Neurobehavioral profile of neuropeptide Y

Jolicoeur, F.B.; Michaud, Jean-Nil; Rivest, Robert; Ménard, Daniel; Gaudin, Daniel; Fournier, Alain; St‐Pierre, Serge

doi:10.1016/0361-9230(91)90237-e

Cited by 74 publications

(25 citation statements)

References 17 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…With respect to the binding, efficacy was increased about five to 10-fold compared with NPY. Only [Arg6,Pro34]pNPY (8) showed a fivefold loss in efficacy owing to an increase in binding. A 10-fold loss in affinity, but almost equal efficacy was found for [cPP20±23, Pro34]pNPY (2), whereas similar affinity in binding and inhibition of cAMP production was found for [Phe7, Pro34]pNPY (11).…”

Section: Functional Studiesmentioning

confidence: 99%

“…Profound effects on stimulation of food intake, secretion of luteinizing and growth hormone, and insulin release suggest an important role for NPY in the pathophysiology of obesity and diabetes [2±5]. A wide range of other effects of NPY have been reported, such as potent vasoconstriction [6], facilitation of learning and memory [7], modulation of locomotor behaviours [8], induction of hypothermia [9,10], inhibition of sexual behaviour [11], shifts in circadian rhythms [12], modulation of cardiorespiratory parameters[13], anxiolytic potency [14] and inhibition of alcohol consumption and resistance [15].NPY is a 36-amino acid peptide amide belonging to the family of pancreatic polypeptides that includes also pancreatic polypeptide (PP) and peptide YY; it was first isolated from pig brain in 1982 [16].NPY is widely distributed within the central nervous system and in the periphery. [25,26].…”

mentioning

confidence: 99%

mentioning

confidence: 99%

See 2 more Smart Citations

Novel analogues of neuropeptide Y with a preference for the Y₁‐receptor

Söll

Dinger

Lundell

et al. 2001

European Journal of Biochemistry

View full text Add to dashboard Cite

In contrast, cyclo S±S [Cys20,Cys24]pNPY was found to be a highly selective ligand at the Y 2 -receptor, binding only threefold less efficiently than NPY. Analogues containing variations of positions 31 and 32 showed highly reduced affinity to the Y 1 -receptor, while binding to the Y 5 -receptor was affected less. Inhibition of cAMP-accumulation of selected peptides with replacements within position 20±23 of NPY showed preserved agonistic properties. The NPY analogues tested give insights into ligand±receptor interaction of NPY at the Y 1 -, Y 2 -and Y 5 -receptor and contribute to our understanding of subtype selectivity. Furthermore, the Y 1 -receptor-preferring peptides are novel tools that will provide insight into the physiological role of the Y 1 -receptor.Keywords: food intake; neuropeptides; NPY; selective ligands; structure±affinity relationship.Obesity, food intake and energy homeostasis are key areas of growing importance because obesity is beginning to replace malnutrition and infectious diseases as the most significant contributor to ill health in the developed world [1]. Neuropeptide Y (NPY) is one of the most important effector molecules of leptin: it is a key molecule in the regulation of food intake, it acts via several different receptor subtypes and elicits several physiological effects. Profound effects on stimulation of food intake, secretion of luteinizing and growth hormone, and insulin release suggest an important role for NPY in the pathophysiology of obesity and diabetes [2±5]. A wide range of other effects of NPY have been reported, such as potent vasoconstriction [6], facilitation of learning and memory [7], modulation of locomotor behaviours [8], induction of hypothermia [9,10], inhibition of sexual behaviour [11], shifts in circadian rhythms [12], modulation of cardiorespiratory parameters[13], anxiolytic potency [14] and inhibition of alcohol consumption and resistance [15].NPY is a 36-amino acid peptide amide belonging to the family of pancreatic polypeptides that includes also pancreatic polypeptide (PP) and peptide YY; it was first isolated from pig brain in 1982 [16].NPY is widely distributed within the central nervous system and in the periphery. [25,26]. A putative Y 3 -receptor has been described only pharmacologically and no specific agonists or antagonists are known [27]. All receptors belong to the G-protein coupled receptor superfamily [28]. The correlation of a certain receptor subtype to a distinct physiological effect is not yet fully understood. Recent studies even suggest that different receptor subtypes redundantly mediate identical actions in a given system, as has been shown for the Y 1 -and Y 5 -receptor in the regulation of food intake [3]. Findings that deficiencies in either the Y 1 -or the Y 5 -receptors do not significantly impair the normal feeding response to fasting or NPY stimulation, strongly indicate that both Y receptors are involved in appetite regulation by NPY [29,30]. Selective receptor agonists or antagonists are useful tools with which to stu...

show abstract

Section: Functional Studiesmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

