Pancreatic Polypeptide Family: Pancreatic Polypeptide, Neuropeptide Y, and Peptide YY

2011 ◽  
Author(s):  
Ian L. Taylor
Keyword(s):  
Neuropeptide Y ◽  
Pancreatic Polypeptide ◽  
Peptide Yy

Lack of cross reactivity of peptide YY (PYY) and neuropeptide Y (NPY) with antibodies to pancreatic polypeptide (PP) in radioimmunoassay.

1983 ◽  
Vol 29 (8) ◽  
pp. 1553-1554 ◽  
Author(s):  
M M O'Hare ◽  
M H Chen ◽  
K Tatemoto ◽  
K D Buchanan ◽  
S N Joffe ◽  
...  
Keyword(s):  
Neuropeptide Y ◽  
Pancreatic Polypeptide ◽  
Peptide Yy ◽  
Cross Reactivity

Lateral cerebroventricular injection of neuropeptide Y stimulates feeding in sheep

1989 ◽  
Vol 257 (2) ◽  
pp. R383-R387 ◽  
Author(s):  
J. L. Miner ◽  
M. A. Della-Fera ◽  
J. A. Paterson ◽  
C. A. Baile
Keyword(s):  
Neuropeptide Y ◽  
Water Intake ◽  
Pancreatic Polypeptide ◽  
Feed Intake ◽  
Lateral Ventricle ◽  
Bolus Injection ◽  
Peptide Yy ◽  
Consummatory Behavior ◽  
Central Regulation ◽  
Human Pancreatic Polypeptide

We compared the effects of neuropeptide Y (NPY) injected into the lateral ventricle (LV) and periphery (ip in rats; iv in sheep) on feed and water intake. In sated rats, a bolus injection of 1.18 or 2.35 nmol of NPY administered LV, but not ip, increased (P less than 0.05) feed intake on average of 809% within 30 min of injection. In sated sheep, an LV bolus injection of 2.35 nmol of NPY increased feed intake by 154% within 30 min. Similar doses of human pancreatic polypeptide and peptide YY were less orexigenic than NPY in sheep. After 24 h, cumulative feed intakes were similar among control and peptide treatments. Intravenous injection of 2.35 nmol NPY did not increase feed intake in sheep. Water intake was stimulated (P less than 0.05) by NPY (LV injection) in both the presence and absence of feed. We propose that NPY is involved in the central regulation of consummatory behavior in sheep.

Peptide YY-2 (PYY2) and Pancreatic Polypeptide-2 (PPY2): Species-Specific Evolution of Novel Members of the Neuropeptide Y Gene Family

Genomics ◽  
2000 ◽  
Vol 64 (3) ◽  
pp. 318-323 ◽  
Author(s):  
Michelle Couzens ◽  
Marjorie Liu ◽  
Camilla Tüchler ◽  
Barbara Kofler ◽  
Claudia Nessler-Menardi ◽  
...  
Keyword(s):  
Neuropeptide Y ◽  
Gene Family ◽  
Pancreatic Polypeptide ◽  
Peptide Yy ◽  
Species Specific

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

2017 ◽  
Vol 45 (1) ◽  
pp. 88-107 ◽  
Author(s):  
Min Yi ◽  
Hekai Li ◽  
Zhiye Wu ◽  
Jianyun Yan ◽  
Qicai Liu ◽  
...  
Keyword(s):  
Neuropeptide Y ◽  
Pancreatic Polypeptide ◽  
Metabolic Diseases ◽  
Peptide Yy ◽  
Cortical Excitability ◽  
Structural Characteristics ◽  
Mammalian Brain ◽  
Surface Receptors ◽  
Wide Range ◽  
Npy Receptors

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.

