The distribution of Neuropeptide FF and Neuropeptide VF in central and peripheral tissues and their role in energy homeostasis control

Koller, Júlia; Herzog, Herbert; Zhang, Lei

doi:10.1016/j.npep.2021.102198

Cited by 19 publications

(5 citation statements)

References 86 publications

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“…26RFa and its N-terminus elongated 43-amino acid form, called QRFP or pyroglutamylated RFamide peptide, are the cognate ligands of the human orphan receptor GPR103 [1,3]. Additionally, 26RFa is a member of the RFamide-related peptide (RFRP) family characterized by the same Arg-Phe-NH 2 amino acid signature at their C-terminus and is involved in the modulation of various neuronal and neuroendocrine functions [4][5][6]. In the brain, 26RFa's precursor mRNA is highly expressed in the regions controlling energy metabolism and appetite, such as in the ventromedial hypothalamus (VMH) and the lateral hypothalamic area (LHA) [7].…”

Section: Introductionmentioning

confidence: 99%

Blood Levels of Neuropeptide 26RFa in Relation to Anxiety and Aggressive Behavior in Humans—An Exploratory Study

et al. 2023

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26RFa, also referred to as QRFP, is a hypothalamic neuropeptide mainly known for its role in the regulation of appetite and glucose metabolism. Its possible relevance to emotional regulation is largely unexplored. To address this, in the present exploratory study, we analyzed the plasma concentrations of 26RFa in humans characterized by different levels of anxiety and aggressive behavior. For this purpose, the study included 13 prison inmates who have committed violent crimes and 19 age-matched healthy men from the general population as controls. Anxiety, depression and aggressive behavior were evaluated in both groups using standard questionnaires. The inmate group was characterized by increased aggression and anxiety compared to the controls. We found that the mean plasma levels of 26RFa did not significantly differ between the inmates and the controls. However, several high outliers were present only in the inmate group. The plasma levels of 26RFa correlated positively with the anxiety scores in all the studied subjects and controls. After removing the high outliers in the inmate group, positive correlations of 26RFa with anxiety and a subscale of hostility in the aggression scale were also recorded in this group. No significant correlations of 26RFa with depression scores or other parameters of aggressive behavior were found. Thus, the present results did not support an involvement of 26RFa in aggressive behavior in humans but pointed to a link between this neuropeptide and anxiety. Nevertheless, considering the exploratory nature of the present study, this conclusion should be verified in a larger cohort, including the clinical degree of anxiety.

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Section: Introductionmentioning

confidence: 99%

Blood Levels of Neuropeptide 26RFa in Relation to Anxiety and Aggressive Behavior in Humans—An Exploratory Study

et al. 2023

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“…Extensive evidence has shown that NPFF is involved in a variety of physiological processes in mammals, including anxiety, feeding, gut motility, cardiovascular regulation, pain and stress response, among others (Lin and Chen, 2019;Nguyen et al, 2020;Koller et al, 2021). Preliminary results also showed that NPFF has been implicated in the regulation of reproduction in fish (Osugi et al, 2011;Shahjahan et al, 2015;Tomihara et al, 2022).…”

Section: Introductionmentioning

confidence: 92%

“…Both peptides belong to the RFamide peptide family (Osugi et al, 2014b;Tsutsui and Ubuka, 2021). Depending on the species, the GnIH precursor encodes 2 to 4 mature peptides that have a conserved LPXRFa (X=L or Q) motif at their C-termini, while the NPFF precursor encodes 2 mature peptides, namely NPFF and NPAF, which are characterized by a common C-terminal PQRFa motif (Koller et al, 2021;Pinelli et al, 2022). The receptors for GnIH (GnIHR, also known as NPFFR1 or GPR147) and NPFF (NPFFR2, also called GPR74) are also paralogous.…”

Section: Introductionmentioning

confidence: 99%

Differential activation of neuropeptide FF receptors by gonadotropin-inhibitory hormone peptides in the European sea bass

et al. 2023

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Neuropeptide FF (NPFF) and gonadotropin-inhibitory hormone (GnIH) are thought to be paralogous, and a recent study has revealed that both NPFF and GnIH peptides can activate the GnIH receptor (GnIHR, also called NPFFR1) in the European sea bass (Dicentrarchus labrax). However, whether GnIH can bind to the NPFF receptor (NPFFR2) is still yet unknown in this species. Accordingly, we further investigated the potential interactions between GnIH and NPFFR2 (two NPFFR2 forms present in sea bass, namely NPFFR2-1 and NPFFR2-2) on the intracellular signaling pathways. Neither GnIH1 nor GnIH2 had any effect on basal CRE-luc activity, while forskolin-stimulated CRE-luc activity was significantly reduced when COS-7 cells expressing sea bass NPFFR2-1 and NPFFR2-2 were challenged with these two GnIH peptides. NPFF and NPAF also inhibited forskolin-induced CRE-luc activity via their cognate receptors. An evident stimulation of SRE-luc activity was observed when COS-7 cells transfected with NPFFR2-1 and NPFFR2-2 were treated with NPFF and NPAF, whereas GnIH peptides had no effect, except a slight but significant increase elicited by 1000 nM of GnIH1 in COS-7 cells expressing NPFFR2-2. Moreover, only GnIH2 exerted an inhibitory action on NFAT-RE-luc activity in COS-7 cells expressing NPFFR2-1. None of GnIH or NPFF peptides altered ERK phosphorylation levels via NPFFR2 receptors. Our results provide new evidence that sea bass GnIH peptides may exert their functions partially via NPFFR2, and PKA, PKC and Ca2+ routes are potential mediators.

