Characterization of Neuropeptide B (NPB), Neuropeptide W (NPW), and Their Receptors in Chickens: Evidence for NPW Being a Novel Inhibitor of Pituitary GH and Prolactin Secretion

Bu, Guixian; Lin, Dongliang; Cui, Lin; Huang, Long; Lv, Can; Huang, Shiyao; Wan, Ying; Fang, Chao; Li, Juan; Wang, Yajun

doi:10.1210/en.2016-1141

Cited by 39 publications

(48 citation statements)

References 56 publications

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“…The name of NPW is derived from tryptophan residues (single-letter code W) as it appears in both the terminal N- and C- in its two mature forms ( Takenoya et al, 2012 ). Abundance of both these isoforms were demonstrated in several species including human, rat, mouse, pig, and chicken ( Brezillon et al, 2003 ; Tanaka et al, 2003 ; Kitamura et al, 2006 ; Fang et al, 2015 ; Bu et al, 2016 ). Chicken NPW exerts a noteworthy structural conservation with NPW of mammals ( Figure 1 ; Bu et al, 2016 ).…”

Section: Structurementioning

confidence: 99%

“…Such modification is unique among the mammalian bioactive peptides and its biological significance remains to be clarified, while the brominated and unbrominated forms of NPB exert comparable functional activities ( Fujii et al, 2002 ; Sakurai, 2013 ). In chicken, NPB precursor produces a mature peptide of 28 amino acids that is different from the 23- or 29 amino acids NPB of mammals ( Bu et al, 2016 ). Additionally, mammalian and avian NPB differ in their N termini where mammals have a “WYK” motif however birds have “WYR” motif.…”

Section: Structurementioning

confidence: 99%

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Distribution and Function of Neuropeptides W/B Signaling System

Dvoráková

2018

Front. Physiol.

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Neuropeptide W (NPW) and neuropeptide B (NPB) are two structurally and functionally related regulatory peptides, which are highly expressed in several brain regions and, additionally, in some peripheral tissues. Nevertheless, their distributions in the tissues are not similar. They act on target tissues via two subtypes of G protein-coupled receptors which are designated as NPBWR1 (GPR7) and NPBWR2 (GPR8), respectively, and possess different binding affinities. NPB activates NPBWR1, whereas NPW stimulates both the receptors with similar potency. Both of these peptides takes a part in the central regulation of neuroendocrine axes, feeding behavior, energy homeostasis, cardiovascular functions, circadian rhythm, pain sensation, modulation of inflammatory pain, and emotions. Over the past few years, studies have shown that NPB is also involved in sleep regulation. On the contrary, NPW participates in regulation of vascular myogenic tone, inhibits gastric tension sensitive vagal afferents and insulin secretion. Also, expression of NPW in the stomach is regulated by feeding. Abovementioned findings clearly demonstrate the functional diversity among NPW versus NPB signaling systems. In this review, signal transduction pathways of NPW/NPB are critically evaluated and observed together with mapping of expression of their signaling systems.

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Section: Structurementioning

confidence: 99%

Section: Structurementioning

confidence: 99%

Distribution and Function of Neuropeptides W/B Signaling System

Dvoráková

2018

Front. Physiol.

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“…Growth hormone (Gh), a single chain polypeptide hormone secreted from Gh cells in the anterior pituitary, plays important roles in the growth and development of vertebrates. Previous studies has established that the secretion of Gh is regulated by many neuroendocrine factors produced by the brain (especially the hypothalamus), including stimulators like Gh-releasing hormone ( 36 ) and ghrelin ( 37 ), and inhibitors like somatostatin (SS) ( 36 ) and neuropeptide W ( 38 ). Recently, it has been shown that Oxt stimulates GH release possibly directly via Oxtr in the pituitary of rats ( 10 ), adding a new player in the list of neuroendocrine factors regulating Gh cell functions.…”

Section: Discussionmentioning

confidence: 99%

Isotocin Regulates Growth Hormone but Not Prolactin Release From the Pituitary of Ricefield Eels

