Intestinal levels of anandamide and oleoylethanolamide in food-deprived rats are regulated through their precursors

Petersen, Gitte; Sørensen, Camilla T. N.; Schmid, Patricia C.; Artmann, Andreas; Tang-Christensen, Mads; Hansen, Steen Honoré; Larsen, Philip J.; Schmid, Harald H.O.; Hansen, Harald S.

doi:10.1016/j.bbalip.2005.12.011

Cited by 81 publications

(96 citation statements)

References 60 publications

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“…Nutrient status regulates OEA mobilization in a tissue-specific manner. In the small intestine, OEA levels decrease during food deprivation and increase upon re-feeding in rat (Rodríguez de Fonseca et al, 2001;Petersen et al, 2006) and mice (Fu et al, 2007). A feeding-induced OEA mobilization in small intestine of the Burmese python (Python molurus) has also been described (Astarita et al, 2006a).…”

Section: Introductionmentioning

confidence: 96%

“…The Journal of Experimental Biology (2014) Feeding promotes OEA mobilization in the small intestine of studied species, such as rats (Rodríguez de Fonseca et al, 2001;Petersen et al, 2006;Fu et al, 2007), mice (Fu et al, 2007) and Burmese pythons (Astarita et al, 2006a). Our results also support this hypothesis in fish, as intestinal OEA content decreased after 48 h of fasting, and subsequently returned to baseline levels following re-feeding.…”

Section: Research Articlementioning

confidence: 99%

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Role of oleoylethanolamide as a feeding regulator in goldfish

Tinoco

Armirotti

Isorna

et al. 2014

Journal of Experimental Biology

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Oleoylethanolamide (OEA) is a bioactive lipid mediator, produced in the intestine and other tissues, which is involved in energy balance regulation in mammals, modulating feeding and lipid metabolism. The purpose of the present study was to investigate the presence and possible role of OEA in feeding regulation in goldfish (Carassius auratus). We assessed whether goldfish peripheral tissues and brain contain OEA and their regulation by nutritional status. OEA was detected in all studied tissues (liver, intestinal bulb, proximal intestine, muscle, hypothalamus, telencephalon and brainstem). Food deprivation (48 h) reduced intestinal OEA levels and levels increased upon re-feeding, suggesting that this compound may be involved in the short-term regulation of food intake in goldfish, as a satiety factor. Next, the effects of acute intraperitoneal administration of OEA on feeding, swimming and plasma levels of glucose and triglycerides were analysed. Food intake, swimming activity and circulating triglyceride levels were reduced by OEA 2 h post-injection. Finally, the possible interplay among OEA and other feeding regulators (leptin, cholecystokinin, ghrelin, neuropeptide Y, orexin and monoamines) was investigated. OEA actions on energy homeostasis in goldfish could be mediated, at least in part, through interactions with ghrelin and the serotonergic system, as OEA treatment reduced ghrelin expression in the intestinal bulb, and increased serotonergic activity in the telencephalon. In summary, our results indicate for the first time in fish that OEA could be involved in the regulation of feeding, swimming and lipid metabolism, suggesting a high conservation of OEA actions in energy balance throughout vertebrate evolution.

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Section: Introductionmentioning

confidence: 96%

Section: Research Articlementioning

confidence: 99%

Role of oleoylethanolamide as a feeding regulator in goldfish

Tinoco

Armirotti

Isorna

et al. 2014

Journal of Experimental Biology

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“…2005; Peterson et al. 2006; Azari et al. 2013), but the exact mechanism through which OEA inhibits eating is still uncertain.…”

Section: Introductionmentioning

confidence: 99%

Oleoylethanolamide-induced anorexia in rats is associated with locomotor impairment

et al. 2018

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The endogenous peroxisome proliferator‐activated receptor alpha (PPAR‐α) agonist Oleoylethanolamide (OEA) inhibits eating in rodents, mainly by delaying the onset of meals. The underlying mechanisms of OEA‐induced anorexia, however, remain unclear. Animals treated with high OEA doses were shown to display signs of discomfort and impaired locomotion. Therefore, we first examined whether the impaired locomotion may contribute to OEA's anorectic effect. Second, it is controversial whether abdominal vagal afferents are necessary for OEA's anorectic effect. Thus, we explored alternative peripheral neural pathways mediating IP OEA's anorectic effect by performing a celiac‐superior mesenteric ganglionectomy (CGX) or a subdiaphragmatic vagal deafferentation (SDA) alone or in combination. Exogenously administered OEA at a commonly used dose (10 mg/kg BW, IP) concurrently reduced food intake and compromised locomotor activity. Attempts to dissociate both phenomena using the dopamine D2/D3 receptor agonist Quinpirole (1 mg/kg BW, SC) failed because Quinpirole antagonized both, OEA‐induced locomotor impairment and delay in eating onset. CGX attenuated the prolongation of the latency to eat by IP OEA, but neither SDA nor CGX prevented IP OEA‐induced locomotor impairment. Our results indicate that IP OEA's anorectic effect may be secondary to impaired locomotion rather than due to physiological satiety. They further confirm that vagal afferents do not mediate exogenous OEA's anorectic effects, but suggest a role for spinal afferents in addition to an alternative, nonneuronal signaling route.

