Cloning and characterization of a novel receptor to pancreatic polypeptide, a member of the neuropeptide Y receptor family

Gregor, Paul; Millham, Michele L.; Feng, Yun; DeCarr, Lynn B.; McCaleb, Michael L.; Cornfield, Linda J.

doi:10.1016/0014-5793(96)00067-1

Cited by 94 publications

(44 citation statements)

References 22 publications

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“…The first receptor to be cloned was the Y1 receptor (Y1-R) (Eva et al 1990(Eva et al , 1992Herzog et al 1992;Larhammar et al 1992). Subsequently, the Y2 receptor (Gerald et al 1995;Rose et al 1995;Gehlert et al 1996;Nakamura et al 1996), the Y4/PP1 receptor (Bard et al 1995;Lundell et al 1995;Gregor et al 1996b;Yan et al 1996), the Y5 receptor (Gerald et al 1996;Hu et al 1996), and the Y5/PP2/Y2b receptor (Gregor et al 1996a;Matsumoto et al 1996;Weinberg et al 1996) were cloned. These receptors show low sequence similarity and differ in binding properties and tissue distribution.…”

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confidence: 99%

Immunocytochemical Localization of the NPY/PYY Y1 Receptor in Enteric Neurons, Endothelial Cells, and Endocrine-like Cells of the Rat Intestinal Tract

Jackerott

Larsson

1997

J Histochem Cytochem.

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SUMMARY Neuropeptide Y (NPY) and peptide YY (PYY) are structurally related peptides that are considered to mediate inhibitory actions on gastrointestinal motility, secretion, and blood flow. Several receptor subtypes for these peptides have been identified and the Y1, Y2, Y4/PP1, Y5, and Y5/PP2/Y2b receptors have been cloned. In this article we report the immunocytochemical localization of the Y1 receptor to myenteric and submucosal nerve cell bodies, endothelial cells, and scattered endocrine-like cells of rat intestinal tract. Moreover, double immunofluorescence demonstrates that subpopulations of the Y1 receptorpositive nerve cell bodies are immunopositive for NPY, vasoactive intestinal polypeptide, and nitric oxide synthase. In part, such co-localizations were made possible by use of peroxidase-mediated deposition of tyramide, which permitted use of antisera derived from the same species. Our observations suggest the existence of multiple neuronal, endothelial, and endocrine target sites for NPY and PYY and that some of the actions of these regulatory peptides can be mediated by vasoactive intestinal peptide and nitric oxide synthase.

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confidence: 99%

Immunocytochemical Localization of the NPY/PYY Y1 Receptor in Enteric Neurons, Endothelial Cells, and Endocrine-like Cells of the Rat Intestinal Tract

Jackerott

Larsson

1997

J Histochem Cytochem.

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“…Because PYY has very low affinity for rat Y4, iodinated pancreatic polypeptide was used as a radioligand in its characterisation. The Y4 receptor has been extensively studied by different groups using both iodinated PYY, pancreatic polypeptide and LP-NPY (Gehlert et al 1996b, c, 1997, Gregor et al 1996, Voisin et al 2000, Parker et al 2001. Depending on the radioligand used, different affinities have been reported for the ligands in the various studies.…”

Section: Discussionmentioning

confidence: 99%

“…In mammals, the affinity of pancreatic polypeptide for this receptor is much greater than the affinities of NPY and PYY (Bard et al 1995, Lundell et al 1995, 1996, Gregor et al 1996. The rat receptor is even more selective for pancreatic polypeptide than are the human and guinea pig receptors (Lundell et al 1996, Eriksson et al 1998.…”

Section: Introductionmentioning

confidence: 99%

“…The integrity of Figure 1 Amino acid sequence alignment made using the Lasergene DNASTAR Megalign software. The chY4 receptor serves as master sequence in alignment with human (Lundell et al 1995), guinea pig (Eriksson et al 1998), pig , rat (Lundell et al 1996) and mouse (Gregor et al 1996) Y4 receptors. Dashes represent gaps introduced to optimise alignment.…”