et al. 2018

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The neurohypophyseal hormone oxytocin (Oxt) has been shown to stimulate prolactin (Prl) synthesis and release from the adenohypophysis in rats. However, little is known about the functional roles of Oxt-like neuropeptides in the adenohypophysis of non-mammalian vertebrates. In this study, cDNAs encoding ricefield eel oxytocin-like receptors (Oxtlr), namely isotocin (Ist) receptor 1 (Istr1) and 2 (Istr2), were isolated and specific antisera were generated, respectively. RT-PCR and Western blot analysis detected the presence of both Istr1 and Istr2 in the brain and pituitary, but differential expression in some peripheral tissues, including the liver and kidney, where only Istr1 was detected. In the pituitary, immunoreactive Istr1 and Istr2 were differentially distributed, with the former mainly in adenohypophyseal cell layers adjacent to the neurohypophysis, whereas the latter in peripheral areas of the adenohypophysis. Double immunofluorescent images showed that immunostaining of Istr1, but not Istr2 was localized to growth hormone (Gh) cells, but neither of them was expressed in Prl cells. Ist inhibited Gh release in primary pituitary cells of ricefield eels and increased Gh contents in the pituitary gland of ricefield eels at 6 h after in vivo administration. Ist inhibition of Gh release is probably mediated by cAMP, PKC/DAG, and IP3/Ca2+ pathways. In contrast, Ist did not affect either prl gene expression or Prl contents in primary pituitary cells. Results of this study demonstrated that Ist may not be involved in the regulation of Prl, but inhibit Gh release via Istr1 rather than Istr2 in ricefield eels, and provided evidence for the direct regulation of Gh cells by oxytocin-like neuropeptides in the pituitary of non-mammalian vertebrates.

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“…Neuropeptides W, NPB and their receptors are mainly expressed in the central and periphery issues, which are involved in many physiological processes, including inflammatory pain, energy homeostasis, cardiovascular functions, immune system, stress and the neuroendocrine and respiratory systems . Previous studies have detected NPW/NPB mRNA, including bone marrow, femur and costal cartilagein, in humans, rats, pigs and chickens . The effect of G protein activation was mediated by protein kinase A (PKA), protein kinase C (PKC) and the mitogen‐activated protein kinases (MAPKs) cascades reaction .…”

Section: Introductionmentioning

confidence: 99%

“…[4][5][6] Previous studies have detected NPW/NPB mRNA, including bone marrow, femur and costal cartilagein, in humans, rats, pigs and chickens. 1,7,8 The effect of G protein activation was mediated by protein kinase A (PKA), protein kinase C (PKC) and the mitogen-activated protein kinases (MAPKs) cascades reaction. 9,10 The down-regulation or inhibition of PKA and PKC blocks chondrogenesis.…”

Section: Introductionmentioning

confidence: 99%

Neuropeptide W regulates proliferation and differentiation of ATDC5: Possible involvement of GPR7 activation, PKA and PKC‐dependent signalling cascades

Wang

Zheng

Jiang

et al. 2019

J Cellular Molecular Medi

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Various neuropeptides related to the energy equilibrium affect bone growth in humans and animals. Neuropeptides W (NPW) are identical in the internal ligands of the two G‐protein receptors (GPRs) included in subtypes 7 and 8. Neuropeptides W inhibits proliferation in the cultivated rat calvarial osteoblast‐like (ROB) cells. This study examines the expression of NPW and GPR7 in murine chondrocyte and their function. An immunohistochemical analysis showed that NPW and GPR7 were expressed in the proliferative chondrocytes of the growth plates in the hind limbs of mice. The NPW mRNA quickly elevated in the early differentiation (7‐14 days) of ATDC5 cells, while NPW and GPR7 mRNA were reduced during the late stage (14‐21 days) of differentiation. Neuropeptide W‐23 (NPW‐23) promoted the proliferation of ATDC5 cells, which was attenuated by inhibiting the GPR7, protein kinase A (PKA), protein kinase C (PKC) and ERK1/2 pathways. Neuropeptide W‐23 enhanced the early cell differentiation, as evaluated by collagen type II and the aggrecan gene expression, which was unaffected by inhibiting the ERK1/2 pathway, but significantly decreased by inhibiting the PKA, PKC and p38 MAPK pathways. In contrast, NPW‐23 was not involved in the terminal differentiation of the chondrocytes, as evaluated by the mineralization of the chondrocytes and the activity of the alkaline phosphatase. Neuropeptides W stimulated the PKA, PKC, p38 MAPK and ERK1/2 activities in a dose‐ and time‐dependent manner in the ATDC5 cells. These results show that NPW promotes the proliferation and early differentiation of murine chondrocyte via GPR7 activation, as well as PKA and PKC‐dependent signalling cascades, which may be involved in endochondral bone formation.

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Characterization of Neuropeptide B (NPB), Neuropeptide W (NPW), and Their Receptors in Chickens: Evidence for NPW Being a Novel Inhibitor of Pituitary GH and Prolactin Secretion

Cited by 39 publications

References 56 publications

Distribution and Function of Neuropeptides W/B Signaling System

Distribution and Function of Neuropeptides W/B Signaling System

Isotocin Regulates Growth Hormone but Not Prolactin Release From the Pituitary of Ricefield Eels

Neuropeptide W regulates proliferation and differentiation of ATDC5: Possible involvement of GPR7 activation, PKA and PKC‐dependent signalling cascades

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