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“…3Ϫ (8500 Ci/mmol, 10 mCi/ml) and palmitoyl- [1][2][3][4][5][6][7][8][9][10][11][12][13][14] C]CoA (60 mCi/mmol, 0.02 mCi/ml) were from PerkinElmer Life Sciences. Palmitoyl-CoA and arachidonyl-CoA, porcine pancreas phospholipase A 2 , and Streptomyces chromofuscus phospholipase D were from Sigma.…”

Section: Methodsmentioning

confidence: 99%

“…N-acylethanolamines (NAEs), a class of bioactive lipids that are involved in a variety of physiological processes, such as responses to pathogens, plant development, and germination in plants (8 -10) as well as control of appetite, inflammation, and apoptosis (11)(12)(13) in animals.…”

mentioning

confidence: 99%

Putative N-Acylphosphatidylethanolamine Synthase from Arabidopsis thaliana Is a Lysoglycerophospholipid Acyltransferase

Bulat

Garrett

2011

Journal of Biological Chemistry

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AT1G78690, a gene found in Arabidopsis thaliana, has been reported to encode a N-acyltransferase that transfers an acyl chain from acyl-CoA to the headgroup of phosphatidylethanolamine (PE) to form N-acylphosphatidylethanolamine (N-acyl-PE). Our investigation suggests that At1g78690p is not a PE-dependent N-acyltransferase but is instead a lysoglycerophospholipid O-acyltransferase. We overexpressed AT1G78690 in Escherichia coli, extracted the cellular lipids, and identified the accumulating glycerophospholipid as acylphos- phatidylglycerol (acyl-PG). Electrospray ionization quadrupole time-of-flight mass spectrometry (ESI-MS) analysis yielded [M ؊ H]؊ ions, corresponding by exact mass to acyl-PG rather than N-acyl-PE. Collision-induced dissociation mass spectrometry (MS/MS) yielded product ions consistent with acyl-PG. In addition, in vitro enzyme assays using both 32 P-and 14 C-radiolabeled substrates showed that AT1G78690 acylates 1-acyllysophosphatidylethanolamine (1-acyllyso-PE) and 1-acyllysophosphatidylglycerol (1-acyllyso-PG), but not PE or phosphatidylglycerol (PG), to form a diacylated product that co-migrates with PE and PG, respectively. We analyzed the diacylated product formed by AT1G78690 using a combination of base hydrolysis, phospholipase D treatment, ESI-MS, and MS/MS to show that AT1G78690 acylates the sn-2-position of 1-acyllyso-PE and 1-acyllyso-PG. N-Acylphosphatidylethanolamine (N-acyl-PE)2 is an anionic minor membrane glycerophospholipid (GPL) that is abundant in animals, higher plants, and certain microorganisms, such as yeast and Escherichia coli (1-7). This GPL is of particular interest because of its well documented role as the precursor to N-acylethanolamines (NAEs), a class of bioactive lipids that are involved in a variety of physiological processes, such as responses to pathogens, plant development, and germination in plants (8 -10) as well as control of appetite, inflammation, and apoptosis (11-13) in animals.In animals, N-acyl-PE synthesis is catalyzed by two distinct biochemical activities. A Ca 2ϩ -dependent membrane-associated protein has been characterized in brain, testis, and heart (14). This enzyme has been shown to catalyze the transfer of an acyl chain from the sn-1-position of a diacylated GPL, functions most efficiently at alkaline pH, and requires divalent cations (13,15,16). The gene encoding this enzyme has yet to be identified.A lecithin retinol acyltransferase-like protein from rats, RLP-1, has been shown to encode a Ca 2ϩ -independent N-acyltransferase (NAT) (17). It is predominantly expressed in testis and is, therefore, thought to be distinct from the Ca 2ϩ -dependent NAT. Ca 2ϩ -independent NAT activity is detected in both the soluble and membrane fractions when overexpressed in COS-7 cells and does not show preference for transfer of the sn-1 or sn-2 acyl chain to the amine of PE (17). Human and mouse homologs have been cloned and shown to possess similar NAT activity (18).In plants, N-acyl-PE is proposed to be synthesized from PE and unesterified fatty acid...

show abstract

Intestinal levels of anandamide and oleoylethanolamide in food-deprived rats are regulated through their precursors

Cited by 81 publications

References 60 publications

Role of oleoylethanolamide as a feeding regulator in goldfish

Role of oleoylethanolamide as a feeding regulator in goldfish

Oleoylethanolamide-induced anorexia in rats is associated with locomotor impairment

Putative N-Acylphosphatidylethanolamine Synthase from Arabidopsis thaliana Is a Lysoglycerophospholipid Acyltransferase

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