See 1 more Smart Citation

Novel analogues of neuropeptide Y with a preference for the Y₁‐receptor

Söll

Dinger

Lundell

et al. 2001

European Journal of Biochemistry

View full text Add to dashboard Cite

show abstract

“…Although NPY was first identified as a potent orexigenic neuropeptide [42, 124], subsequent studies demonstrated that NPY ICV decreased resting behavior [125]. Other studies demonstrated that NPY ICV decreased [125,126,127] or had no effect [128] on SPA while NPY in the PVN [129, 130], PFA [129] or sulcal prefrontal cortex [131] also had no effect on SPA. NPY effects on energy expenditure have also been demonstrated [79,131,132,133,134] and animals given repeated NPY injections gain weight and exhibit excess adiposity.…”

Section: Potential Mediators Of Neatmentioning

confidence: 99%

Neuropeptidergic Mediators of Spontaneous Physical Activity and Non-Exercise Activity Thermogenesis

Teske¹,

Billington

Kotz³

2007

Neuroendocrinology

View full text Add to dashboard Cite

Lean individuals have high levels of spontaneous physical activity (SPA) and the energy expenditure derived from that activity, termed non-exercise activity thermogenesis or NEAT, appears to protect them from obesity. Conversely, obesity in different human populations is characterized by low levels of SPA and NEAT. Like in humans, elevated SPA in rats appears to protect against obesity: obesity-resistant rats have significantly greater SPA and NEAT than obesity-prone rats. We review the literature on brain mechanisms important in mediating SPA and NEAT. The focus is on neuropeptides, including cholecystokinin, corticotropin-releasing hormone (also known as corticotropin-releasing factor), neuromedin U, neuropeptide Y, leptin, agouti-related protein, orexin-A (also known as hypocretin-1), and ghrelin. We also review information regarding interactions between these neuropeptides and dopamine, a neurotransmitter important in mediating motor function. Finally, we present evidence that elevated signaling of pathways mediating SPA and NEAT may protect against weight gain and obesity.

show abstract

“…NPY is expressed in neurons throughout the brain and intensely expressed in the ARC [1,11]. NPY is the most potent molecule identified so far to stimulate feeding behavior in various species including the rat [40,77] and mouse [61]. Direct injection of NPY into specific hypothalamic sites [12,43,51] and i.c.v.…”

Section: Introductionmentioning

confidence: 99%

Distribution and Neuronal Networks of Novel GPCR Ligands in Feeding Regulation

Takenoya

Kageyama

Guan

et al. 2005

Acta Histochem. Cytochem

View full text Add to dashboard Cite

Recent studies have shown that a number of novel G-protein coupled receptor (GPCR) ligands localize in brain tissue and perform a range of physiological functions, some of which have been studied and clarified, and others about which less is known. Here, we wish to describe the distribution and localization of GPCR ligands identified thus far and to examine their involvement in neuronal networks, particularly those networks related to feeding regulation. The review analyzes published reports of morphological and physiological data looking mainly at the functional significance of feeding-regulation factors, such as those described by our research group and others, and neuronal interactions among these GPCR ligands in the hypothalamus. Cross-talk among several GPCR ligand-containing neuron types in the hypothalamus plays a role in determining feeding states. We introduce structural and functional characteristics of novel GPCR ligands and summarize the known interactions between several GPCR ligand-containing neuron types and leptin-targeting neurons in the hypothalamus. Finally, we present a new scheme summarizing neuronal networks with regard to feeding regulation in the hypothalamus. Research in this area will play an important role in clarifying neurologically-based causes for appetite dysfunction and establishing therapies for people suffering from such conditions.

show abstract

Neurobehavioral profile of neuropeptide Y

Cited by 74 publications

References 17 publications

Novel analogues of neuropeptide Y with a preference for the Y₁‐receptor

Novel analogues of neuropeptide Y with a preference for the Y₁‐receptor

Neuropeptidergic Mediators of Spontaneous Physical Activity and Non-Exercise Activity Thermogenesis

Distribution and Neuronal Networks of Novel GPCR Ligands in Feeding Regulation

Contact Info

Product

Resources

About

Neurobehavioral profile of neuropeptide Y

Cited by 74 publications

References 17 publications

Novel analogues of neuropeptide Y with a preference for the Y1‐receptor

Novel analogues of neuropeptide Y with a preference for the Y1‐receptor

Neuropeptidergic Mediators of Spontaneous Physical Activity and Non-Exercise Activity Thermogenesis

Distribution and Neuronal Networks of Novel GPCR Ligands in Feeding Regulation

Contact Info

Product

Resources

About

Novel analogues of neuropeptide Y with a preference for the Y₁‐receptor

Novel analogues of neuropeptide Y with a preference for the Y₁‐receptor