Changes in Subcellular Distribution of n-Octanoyl or n-Decanoyl Ghrelin in Ghrelin-Producing Cells

Nishi, Yoshihiro; Mifune, Hiroharu; Yabuki, Akira; Tajiri, Yuji; Hirata, Rumiko; Tanaka, Eiichiro; Hosoda, Hiroshi; Kangawa, Kenji; Kojima, Masayasu

doi:10.3389/fendo.2013.00084

Cited by 10 publications

(14 citation statements)

References 33 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The next issue was to determine if this higher available stomach C8:0 level influenced the stomach total ghrelin expression and increased the concentration of circulating acylated ghrelin, after the action of the gastric GOAT enzyme. Indeed, Nishi et al detected heptanoylghrelin [ 25 ] or decanoylghrelin [ 48 ] in the stomachs of mice fed with triheptanoin or tricaprin. This suggests that ingested MCFAs were directly utilized for the ghrelin acylation.…”

Section: Discussionmentioning

confidence: 99%

“…In addition, when related to dietary lipids and especially dietary MCFAs, the importance of the so-called GOAT-ghrelin-GHSR-1a axis on these parameters is unclear. Nishi et al [ 48 ] found no effect on body weight and food intake after feeding mice during two weeks with diets enriched in tricaprylin or tricaprin compared to control diets. However, feeding GOAT-null mice with MCT-enriched diets during 8 weeks resulted in significantly lower body weight compared with control mice [ 26 ].…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Dietary Caprylic Acid (C8:0) Does Not Increase Plasma Acylated Ghrelin but Decreases Plasma Unacylated Ghrelin in the Rat

et al. 2015

View full text Add to dashboard Cite

Focusing on the caprylic acid (C8:0), this study aimed at investigating the discrepancy between the formerly described beneficial effects of dietary medium chain fatty acids on body weight loss and the C8:0 newly reported effect on food intake via ghrelin octanoylation. During 6 weeks, Sprague-Dawley male rats were fed with three dietary C8:0 levels (0, 8 and 21% of fatty acids) in three experimental conditions (moderate fat, caloric restriction and high fat). A specific dose-response enrichment of the stomach tissue C8:0 was observed as a function of dietary C8:0, supporting the hypothesis of an early preduodenal hydrolysis of medium chain triglycerides and a direct absorption at the gastric level. However, the octanoylated ghrelin concentration in the plasma was unchanged in spite of the increased C8:0 availability. A reproducible decrease in the plasma concentration of unacylated ghrelin was observed, which was consistent with a decrease in the stomach preproghrelin mRNA and stomach ghrelin expression. The concomitant decrease of the plasma unacylated ghrelin and the stability of its acylated form resulted in a significant increase in the acylated/total ghrelin ratio which had no effect on body weight gain or total dietary consumption. This enhanced ratio measured in rats consuming C8:0 was however suspected to increase (i) growth hormone (GH) secretion as an increase in the GH-dependent mRNA expression of the insulin like growth Factor 1 (IGF-1) was measured (ii) adipocyte diameters in subcutaneous adipose tissue without an increase in the fat pad mass. Altogether, these results show that daily feeding with diets containing C8:0 increased the C8:0 level in the stomach more than all the other tissues, affecting the acylated/total ghrelin plasma ratio by decreasing the concentration of circulating unacylated ghrelin. However, these modifications were not associated with increased body weight or food consumption.

show abstract

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Dietary Caprylic Acid (C8:0) Does Not Increase Plasma Acylated Ghrelin but Decreases Plasma Unacylated Ghrelin in the Rat

et al. 2015

View full text Add to dashboard Cite

show abstract

“…Rodent studies support the concept that circulating acyl-ghrelin levels are at least in part dependent on nutritional availability of MCFAs (16). This observation is supported by studies of Nishi et al (17), who showed that the amount of C8 or C10 acyl-ghrelin content in the stomach depends on nutritional conditions. Ingestion of the medium-chain triglyceride, glycerol triheptanoate, which is not naturally synthesized by mammalian cells, resulted in the production of n-heptanoyl-ghrelin, which was found both in the circulation and in the stomach of the animals (16).…”

Section: Discussionmentioning

confidence: 64%

The Level of Circulating Octanoate Does Not Predict GhrelinO-Acyl Transferase (GOAT)-Mediated Acylation of Ghrelin During Fasting

