][30][31][32][33][34][35][36] , pNPY [26][27][28][29][30][31][32][33][34][35][36] , and bovine PP were from Bachem (King of Prussia, PA, USA); p[D-Trp32]NPY was from Peninsula Laboratories Inc. Lamprey peptides were synthesized as described below. BIBP3226 was kindly provided by K. Thomae GmBH, Biberach, Germany.…”

Section: Peptides and Nonpeptidic Antagonistsmentioning

confidence: 99%

A neuropeptide Y receptor Y1‐subfamily gene from an agnathan, the European river lamprey

Salaneck

Fredriksson

Larson

et al. 2001

European Journal of Biochemistry

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We report here the isolation and functional expression of a neuropeptide Y (NPY) receptor from the river lamprey, Lampetra fluviatilis. The receptor displays < 50% aminoacid sequence identity to all previously cloned Y1-subfamily receptors including Y1, Y4, and y6 and the teleost subtypes Ya, Yb and Yc. Phylogenetic analyses point to a closer relationship with Y4 and Ya/b/c suggesting that the lamprey receptor could possibly represent a pro-orthologue of some or all of those gnathostome receptors. Our results support the notion that the Y1 subfamily increased in number by genome or large-scale chromosome duplications, one of which may have taken place prior to the divergence of lampreys and gnathostomes whereas the second duplication probably occurred in the gnathostome lineage after this split. Functional expression of the lamprey receptor in a cell line facilitated specific binding of the three endogenous lamprey peptides NPY, peptide YY and peptide MY with picomolar affinities. Binding studies with a large panel of NPY analogues revealed indiscriminate binding properties similar to those of another nonselective Y1-subfamily receptor, zebrafish Ya. RT-PCR detected receptor mRNA in the central nervous system as well as in several peripheral organs suggesting diverse functions. This lamprey receptor is evolutionarily the most distant NPY receptor that clearly belongs to the Y1 subfamily as defined in mammals, which shows that subtypes Y2 and Y5 arose even earlier in evolution.Keywords: NPY; PYY; evolution; gene duplication; G-protein coupled receptor; Lamprey.Neuropeptide Y (NPY), peptide YY (PYY) and pancreatic polypeptide (PP) are closely related 36-amino-acid neuroendocrine peptides found in all tetrapods. NPY and PYY have also been found in nontetrapod gnathostomes as well as agnathans [1]. These peptides have a large number of physiological effects in the nervous system, the circulatory system and the gastrointestinal tract. NPY is most abundant in the nervous system and stimulates food intake, regulates blood pressure and influences release of pituitary peptides [2,3]. PYY and PP are found in the gastrointestinal tract and are released upon food intake. In nontetrapod vertebrates PYY is also present in the central nervous system (CNS) [4,5]. PY, a PYY-like peptide is only found in certain teleost fishes, and appears to have arisen from a fairly recent gene duplication [1,6]. In the river lamprey, Lampetra fluviatilis, the ancestral PYY gene appears to have undergone a separate gene duplication, resulting in peptide YY and peptide MY [4,7].The effects of the NPY family of peptides are relayed by a family of G-protein coupled receptors [8 -10]. Five receptors have been cloned in mammals; Y1, Y2, Y4, Y5 and y6, most of which have high affinities for NPY and PYY. Y4 is the only receptor for which PP has higher affinity than NPY or PYY. The y6 gene still lacks a physiological correlate, hence it is designated with a lower case 'y'. In humans and other primates, the y6 gene is a pseudogene. Sequence comparisons ...

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Cloning of a neuropeptide Y/peptide YY receptor from the atlantic cod: the Yb receptor

Cited by 26 publications

References 20 publications

A Promising Therapeutic Target for Metabolic Diseases: Neuropeptide Y Receptors in Humans

A Promising Therapeutic Target for Metabolic Diseases: Neuropeptide Y Receptors in Humans

Appetite suppression based on selective inhibition of NPY receptors

A neuropeptide Y receptor Y1‐subfamily gene from an agnathan, the European river lamprey

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