Pancreatic polypeptide, peptide YY, and neuropeptide Y family of regulatory peptides

1985 ◽  
Vol 88 (3) ◽  
pp. 838-841 ◽  
Author(s):  
Travis E. Solomon
2002 ◽  
Vol 28 (3) ◽  
pp. 225-235 ◽  
Author(s):  
I Lundell ◽  
T Boswell ◽  
D Larhammar

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, (125)I-labelled porcine (p) PYY bound with a K(d) of 20 pM. In competition with (125)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.


Life ◽  
2021 ◽  
Vol 11 (6) ◽  
pp. 547
Author(s):  
Daniel Assan ◽  
Umar Farouk Mustapha ◽  
Huapu Chen ◽  
Zhiyuan Li ◽  
Yuhao Peng ◽  
...  

Neuropeptide Y family (NPY) is a potent orexigenic peptide and pancreatic polypeptide family comprising neuropeptide Y (Npy), peptide YYa (Pyya), and peptide YYb (Pyyb), which was previously known as peptide Y (PY), and tetrapod pancreatic polypeptide (PP), but has not been exhaustively documented in fish. Nonetheless, Npy and Pyy to date have been the key focus of countless research studies categorizing their copious characteristics in the body, which, among other things, include the mechanism of feeding behavior, cortical neural activity, heart activity, and the regulation of emotions in teleost. In this review, we focused on the role of neuropeptide Y gene (Npy) and peptide YY gene (Pyy) in teleost food intake. Feeding is essential in fish to ensure growth and perpetuation, being indispensable in the aquaculture settings where growth is prioritized. Therefore, a better understanding of the roles of these genes in food intake in teleost could help determine their feeding regime, regulation, growth, and development, which will possibly be fundamental in fish culture.


1983 ◽  
Vol 29 (8) ◽  
pp. 1553-1554 ◽  
Author(s):  
M M O'Hare ◽  
M H Chen ◽  
K Tatemoto ◽  
K D Buchanan ◽  
S N Joffe ◽  
...  

1989 ◽  
Vol 257 (2) ◽  
pp. R383-R387 ◽  
Author(s):  
J. L. Miner ◽  
M. A. Della-Fera ◽  
J. A. Paterson ◽  
C. A. Baile

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.


Genomics ◽  
2000 ◽  
Vol 64 (3) ◽  
pp. 318-323 ◽  
Author(s):  
Michelle Couzens ◽  
Marjorie Liu ◽  
Camilla Tüchler ◽  
Barbara Kofler ◽  
Claudia Nessler-Menardi ◽  
...  

2017 ◽  
Vol 45 (1) ◽  
pp. 88-107 ◽  
Author(s):  
Min Yi ◽  
Hekai Li ◽  
Zhiye Wu ◽  
Jianyun Yan ◽  
Qicai Liu ◽  
...  

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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