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Metabolites
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Multipurpose Enzymes in Lipid Metabolism
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Multipurpose Enzymes in Lipid Metabolism

A special issue of Metabolites (ISSN 2218-1989). This special issue belongs to the section "Lipid Metabolism".

Deadline for manuscript submissions: closed (31 May 2022) | Viewed by 18335

Special Issue Editor

Dr. Christoph Heier

E-Mail Website
Guest Editor
Institute of Molecular Biosciences, University of Graz, 8010 Graz, Austria
Interests: lipid metabolism; sterol metabolism; enzymes

Special Issue Information

Dear Colleagues,

Lipid homeostasis results from the coordinated activity of countless enzymes that channel lipids through various metabolic pathways. Traditionally, certain enzymes have been assigned fixed places in the lipid metabolism network, often assuming the monofunctionality of these enzymes. However, a growing body of research shows how individual enzymes can interfere with different lipid metabolic pathways through their ability to act on multiple substrates. A prominent example is hormone-sensitive lipase with documented roles in the metabolism of acylglycerols, cholesterol and vitamin A. The multifunctionality of enzymes can occur as a result of the cell- or tissue-specific compartmentalization of lipid metabolic pathways, but can also be manifested within a single cell. How such multiple functions can be independently retrieved and how functional flexibility can be adapted to specific cellular needs remain to be elucidated. This Special Issue promotes research aimed at a better understanding of the multifunctionality of enzymes in the context of lipid metabolism. We welcome both primary research articles covering new perspectives and in-depth reviews summarizing selected examples of multifunctional enzymes in lipid metabolism.

Dr. Christoph Heier
Guest Editor

Manuscript Submission Information

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Keywords

  • lipid
  • metabolism
  • enzymology
  • multifunctional enzyme
  • lipid synthesis
  • lipolysis
  • lipase
  • acyltransferase
  • hydrolase
  • esterase

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Published Papers (6 papers)

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Research

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16 pages, 3912 KiB  
Article
The Catalytic Domain of Neuropathy Target Esterase Influences Lipid Droplet Biogenesis and Lipid Metabolism in Human Neuroblastoma Cells
by Lin He, Feifei Huang, Yu Wang, Yijun Wu, Li Xu and Pingan Chang
Metabolites 2022, 12(7), 637; https://doi.org/10.3390/metabo12070637 - 12 Jul 2022
Cited by 2 | Viewed by 1768
Abstract
As an endoplasmic reticulum (ER)-anchored phospholipase, neuropathy target esterase (NTE) catalyzes the deacylation of lysophosphatidylcholine (LPC) and phosphatidylcholine (PC). The catalytic domain of NTE (NEST) exhibits comparable activity to NTE and binds to lipid droplets (LD). In the current study, the nucleotide monophosphate [...] Read more.
As an endoplasmic reticulum (ER)-anchored phospholipase, neuropathy target esterase (NTE) catalyzes the deacylation of lysophosphatidylcholine (LPC) and phosphatidylcholine (PC). The catalytic domain of NTE (NEST) exhibits comparable activity to NTE and binds to lipid droplets (LD). In the current study, the nucleotide monophosphate (cNMP)-binding domains (CBDs) were firstly demonstrated not to be essential for the ER-targeting of NTE, but to be involved in the normal ER distribution and localization to LD. NEST was associated with LD surface and influenced LD formation in human neuroblastoma cells. Overexpression of NEST enhances triacylglycerol (TG) accumulation upon oleic acid loading. Quantitative targeted lipidomic analysis shows that overexpression of NEST does not alter diacylglycerol levels but reduces free fatty acids content. NEST not only lowered levels of LPC and acyl-LPC, but not PC or alkyl-PC, but also widely altered levels of other lipid metabolites. Qualitative PCR indicates that the increase in levels of TG is due to the expression of diacylglycerol acyltransferase 1 gene by NEST overexpression. Thus, NTE may broadly regulate lipid metabolism to play roles in LD biogenesis in cells. Full article
(This article belongs to the Special Issue Multipurpose Enzymes in Lipid Metabolism)
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Review

