Involvement of phospholipase A/acyltransferase-1 in N-acylphosphatidylethanolamine generation

Uyama, Toru; Inoue, Manami; Okamoto, Yoko; Shinohara, Naoki; Tai, Tatsuya; Tsuboi, Kazuhito; Inoue, Tomohito; Tokumura, Akira; Ueda, Natsuo

doi:10.1016/j.bbalip.2013.08.017

Cited by 26 publications

(22 citation statements)

References 44 publications

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“…Previously, we suggested that the overexpression of PLA/ AT-2 (HRASLS2) also causes the dysfunction of peroxisomes (28), whereas PLA/AT-1 (HRASLS1, A-C1) did not appear to affect peroxisomal functions (45). In the present study, we observed that PLA/AT-2 inhibited the binding of Pex19p to Pex3p and Pex11␤p and decreased the protein level of PMP70.…”

Section: Discussionsupporting

confidence: 63%

Interaction of Phospholipase A/Acyltransferase-3 with Pex19p

Uyama

Kawai

Kono

et al. 2015

Journal of Biological Chemistry

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Section: Discussionsupporting

confidence: 63%

Interaction of Phospholipase A/Acyltransferase-3 with Pex19p

Uyama

Kawai

Kono

et al. 2015

Journal of Biological Chemistry

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“…1A), similarly to N ‐acylphosphatidylserine 42. While other approaches to NAPE determination rely on either full scan, SIM, or a single SRM transition per analyte 6, 7, 25, 26, 27, 28, 29, 30, 31, our method uses these two N ‐acyl specific transitions for each analyte, leading to a more selective identification and minimizing the risk of false positive results, as shown in Supporting Information Fig. S1.…”

Section: Resultsmentioning

confidence: 99%

“…Although they are partially separated by chromatography, the chromatographic resolution is not sufficient for individual quantification when using only the pseudo‐molecular ion, regardless of mass resolution. SRM in negative ion mode, using the neutral loss or carboxylate ion of the sn ‐2 fatty acyl chain, also does not resolve ambiguity, since the identities of the N ‐acyl (and the sn ‐1) chain remains unknown 27, 28. This shortcoming can be circumvented by N ‐acyl specific SRM transitions in positive ion mode, enabling identification of the N ‐acyl chain and the phosphatidylethanolamine moiety.…”

Section: Resultsmentioning

confidence: 99%

Quantitative analysis of N‐acylphosphatidylethanolamine molecular species in rat brain using solid‐phase extraction combined with reversed‐phase chromatography and tandem mass spectrometry

Triebl

Weissengruber

Trötzmüller

et al. 2016

J of Separation Science

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A novel method for the sensitive and selective identification and quantification of N‐acylphosphatidylethanolamine molecular species was developed. Samples were prepared using a combination of liquid–liquid and solid‐phase extraction, and intact N‐acylphosphatidylethanolamine species were determined by reversed‐phase high‐performance liquid chromatography coupled to positive electrospray tandem mass spectrometry. As a result of their biological functions as precursors for N‐acylethanolamines and as signaling molecules, tissue concentrations of N‐acylphosphatidylethanolamines are very low, and their analysis is additionally hindered by the vast excess of other sample components. Our sample preparation methods are able to selectively separate the analytes of interest from any expected biological interferences. Finally, the highest selectivity is achieved by coupling chromatographic separation and two N‐acyl chain specific selected reaction monitoring scans per analyte, enabling identification of both the N‐acyl chain and the phosphatidylethanolamine moiety. The validated method is suitable for the reliable quantification of N‐acylphosphatidylethanolamine species from rat brain with a lower limit of quantification of 10 pmol/g and a linear range up to 2300 pmol/g. In total, 41 N‐acylphosphatidylethanolamine molecular species with six different N‐acyl chains, amounting to a total concentration of 3 nmol/g, were quantified.

