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

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.

Author(s):  
Jos� Miguel Cerd�-Reverter ◽  
Gonzalo Mart�nez-Rodr�guez ◽  
Isabelle Anglade ◽  
Olivier Kah ◽  
Silvia Zanuy

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.


1998 ◽  
Vol 839 (1 TRENDS IN COM) ◽  
pp. 493-495 ◽  
Author(s):  
JOSE M. CERDA-REVERTER ◽  
GONZALO MARTINEZ RODRIGUEZ ◽  
SILVIA ZANUY ◽  
MANUEL CARRILLO ◽  
DAN LARHAMMAR

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