Prolactin Releasing Peptide Has High Affinity and Efficacy at Neuropeptide FF2 Receptors

Engström, Mia; Brandt, Annika; Wurster, Siegfried; Savola, Juha‐Matti; Panula, Pertti

doi:10.1124/jpet.102.047118

Cited by 96 publications

(94 citation statements)

References 31 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Similarly, both the PrRP and the metastin receptors only bind their endogenous ligands (PrRPs and kisspeptins respectively) and are unaffected by other RFamides (Muir et al, 2001;Engstrom et al, 2003). In contrast, NPFF-1 and NPFF-2 receptors are relatively promiscuous and are activated by FMRFamide (Engstrom et al, 2003). However, both NPFF-1 and NPFF-2 can be blocked by the NPY-1 receptor antagonist BIBP3226 (Mollereau et al, 2001;Mollereau et al, 2002).…”

Section: Discussionmentioning

confidence: 90%

“…Thus other RFamides do not activate the QRFP receptors. Similarly, both the PrRP and the metastin receptors only bind their endogenous ligands (PrRPs and kisspeptins respectively) and are unaffected by other RFamides (Muir et al, 2001;Engstrom et al, 2003). In contrast, NPFF-1 and NPFF-2 receptors are relatively promiscuous and are activated by FMRFamide (Engstrom et al, 2003).…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Heterologous expression of the invertebrate FMRFamide–gated sodium channel as a mechanism to selectively activate mammalian neurons

Schanuel¹,

Bell²,

Henderson³

et al. 2008

Neuroscience

View full text Add to dashboard Cite

Considerable effort has been directed toward the development of methods to selectively activate specific subtypes of neurons. Focus has been placed on the heterologous expression of proteins that are capable of exciting neurons in which they are expressed. Here we describe the heterologous expression of the invertebrate FMRFamide-gated sodium channel from Helix aspersa (HaFaNaC) in hippocampal slice cultures. HaFaNaC was co-expressed with a fluorescent protein (GFP, dsRed or tdTomato) in CA3 pyramidal neurons of rat hippocampal slice cultures using single cell electroporation. Pressure application of the agonist FMRFamide to HaFaNaC-expressing neuronal somata produced large prolonged depolarizations and bursts of action potentials (AP). FMRFamide responses were inhibited by amiloride (100 µM). In contrast, pressure application of FMRFamide to the axons of neurons expressing HaFaNaC produced no response. Fusion of GFP to the N-terminus of HaFaNaC showed that GFP-HaFaNaC was absent from axons. Bath application of FMRFamide produced persistent AP firing in HaFaNaC-expressing neurons. This FMRFamide-induced increase in the frequency of APs was dose-dependent. The concentrations of FMRFamide required to activate HaFaNaC-expressing neurons were below that required to activate the homologous acid sensing ion channel normally found in mammalian neurons. Furthermore, the mammalian neuropeptides neuropeptide FF and RFRP-1, which have amidated RF C-termini, did not affect HaFaNaCexpressing neurons. Antagonists of NPFF receptors (BIBP3226) also had no effect on HaFaNaC. Therefore, we suggest that heterologous-expression of HaFaNaC in mammalian neurons could be a useful method to selectively and persistently excite specific subtypes of neurons in intact nervous tissue.

show abstract

Section: Discussionmentioning

confidence: 90%

Section: Discussionmentioning

confidence: 99%

Heterologous expression of the invertebrate FMRFamide–gated sodium channel as a mechanism to selectively activate mammalian neurons

Schanuel¹,

Bell²,

Henderson³

et al. 2008

Neuroscience

View full text Add to dashboard Cite

show abstract

“…RFRP-1 and -3 share a similar C-terminal sequence with NPFF (Table 1) and as discussed above RFRP analogues bind with relatively high affinity to the NPFF1 and NPFF2 receptors , Liu et al 2001, Engstrom et al 2003, first identified as cognate receptors for NPFF (Bonini et al 2000). NPFF1 exhibits a higher affinity for RFRP-1 and -3 than for NPFF and is now considered to be the endogenous RFRP receptor , Engstrom et al 2003.…”