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24 pages, 7747 KiB  
Review
ABHD5—A Regulator of Lipid Metabolism Essential for Diverse Cellular Functions
by Margarita Schratter, Achim Lass and Franz P. W. Radner
Metabolites 2022, 12(11), 1015; https://doi.org/10.3390/metabo12111015 - 24 Oct 2022
Cited by 14 | Viewed by 3180
Abstract
The α/β-Hydrolase domain-containing protein 5 (ABHD5; also known as comparative gene identification-58, or CGI-58) is the causative gene of the Chanarin-Dorfman syndrome (CDS), a disorder mainly characterized by systemic triacylglycerol accumulation and a severe defect in skin barrier function. The clinical [...] Read more.
The α/β-Hydrolase domain-containing protein 5 (ABHD5; also known as comparative gene identification-58, or CGI-58) is the causative gene of the Chanarin-Dorfman syndrome (CDS), a disorder mainly characterized by systemic triacylglycerol accumulation and a severe defect in skin barrier function. The clinical phenotype of CDS patients and the characterization of global and tissue-specific ABHD5-deficient mouse strains have demonstrated that ABHD5 is a crucial regulator of lipid and energy homeostasis in various tissues. Although ABHD5 lacks intrinsic hydrolase activity, it functions as a co-activating enzyme of the patatin-like phospholipase domain-containing (PNPLA) protein family that is involved in triacylglycerol and glycerophospholipid, as well as sphingolipid and retinyl ester metabolism. Moreover, ABHD5 interacts with perilipins (PLINs) and fatty acid-binding proteins (FABPs), which are important regulators of lipid homeostasis in adipose and non-adipose tissues. This review focuses on the multifaceted role of ABHD5 in modulating the function of key enzymes in lipid metabolism. Full article
(This article belongs to the Special Issue Multipurpose Enzymes in Lipid Metabolism)
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17 pages, 1789 KiB  
Review
α/β-Hydrolase Domain-Containing 6 (ABHD6)— A Multifunctional Lipid Hydrolase
by Lisa-Maria Pusch, Lina Riegler-Berket, Monika Oberer, Robert Zimmermann and Ulrike Taschler
Metabolites 2022, 12(8), 761; https://doi.org/10.3390/metabo12080761 - 18 Aug 2022
Cited by 9 | Viewed by 3000
Abstract
α/β-hydrolase domain-containing 6 (ABHD6) belongs to the α/β-hydrolase fold superfamily and was originally discovered in a functional proteomic approach designed to discover monoacylglycerol (MAG) hydrolases in the mouse brain degrading the endocannabinoid 2-arachidonoylglycerol. Subsequent studies confirmed that ABHD6 acts as an MAG hydrolase [...] Read more.
α/β-hydrolase domain-containing 6 (ABHD6) belongs to the α/β-hydrolase fold superfamily and was originally discovered in a functional proteomic approach designed to discover monoacylglycerol (MAG) hydrolases in the mouse brain degrading the endocannabinoid 2-arachidonoylglycerol. Subsequent studies confirmed that ABHD6 acts as an MAG hydrolase regulating cannabinoid receptor-dependent and -independent signaling processes. The enzyme was identified as a negative modulator of insulin secretion and regulator of energy metabolism affecting the pathogenesis of obesity and metabolic syndrome. It has been implicated in the metabolism of the lysosomal co-factor bis(monoacylglycerol)phosphate and in the surface delivery of α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid-type glutamate receptors. Finally, ABHD6 was shown to affect cancer cell lipid metabolism and tumor malignancy. Here, we provide new insights into the experimentally derived crystal structure of ABHD6 and its possible orientation in biological membranes, and discuss ABHD6′s functions in health and disease. Full article
(This article belongs to the Special Issue Multipurpose Enzymes in Lipid Metabolism)
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18 pages, 1809 KiB  
Review
KIAA1363—A Multifunctional Enzyme in Xenobiotic Detoxification and Lipid Ester Hydrolysis
by Carina Wagner, Victoria Hois, Ulrike Taschler, Michael Schupp and Achim Lass
Metabolites 2022, 12(6), 516; https://doi.org/10.3390/metabo12060516 - 2 Jun 2022
Cited by 3 | Viewed by 2535
Abstract
KIAA1363, annotated as neutral cholesterol ester hydrolase 1 (NCEH1), is a member of the arylacetamide deacetylase (AADAC) protein family. The name-giving enzyme, AADAC, is known to hydrolyze amide and ester bonds of a number of xenobiotic substances, as well as clinical drugs and [...] Read more.
