NPB

Official Full Name

neuropeptide B

Organism

Homo sapiens

Gene ID

256933

Background

This gene encodes a member of the neuropeptide B/W family of proteins and preproprotein that is proteolytically processed to generate multiple protein products. The encoded products include neuropeptide B-23 and a C-terminally extended form, neuropeptide B-29, which are characterized by an N-terminal brominated tryptophan amino acid. Both of the encoded peptides bind with higher affinity to neuropeptide B/W (NPB/W) receptor 1 compared to the related NPB/W receptor 2. These peptides may regulate feeding, pain perception, and stress in rodents. [provided by RefSeq, Jul 2015]

Synonyms

L7; PPL7; PPNPB

Cat.No.	Product Name	Price
CSC-DC010537	Panoply™ Human NPB Knockdown Stable Cell Line	Inquiry
CSC-SC010537	Panoply™ Human NPB Over-expressing Stable Cell Line	Inquiry

Cat.No.	Product Name	Price
AD10927Z	Human NPB adenoviral particles	Inquiry
LV19767L	human NPB (NM_148896) lentivirus particles	Inquiry

Cat.No.	Product Name	Price
SHH354068	shRNA set against Mouse NPB (NM_153288.3)	Inquiry
SHH354072	shRNA set against Rat NPB (NM_153293.1)	Inquiry
SHR017408	shRNA set against Rat Npb(NM_153293.1)	Inquiry
SHR017454	shRNA set against Mouse Npb(NM_153288.3)	Inquiry
SHW012671	shRNA set against Danio rerio NPB (NM_001127369)	Inquiry

Cat.No.	Product Name	Price
CDFL008487	Mouse Npb cDNA Clone(NM_153288.3)	Inquiry
CDFR014573	Rat Npb cDNA Clone(NM_153293.1)	Inquiry
MiUTR1M-07762	NPB miRNA 3'UTR clone	Inquiry
MiUTR1R-04248	NPB miRNA 3'UTR clone	Inquiry
MiUTR4H-TG06093	NPB miRNA 3'UTR clone	Inquiry
CDCB174146	Danio rerio NPB ORF Clone (NM_001127369)	Inquiry
CDCH392123	Human NPB ORF clone(NM_148896.3)	Inquiry
CDCR270274	Mouse Npb ORF Clone(NM_153288.3)	Inquiry
CDCR381660	Rat Npb ORF Clone(NM_153293.1)	Inquiry

Detailed Information

Neuropeptide B (NPB) is an endogenous ligand of G-protein-coupled receptor 7 (GP7) and G-protein-coupled receptor 8 (GPR8) identified in 2002. It is a unique nitrogen-terminal tryptophan C-6 brominated peptide with a structure similar to the neuropeptide W. In vitro pharmacological studies have found that NPB is only a high affinity ligand for GP7.

NPB Expression

In the central nervous system, in situ hybridization revealed that mouse NPB precursor mRNA was expressed in the hippocampal CA1-CA3 region, lateral phrenic nucleus, hypothalamic paraventricular nucleus (PVN), and some nucleus groups in the midbrain and brainstem. This includes the E. Westfal nucleus (EW nucleus), blue spots, lateral parabrachial nucleus, etc., among which the EW nucleus expresses the most. Immunohistochemistry and fluorescence showed that there were NPB immunoreactive (irNPB) cells in multiple regions of the hypothalamus. In peripheral tissues, RT-PCR showed that human NBMB mRNA was expressed in kidney, testis, uterus, ovary and placenta. The expression of NPB mRNA in the stomach, spinal cord, and testis was detected by Northern blot, but it was less expressed in liver and kidney. NPB immunocompetent cells were also found in isolated islet cells from rats, and ppNPB and NPWR1-like mRNAs were expressed.

NPB Figure 1. The ligand-receptor pair(s) in chickens, humans, and zebrafish. (Bu, G., et al. 2016)

NPB and Biological Rhythm

NPB and GP7mRNA show a high degree of supraoptic nucleus (SCN), and NPB also has a strong signal there, suggesting that NPB and its receptor GP7 may participate in the regulation of biological rhythm. Studies have found that NPB has a two-way regulatory effect on food intake and is affected by CRF. At the same time, NPB also participates in regulating the hypothalamus-pituitary-adrenal (HPA) cortex axis. In the light and dark phases, NPB was injected through the lateral ventricle, and it was found that NPB reduced the spontaneous activity of mice in the dark phase. EEG and EMG measurements also showed that at this time NPB increased slow wave sleep (SWS) in mice, while heterophasic sleep was not affected, and the spectral power of NPB-induced slow wave sleep was similar to physiology. NPB immunopositive cells were present in the ventral tegmental area (VTA) and substantia nigra (SN) of the midbrain, and co-expressed with tyrosine hydroxylase-positive neurons (possibly dopaminergic neurons). Dopamine is an important neurological substance regulating sleep-wake, suggesting that in the midbrain, NPB may interact with dopaminergic neurons to participate in the regulation of sleep-wake.

NPB and Energy Metabolism

The regulation of NPB on feeding behavior is more complicated. Intravenous injection of NPB in conscious mice during the dark period found that in the initial 2 h low dose (3 nmol) induced increased food intake, but high doses inhibited food intake, and the two doses of NPB both suppressed appetite in the subsequent period. When a known appetite-suppressing peptide, a hormone-releasing hormone-reducing factor (CRF), is injected into the ventricle in advance, the appetite suppressive effect of NPB can be significantly increased. When both CRF and NPB were given at the same time, the appetite of the mice was completely inhibited for more than 4 h, indicating that NPB has a two-way regulatory effect on food intake and that the peptide is related to food intake inhibition under stress conditions.

NPB can also increase the secretion and expression of resistin. Studies have shown that resistin can increase insulin resistance and stimulate liver glucose production, both of which can cause blood glucose concentrations to increase, suggesting that NPB can regulate blood glucose concentrations in rats. Studies have found that sleep deprivation increases appetite, reduces energy expenditure, and affects glucose metabolism. Therefore, NPB may be involved in regulating energy metabolism abnormalities caused by chronic stress such as chronic sleep restriction, especially long-term sleep restriction.

References:

Bu, G. , Lin, D. , Cui, L. , Huang, L. , Lv, C. , & Huang, S. , et al. (2016). Characterization of neuropeptide b (npb), neuropeptide w (npw) and their receptors in chickens: evidence for npw being a novel inhibitor of pituitary growth hormone and prolactin secretion. Endocrinology, en.2016-1141.
Teresa, G. , Marta, T. N. , Agata, D. , Ada, M. A. , Monika, D. W. , & Agnieszka, S. , et al. (2018). Neuropeptide b and vaspin as new biomarkers in anorexia nervosa. BioMed Research International, 2018, 1-8.
Magdalena, C. D. . (2018). Distribution and function of neuropeptides w/b signaling system. Frontiers in Physiology, 9, 981.

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