Nass

Nikolayev

Liu

et al. 2015

The Journal of Clinical Endocrinology & Metabolism

View full text Add to dashboard Cite

show abstract

“…Indeed, ingestion by mice of either MCFAs or MCTs increased the stomach concentration of acylated ghrelin (Nishi, Hiejima, Hosoda, et al, 2005), without changing the total ghrelin amounts. Nishi et al detected heptanoylghrelin (Nishi, Hiejima, Hosoda, et al, 2005) or decanoylghrelin (Nishi et al, 2013) in the stomachs of mice fed with triheptanoin or tricaprin, confirming that at least part of the ingested MCFAs was directly used for ghrelin acylation. These results are consistent with the hypothesis of gastric absorption of MCTs but part of the caprylic acid present in the stomach may also come from intestinal absorption followed by uncompleted uptake by the liver.…”

Section: Impact Of Dietary Sfas On Cellular Protein Acylationmentioning

confidence: 98%

Fatty acid acylation of proteins: specific roles for palmitic, myristic and caprylic acids

Rioux¹

2016

OCL

View full text Add to dashboard Cite

-Fatty acid acylation of proteins corresponds to the co-or post-translational covalent linkage of an acyl-CoA, derived from a fatty acid, to an amino-acid residue of the substrate protein. The cellular fatty acids which are involved in protein acylation are mainly saturated fatty acids. Palmitoylation (S-acylation) corresponds to the reversible attachment of palmitic acid (C16:0) via a thioester bond to the side chain of a cysteine residue. N-terminal myristoylation refers to the covalent attachment of myristic acid (C14:0) by an amide bond to the N-terminal glycine of many eukaryotic and viral proteins. Octanoylation (O-acylation) typically concerns the formation of an ester bond between octanoic acid (caprylic acid, C8:0) and the side chain of a serine residue of the stomach peptide ghrelin. An increasing number of proteins (enzymes, hormones, receptors, oncogenes, tumor suppressors, proteins involved in signal transduction, eukaryotic and viral structural proteins) have been shown to undergo fatty acid acylation. The addition of the acyl moiety is required for the protein function and usually mediates protein subcellular localization, protein-protein interaction or protein-membrane interaction. Therefore, through the covalent modification of proteins, these saturated fatty acids exhibit emerging specific and important roles in modulating protein functions. This review provides an overview of the recent findings on the various classes of protein acylation leading to the biological ability of saturated fatty acids to regulate many pathways. Finally, the nutritional links between these elucidated biochemical mechanisms and the physiological roles of dietary saturated fatty acids are discussed. L'acylation concerne de très nombreuses protéines (enzymes, hormones, récepteurs, oncogènes, suppresseurs de tumeur, protéines impliquées dans la transduction des signaux, protéines de structure eucaryotes et même virales) et exerce donc une grande variété de fonctions dans les régulations cellulaires. La liaison covalente de l'acide gras à la protéine est cruciale pour l'acquisition de la fonction de la protéine, en changeant son hydrophobicité, en régulant l'ancrage de la protéine à la membrane, en modifiant son adressage subcellulaire ou encore en induisant des interactions entre sous-unités protéiques. La découverte progressive de nombreuses protéines acylées, dont la fonction est régulée par l'acylation, donne donc un nouvel intérêt fonctionnel à ces acides gras saturés. L'objectif de cette revue est de synthétiser les découvertes récentes sur les différentes classes d'acylation des protéines et sur les fonctions cellulaires émergentes que cette acylation procure à certains acides gras saturés. Le lien nutritionnel entre ces mécanismes moléculaires et les apports alimentaires en acides gras saturés est finalement discuté.

show abstract

Changes in Subcellular Distribution of n-Octanoyl or n-Decanoyl Ghrelin in Ghrelin-Producing Cells

Cited by 10 publications

References 33 publications

Dietary Caprylic Acid (C8:0) Does Not Increase Plasma Acylated Ghrelin but Decreases Plasma Unacylated Ghrelin in the Rat

Dietary Caprylic Acid (C8:0) Does Not Increase Plasma Acylated Ghrelin but Decreases Plasma Unacylated Ghrelin in the Rat

The Level of Circulating Octanoate Does Not Predict GhrelinO-Acyl Transferase (GOAT)-Mediated Acylation of Ghrelin During Fasting

Fatty acid acylation of proteins: specific roles for palmitic, myristic and caprylic acids

Contact Info

Product

Resources

About