Spinal modulation of duodenal and colonic motility and arterial pressure by neuropeptide Y, neuropeptide Y fragment 13–36, peptide YY, and pancreatic polypeptide in rats: involvement of the cholinergic nervous system

1993 ◽  
Vol 71 (2) ◽  
pp. 112-119 ◽  
Author(s):  
S. A. Wager-Pagé ◽  
E. Raizada ◽  
W. L. Veale ◽  
J. S. Davison
Keyword(s):  
Spinal Cord ◽  
Arterial Pressure ◽  
Neuropeptide Y ◽  
Pancreatic Polypeptide ◽  
Peptide Yy ◽  
Colonic Motility ◽  
Intraluminal Pressure ◽  
Thoracic Spinal Cord ◽  
Fold Family ◽  
Thoracic Spinal

The pancreatic polypeptide-fold (PP-fold) peptides, peptide YY (PYY) and pancreatic polypeptide (PP) (200 pmol), increased duodenal intraluminal pressure following intrathecal (IT) administration into the thoracic (T8–T10) spinal cord of urethane-anesthetized rats. Neuropeptide Y (NPY), PPY, and PP (IT) increased colonic intraluminal pressure of rats. The excitatory effects of the PP-fold peptides, NPY and PYY, were accompanied by increases in mean arterial pressure (MAP) during the same time period followed by a decrease to hypotensive levels. There were no further alterations of duodenal or colonic pressure in rats during the hypotensive period. The effect of PP (IT) on MAP was characterized by a pattern of hypotension frequently followed by a hypertensive period. The modulation of duodenal and colonic pressure does not differ between the members of the PP-fold family of peptides; however, the effects of the different members of the PP-fold family of peptides on MAP were varied. The Y2 receptor ligand, NPY (13–36) (200 pmol) (IT), did not alter duodenal and colonic pressure or MAP in rats. Therefore, the effects of PYY and NPY in the thoracic spinal cord on duodenal and colonic motility may be mediated via Y1 (postjunctional) receptors. Atropine, a muscarinic antagonist, attenuated NPY's (IT) excitatory effect on colonic pressure but did not alter the MAP response to this peptide. Atropine did not modify PYY's (IT) regulation of duodenal and colonic intraluminal pressure. However, atropine did attenuate PPY's inhibitory effect on MAP. The modulatory effects of PP (IT) on colonic pressure and MAP were attenuated by atropine, suggesting that the cholinergic system may be mediating the effects of this peptide. These observations provide further evidence that the modulation of gastrointestinal motility by PYY, PP, and NPY in the thoracic spinal cord is through different mechanisms.Key words: PP-fold peptides, duodenum, colon, atropine.

cNeuropeptide Y family of peptides: Structure, anatomical expression, function, and molecular evolution

2000 ◽  
Vol 78 (3) ◽  
pp. 371-392 ◽  
Author(s):  
José Miguel Cerdá-Reverter ◽  
Dan Larhammar
Keyword(s):  
Neuropeptide Y ◽  
Pancreatic Polypeptide ◽  
Peptide Yy ◽  
Sea Bass ◽  
Gene Families ◽  
Duplication Event ◽  
Duplication Events ◽  
Independent Duplication ◽  
Peptide Gene ◽  
Pancreatic Peptide

Evolutionary relationships between neuroendocrine peptides are often difficult to resolve across divergent phyla due to independent duplication events in different lineages. Thanks to peptide purification and molecular cloning in many different species, the situation is beginning to clear for the neuropeptide Y (NPY) family, which also includes peptide YY (PYY), the tetrapod pancreatic polypeptide (PP) and the fish pancreatic peptide Y (PY). It has long been assumed that the first duplication to occur in vertebrate evolution generated NPY and PYY, as both of these are found in all gnathostomes as well as lamprey. Evidence from other gene families show that this duplication was probably a chromosome duplication event. The origin of a second PYY peptide found in lamprey remains to be explained. Our recent cloning of NPY, PYY and PY in the sea bass proves that fish PY is a separate gene product. We favour the hypothesis that PY is a duplicate of the PYY gene and that it may have occurred late in fish evolution, as PY has so far only been found in acanthomorph fishes. Thus, this duplication seems to be independent of the one that generate PP from PYY in tetrapods, although both tetrapod PP and fish PY are expressed in the pancreas. Studies in the sea bass and other fish show that PY, in contrast to PP, is expressed in the nervous system. We review the literature on the distribution and functional aspects of the various NPY-family peptides in vertebrates. Key words: neuropeptide Y, pancreatic polypeptide, fish pancreatic peptide, gene duplication.

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