Section: Lpxrfamide Familymentioning

confidence: 99%

“…Therefore, NPFF2 is now generally considered the endogenous receptor for NPFF, with NPFF1 as the RFRP receptor. However, NPFF2 appears to be fairly promiscuous, showing relatively high affinities for NPFF, RFRPs as well as prolactin-releasing peptide (PrRP; Engstrom et al 2003). Human NPFF1 and NPFF2 share 46% sequence identity and exhibit 31-37% identities with the receptors for orexin, neuropeptide Y, CCK 1 and PrRP.…”

Section: Npff Familymentioning

confidence: 99%

The role of RFamide peptides in feeding

Bechtold

Luckman

2007

Journal of Endocrinology

118

View full text Add to dashboard Cite

In the three decades since FMRFamide was isolated from the clam Macrocallista nimbosa, the list of RFamide peptides has been steadily growing. These peptides occur widely across the animal kingdom, including five groups of RFamide peptides identified in mammals. Although there is tremendous diversity in structure and biological activity in the RFamides, the involvement of these peptides in the regulation of energy balance and feeding behaviour appears consistently through evolution. Even so, questions remain as to whether feedingrelated actions represent a primary function of the RFamides, especially within mammals. However, as we will discuss here, the study of RFamide function is rapidly expanding and with it so is our understanding of how these peptides can influence food intake directly as well as related aspects of feeding behaviour and energy expenditure.

show abstract

“…PrRP was also found to have high affinity to the NPFF2 receptor, resulting in anorexigenic effect (Engström et al 2003). The endogenous ligand of NPFF2 receptor, neuropeptide FF, also has hyperalgesic and antimorphine analgesic properties (for reviews, see Dockray 2004, Chartrel et al 2006.…”

Section: Prolactin-releasing Peptide In Food Intake Regulationmentioning

confidence: 99%

Prolactin-releasing peptide: a new tool for obesity treatment

Kuneš

Pražienková

Popelová

et al. 2016

Journal of Endocrinology

View full text Add to dashboard Cite

Obesity is an escalating epidemic, but an effective noninvasive therapy is still scarce. For obesity treatment, anorexigenic neuropeptides are promising tools, but their delivery from the periphery to the brain is complicated because peptides have a low stability and limited ability to cross the blood-brain barrier. In this review, we summarize results of several studies with our newly designed lipidized analogs of prolactin-releasing peptide (PrRP). PrRP is involved in feeding and energy balance regulation as demonstrated by obesity phenotypes of both PrRP-and PrRP-receptor-knockout mice. Lipidized PrRP analogs showed binding affinity and signaling in PrRP receptor-expressing cells similar to natural PrRP. Moreover, these analogs showed high binding affinity also to anorexigenic neuropeptide FF (NPFF)-2 receptor. Acute peripheral administration of myristoylated and palmitoylated PrRP analogs to mice and rats induced strong and long-lasting anorexigenic effects and neuronal activation in the brain areas involved in food intake regulation. Two-week-long subcutaneous administration of palmitoylated PrRP31 and myristoylated PrRP20 lowered food intake, body weight, improved metabolic parameters and attenuated lipogenesis in mice with diet-induced obesity. A strong anorexigenic, body weight-reducing and glucose tolerance-improving effect of palmitoylated-PrRP31 was shown also in diet-induced obese rats after its repeated 2-week-long peripheral administration. Thus, the strong anorexigenic and body weight-reducing effects of palmitoylated PrRP31 and myristoylated PrRP20 make these analogs attractive candidates for antiobesity treatment. Moreover, PrRP receptor might be a new target for obesity therapy.

show abstract

Prolactin Releasing Peptide Has High Affinity and Efficacy at Neuropeptide FF2 Receptors

Cited by 96 publications

References 31 publications

Heterologous expression of the invertebrate FMRFamide–gated sodium channel as a mechanism to selectively activate mammalian neurons

Heterologous expression of the invertebrate FMRFamide–gated sodium channel as a mechanism to selectively activate mammalian neurons

The role of RFamide peptides in feeding

Prolactin-releasing peptide: a new tool for obesity treatment

Contact Info

Product

Resources

About