Section: Localisation Of Receptor Mrna By Rt-pcr and In Situ Hybridismentioning

confidence: 99%

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Chicken neuropeptide Y-family receptor Y4: a receptor with equal affinity for pancreatic polypeptide, neuropeptide Y and peptide YY

Lundell

Boswell²,

Larhammar³

2002

Journal of Molecular Endocrinology

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Within the neuropeptide Y (NPY) family of peptides, pancreatic polypeptide is the most divergent across species. It differs in 20 of 36 positions between human and chicken. In mammals, it binds primarily to the Y4 receptor, to which NPY and peptide YY (PYY) bind with lower affinities. Because of these large sequence differences in pancreatic polypeptide, we decided to characterise the chicken Y4 receptor. We report here that Y4 displays the least sequence conservation among the Y-family receptors, with only 57-60% overall amino acid identity between chicken and mammals, compared with 64-83% for the Y1, Y2 and Y5 receptors. After expression of the chicken Y4 receptor in COS-7 cells, I-pPYY, chicken pancreatic polypeptide bound with high affinity at 140 pM. Interestingly, chicken PYY bound with even greater affinity at 68 pM. The affinity of NPY, 160 pM, was similar to that of pancreatic polypeptide. Chicken Y4 is less sensitive than is mammalian Y4 to truncation of the amino terminus of the NPY molecule. RT-PCR revealed expression in several peripheral organs, including adipose tissue and oviduct. In brain, Y4 mRNA was detected in the brainstem, cerebellum and hippocampus. In situ hybridisation to brain sections showed expression in the dorsal motor nucleus of the vagus in the brainstem. Thus the chicken Y4 receptor is less selective and anatomically more widespread than that in mammals, probably reflecting the original properties of the Y4 receptor.

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“…Y1, Y2, Y3, Y1-like, as well as a PP receptor (4,5,(11)(12)(13)(14)(15)(16)(17)(18)(19)(20)(21). Recently, we and others have reported cloning and characterization of a PP receptor from human, rat, and mouse, termed Y4 or PP1 (15,16,18,19). The Y4/PP1 receptor has subnanomolar affinity to PP and nanomolar affinity to PYY and NPY, raising the possibility that it may be shared by all three pancreatic polypeptides.…”

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confidence: 99%

Molecular Characterization of a Second Mouse Pancreatic Polypeptide Receptor and Its Inactivated Human Homologue

Gregor

Feng

DeCarr

et al. 1996

Journal of Biological Chemistry

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161

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NPY, which is similar to that of the mouse Y4/PP1 receptor. Mouse PP2 transcripts were not detectable by Northern analysis in adult tissues and in 11-, 15-, and 17-day-old embryos. However, a 9.8-kb PP2 transcript was detectable in 7-day-old mouse embryo, i.e. prior to the organogenesis of pancreas and the onset of PP production. We have also cloned the human homologue of PP2, which is a single copy gene and maps to human chromosome 5q31. Surprisingly, the human PP2 cDNAs and gene sequences display a single base deletion in the coding region. This frameshifting mutation predicts a truncated receptor of 290 amino acids without TM7. Transfection of COS-7 cells with several different human PP2 expression constructs failed to confirm any specific binding of 125 I-PP, 125 I-PYY, or 125 I-NPY to cell membranes. These data suggest that in mouse there are at least two PP receptors, Y4/PP1 and PP2, whereas in humans, PP2 is either functionally inactive or it has acquired a PP-independent function.

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Cloning and characterization of a novel receptor to pancreatic polypeptide, a member of the neuropeptide Y receptor family

Cited by 94 publications

References 22 publications

Immunocytochemical Localization of the NPY/PYY Y1 Receptor in Enteric Neurons, Endothelial Cells, and Endocrine-like Cells of the Rat Intestinal Tract

Immunocytochemical Localization of the NPY/PYY Y1 Receptor in Enteric Neurons, Endothelial Cells, and Endocrine-like Cells of the Rat Intestinal Tract

Chicken neuropeptide Y-family receptor Y4: a receptor with equal affinity for pancreatic polypeptide, neuropeptide Y and peptide YY

Molecular Characterization of a Second Mouse Pancreatic Polypeptide Receptor and Its Inactivated Human Homologue

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