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“…[1,[2][3][4][5][6][7][8][9][10][11][12][13][14] C]ethanolamine HCl was from Moravek Biochemicals (Brea, CA). Horseradish peroxidaselinked anti-mouse and anti-rabbit IgGs were from GE Healthcare (Piscataway, NJ).…”

Section: 2-[1′-mentioning

confidence: 99%

“…However, a series of our recent studies revealed that five members of the HRAS-like suppressor (HRASLS) family, which were originally discovered as tumor suppressors, possess calciumindependent phospholipid-metabolizing activities including NAPE-forming N-acyltransferase and PLA 1/2 activities (8-12), and we proposed to give HRASLS-1-5 the names phospholipase A/acyltransferase-1-5 (PLAAT-1-5), respectively (11). Among the five members, PLAAT-1 particularly received our attention because of its relatively high PE N-acyltransferase activity over PLA 1/2 activity in vitro and predominant expression in testis, skeletal muscle, brain, and heart of humans, mice, and rats, where NAPEs accumulate in response to ischemia and inflammation (11,13).Abstract N-Acylphosphatidylethanolamines (NAPEs) are a class of glycerophospholipids, which are known as precursors for different bioactive N-acylethanolamines. We previously reported that phospholipase A/acyltransferase-1 (PLAAT-1), which was originally found in mammals as a tumor suppressor, catalyzes N-acylation of phosphatidylethanolamines to form NAPEs.…”

mentioning

confidence: 99%

Comparative analyses of isoforms of the calcium-independent phosphatidylethanolamine N-acyltransferase PLAAT-1 in humans and mice

Hussain

Uyama

Kawai

et al. 2016

Journal of Lipid Research

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Fatty acyl ethanolamides [N-acylethanolamines (NAEs)] are a class of lipid mediators. Among them, arachidonoylethanolamide (anandamide) is known to be an endogenous ligand of cannabinoid receptors (namely, an endocannabinoid) (1). In addition, palmitoylethanolamide and oleoylethanolamide show biological activities such as antiinflammation, analgesia, and appetite suppression via different receptors including PPAR- (2-5). These NAEs are biosynthesized principally through a two-step pathway from membrane glycerophospholipids via N-acylphosphatidylethanolamines (NAPEs) (6). The first reaction is the transfer of an acyl chain from a glycerophospholipid molecule such as phosphatidylcholine (PC) to the amino group of phosphatidylethanolamine (PE), resulting in the formation of NAPE, and the enzyme responsible is known as PE N-acyltransferase. Very recently, cPLA 2 ɛ, a member of the cytosolic phospholipase A 2 (PLA 2 ) family (PLA2G4), has been identified as the calcium-stimulated N-acyltransferase capable of catalyzing this step (7). However, a series of our recent studies revealed that five members of the HRAS-like suppressor (HRASLS) family, which were originally discovered as tumor suppressors, possess calciumindependent phospholipid-metabolizing activities including NAPE-forming N-acyltransferase and PLA 1/2 activities (8-12), and we proposed to give HRASLS-1-5 the names phospholipase A/acyltransferase-1-5 (PLAAT-1-5), respectively (11). Among the five members, PLAAT-1 particularly received our attention because of its relatively high PE N-acyltransferase activity over PLA 1/2 activity in vitro and predominant expression in testis, skeletal muscle, brain, and heart of humans, mice, and rats, where NAPEs accumulate in response to ischemia and inflammation (11,13).Abstract N-Acylphosphatidylethanolamines (NAPEs) are a class of glycerophospholipids, which are known as precursors for different bioactive N-acylethanolamines. We previously reported that phospholipase A/acyltransferase-1 (PLAAT-1), which was originally found in mammals as a tumor suppressor, catalyzes N-acylation of phosphatidylethanolamines to form NAPEs. However, recent online database suggested the presence of an uncharacterized isoform of PLAAT-1 with an extra sequence at the N terminus. In the present study, we examined the occurrence, intracellular localization, and catalytic properties of this longer isoform, as well as the original shorter isoform from humans and mice. Our results showed that human tissues express the longer isoform but not the short isoform at all. In contrast, mice expressed both isoforms with different tissue distribution. Unlike the cytoplasmic localization of the shorter isoform, the long isoform was found in both cytoplasm and nucleus, inferring that the extra sequence harbors a nuclear localization signal. As assayed with purified proteins, neither isoform required calcium for full activity. Moreover, the overexpression of each isoform remarkably increased cellular NAPE levels. These results conclude that the new long is...

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Involvement of phospholipase A/acyltransferase-1 in N-acylphosphatidylethanolamine generation

Cited by 26 publications

References 44 publications

Interaction of Phospholipase A/Acyltransferase-3 with Pex19p

Interaction of Phospholipase A/Acyltransferase-3 with Pex19p

Quantitative analysis of N‐acylphosphatidylethanolamine molecular species in rat brain using solid‐phase extraction combined with reversed‐phase chromatography and tandem mass spectrometry

Comparative analyses of isoforms of the calcium-independent phosphatidylethanolamine N-acyltransferase PLAAT-1 in humans and mice

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