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“…The analyses of the amiadation sites of the amastins from L. donovani show that this parasite develop 3 amastins with 4 amidation sites. The biological relevance of the amidation sites show that play important role in the translocation of the parasite from the internal leaf to the nucleus of infected cell; employing the molecular machinary of G proteins coupled receptor, transport the parasite from the cell membrane through of the cytoplasm to the nucleus of the infected cell [92]. However the results show that developed a four amidation sites thereby this mechanism did not play important role in the transport of the amastigote through of the cytoplasm of infected cell, which should be occur by the MHC-1 recycle and endosome formation, drag and transport the parasite in the cytoplasm of infected cell (Tab.…”

Section: Amidation Sites Of the Amastins From L Donovanimentioning

confidence: 99%

From the origin and molecular diversity of the amastins, to the origin and diversity of intracellular parasitism from human Trypanosomatids

Alejandro

2021

Preprint

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The large families of amastins from Leishmania donovani, L. infantum, L. major, L. braziliensis and Trypanosoma cruzi are strongly associated with the evolution of intracellular parasitism of rich cells in human MHC.1 molecules such as the macrophages, dendritic cells, and Langerhans cells by these parasites, recognize the MHC-1 molecules as host receptor. The internalization and transport of the paraste in the cytoplas of infected cell is facilitated by the MHC-1 recycle and endosome formation drag and transport the parasite in the cytoplasm of infected cell. The microbody amastins participate as coreceptor potency the infection, the tropism of L. major and L. braziliensis by the cells from the skin is facilitated by two molecular interactions, the first molecular interaction is faclitated by the amastins interact the human MHC-1 molecules, and the second molecular interaction is facilitated by the numerous microbody amastins; which also participate in the biogenesis of the small prasitophorous vcuole from L. major, and large parasitophorous vacuole from L. braziliensis.All amastins from these parasites developed deactivation domains, in different grade L. donovani develop an amastin surface coat specialized in deactivation of infected macrophages heavily glycosylated developed 38 amastins with 38 glycosylation Asp. N-Glycosylation sites and 45 N-glucosamina glycosylation sites, whereas L. infantum, L. major and L. braziliensis developed one half of glycosylated amastins in asparagine N-glycosylation sites, and T. cruzi did not developed none glycosylated amastin.The amastins surface coat from L. donovani is rich in phosphorylation sites, developed 45 amastins with 45 casein kinase II phosphorylations sites, and 48 amastins with 48 protein kinase phosphorylation sites. L. infantum, L. braziliensis, and T. cruzi developed 32, 42, and 8 amastins, with 94, 114, 21 casein kinase II phosphorylation sites; in similar way developed 35,38, 11 amastins with 89,78, and 22 protein kinase phosphorylation sites. The family of amastins from L. donovani develop 137 phosphoserines. and 128 phosphothreonine, L. major developed 14 phosphoserine and 4 phosphothreonine; L. infantum 1 phophoserine and 7 phosphothreonine; L. braziliensis did not developed phosphoserine and phosphothreonine and T. cruzi 4 phosphoserine and 4 phosphothreonine. The results show that amastin surface coat is equiped with numerous phosphorylations sites atractive for phosphohrylases from the infected host contribute with the dephosphorylation and deactivation of infectetd host cells.The amastins from L. major develop a membrane amastin with laminin G domain, which can interact with the collagen and heparin sulfate proteoglycan sites from the extracellular matrix of the skin tissue. Furthermore develop 14 amastins with tyrosine sulfation site, evade the activation of receptor of chemokines and the activation of the immune response by chemokines.There is an alternative mechanism of polarization of the immune response from protective TH1 to non protective TH2.The parasite nutrition is mediated by amastins that dissimilate the MHC-1 molecules and other subsets of proteins, the dissimilation products can be translocated through of the parasite cell membrane and employed as nutrient source.

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The distribution of Neuropeptide FF and Neuropeptide VF in central and peripheral tissues and their role in energy homeostasis control

Cited by 19 publications

References 86 publications

Blood Levels of Neuropeptide 26RFa in Relation to Anxiety and Aggressive Behavior in Humans—An Exploratory Study

Blood Levels of Neuropeptide 26RFa in Relation to Anxiety and Aggressive Behavior in Humans—An Exploratory Study

Differential activation of neuropeptide FF receptors by gonadotropin-inhibitory hormone peptides in the European sea bass

From the origin and molecular diversity of the amastins, to the origin and diversity of intracellular parasitism from human Trypanosomatids

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