Origins of the many NPY-family receptors in mammals

Larhammar, Dan; Wraith, Amanda; Berglund, Magnus; Holmberg, Sara K.S.; Lundell, Ingrid

doi:10.1016/s0196-9781(01)00331-x

Cited by 110 publications

(91 citation statements)

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“…Although D/E 6.30 is nearly 100% conserved among rhodopsin and monoamine GPCRs (10), it is not universally conserved among all class I GPCRs (i.e. MOR: 33, 41; gonadotrophin releasing hormone receptor (GnRHR): 42; angiotensin I receptor (AT 1 R): 43, 44), and it is not present in the Y1 receptor (45,46).…”

Section: Discussionmentioning

confidence: 99%

The Third Intracellular Loop Stabilizes the Inactive State of the Neuropeptide Y1 Receptor

Chee

Mörl

Lindner

et al. 2008

Journal of Biological Chemistry

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Section: Discussionmentioning

confidence: 99%

The Third Intracellular Loop Stabilizes the Inactive State of the Neuropeptide Y1 Receptor

Chee

Mörl

Lindner

et al. 2008

Journal of Biological Chemistry

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“…2). Mammalian Y4 has a more narrow profile favoring PP among the native ligands, but its preference for PP is clearly a secondary event as Y4 is evolutionarily older than PP and must originally have bound NPY and/or PYY [10].…”

Section: Discussionmentioning

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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“…22 The primary receptors specific for NPY have wide distribution in the body tissues and bind with substituted or truncated NPY peptides. [22][23][24] At least six distinct primary NPY receptors, namely YR1 to YR6, have been identified as members of the G protein-coupled receptor family. Interaction of NPY with its Y1 receptor (Y1R) and Y5 receptor (Y5R) activates the extracellular signalregulated kinases (Erk), which are the key intracellular transducers of mitogenic stimulus implicated in the signaling pathway leading to cell proliferation.…”

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confidence: 99%

Neuropeptide Y and Neuropeptide Y Y5 Receptor Interaction Restores Impaired Growth Potential of Aging Bone Marrow Stromal Cells

Igura

Haider

Ahmed

et al. 2011

Rejuvenation Research

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Physiological aging impairs the proliferative potential of bone marrow-derived stromal cells. We report here the pro-proliferative response and improved growth characteristics of the aging bone marrow cells subsequent to neuropeptide Y (NPY)/neuropeptide Y Y5 receptor (NPY Y5R) ligand-receptor interaction. Bone marrow cells were isolated from neonatal (2-3 weeks), young (8-12 weeks), and old (24-28 months) rats on the basis of their preferential adherence to plastic surface. After culturing the cells at initial seeding density of 1Â10 4 cells/cm 2 , we found that the proliferation potential of bone marrow cells declined with age. Real-time polymerase chain reaction (PCR) and Western blotting showed that bone marrow cells in different age groups constitutively expressed NPY and NPY receptor subtypes (Y1R, Y2R, and Y5R). However, NPY and Y5R expression increased by more than 130-fold and decreased by 28-fold, respectively, in old bone marrow cells as compared to young bone marrow cells. NPY (10 nM) stimulated the proliferation of all bone marrow cells age groups, and their proliferation was blocked by Y5R antagonist. However, the pro-proliferative effect of NPY on old bone marrow cells was weaker than other cell groups due to lower Y5R expression. Y5R gene transfection of old bone marrow cells with subsequent NPY 3-36 (10 nM) treatment significantly increased proliferation of old bone marrow cells (>56%) as compared to green fluorescence protein-transfected control old bone marrow cells. Stimulation of old bone marrow cells by NPY treatment rejuvenated the growth characteristics of aging bone marrow cells as a result of Y5R overexpression.

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Origins of the many NPY-family receptors in mammals

Cited by 110 publications

References 100 publications

The Third Intracellular Loop Stabilizes the Inactive State of the Neuropeptide Y1 Receptor

The Third Intracellular Loop Stabilizes the Inactive State of the Neuropeptide Y1 Receptor

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

Neuropeptide Y and Neuropeptide Y Y5 Receptor Interaction Restores Impaired Growth Potential of Aging Bone Marrow Stromal Cells

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