KIAA1363, annotated as neutral cholesterol ester hydrolase 1 (NCEH1), is a member of the arylacetamide deacetylase (AADAC) protein family. The name-giving enzyme, AADAC, is known to hydrolyze amide and ester bonds of a number of xenobiotic substances, as well as clinical drugs and of endogenous lipid substrates such as diglycerides, respectively. Similarly, KIAA1363, annotated as the first AADAC-like protein, exhibits enzymatic activities for a diverse substrate range including the xenobiotic insecticide chlorpyrifos oxon and endogenous substrates, acetyl monoalkylglycerol ether, cholesterol ester, and retinyl ester. Two independent knockout mouse models have been generated and characterized. However, apart from reduced acetyl monoalkylglycerol ether and cholesterol ester hydrolase activity in specific tissues and cell types, no gross-phenotype has been reported. This raises the question of its physiological role and whether it functions as drug detoxifying enzyme and/or as hydrolase/lipase of endogenous substrates. This review delineates the current knowledge about the structure, function and of the physiological role of KIAA1363, as evident from the phenotypical changes inflicted by pharmacological inhibition or by silencing as well as knockout of KIAA1363 gene expression in cells, as well as mouse models, respectively. Full article
(This article belongs to the Special Issue Multipurpose Enzymes in Lipid Metabolism)
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17 pages, 3669 KiB  
Review
Old but New: Group IIA Phospholipase A2 as a Modulator of Gut Microbiota
by Yoshitaka Taketomi, Yoshimi Miki and Makoto Murakami
Metabolites 2022, 12(4), 352; https://doi.org/10.3390/metabo12040352 - 14 Apr 2022
Cited by 13 | Viewed by 3419
Abstract
Among the phospholipase A2 (PLA2) superfamily, the secreted PLA2 (sPLA2) family contains 11 mammalian isoforms that exhibit unique tissue or cellular distributions and enzymatic properties. Current studies using sPLA2-deficient or -overexpressed mouse strains, along with [...] Read more.
Among the phospholipase A2 (PLA2) superfamily, the secreted PLA2 (sPLA2) family contains 11 mammalian isoforms that exhibit unique tissue or cellular distributions and enzymatic properties. Current studies using sPLA2-deficient or -overexpressed mouse strains, along with mass spectrometric lipidomics to determine sPLA2-driven lipid pathways, have revealed the diverse pathophysiological roles of sPLA2s in various biological events. In general, individual sPLA2s exert their specific functions within tissue microenvironments, where they are intrinsically expressed through hydrolysis of extracellular phospholipids. Recent studies have uncovered a new aspect of group IIA sPLA2 (sPLA2-IIA), a prototypic sPLA2 with the oldest research history among the mammalian PLA2s, as a modulator of the gut microbiota. In the intestine, Paneth cell-derived sPLA2-IIA acts as an antimicrobial protein to shape the gut microbiota, thereby secondarily affecting inflammation, allergy, and cancer in proximal and distal tissues. Knockout of intestinal sPLA2-IIA in BALB/c mice leads to alterations in skin cancer, psoriasis, and anaphylaxis, while overexpression of sPLA2-IIA in Pla2g2a-null C57BL/6 mice induces systemic inflammation and exacerbates arthritis. These phenotypes are associated with notable changes in gut microbiota and fecal metabolites, are variable in different animal facilities, and are abrogated after antibiotic treatment, co-housing, or fecal transfer. These studies open a new mechanistic action of this old sPLA2 and add the sPLA2 family to the growing list of endogenous factors capable of affecting the microbe–host interaction and thereby systemic homeostasis and diseases. Full article
(This article belongs to the Special Issue Multipurpose Enzymes in Lipid Metabolism)
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15 pages, 1222 KiB  
Review
PNPLA6/NTE, an Evolutionary Conserved Phospholipase Linked to a Group of Complex Human Diseases
by Doris Kretzschmar
Metabolites 2022, 12(4), 284; https://doi.org/10.3390/metabo12040284 - 24 Mar 2022
Cited by 9 | Viewed by 3369
Abstract
Patatin-like phospholipase domain-containing protein 6 (PNPLA6), originally called Neuropathy Target Esterase (NTE), belongs to a family of hydrolases with at least eight members in mammals. PNPLA6/NTE was first identified as a key factor in Organophosphate-induced delayed neuropathy, a degenerative syndrome that occurs after [...] Read more.
Patatin-like phospholipase domain-containing protein 6 (PNPLA6), originally called Neuropathy Target Esterase (NTE), belongs to a family of hydrolases with at least eight members in mammals. PNPLA6/NTE was first identified as a key factor in Organophosphate-induced delayed neuropathy, a degenerative syndrome that occurs after exposure to organophosphates found in pesticides and nerve agents. More recently, mutations in PNPLA6/NTE have been linked with a number of inherited diseases with diverse clinical symptoms that include spastic paraplegia, ataxia, and chorioretinal dystrophy. A conditional knockout of PNPLA6/NTE in the mouse brain results in age-related neurodegeneration, whereas a complete knockout causes lethality during embryogenesis due to defects in the development of the placenta. PNPLA6/NTE is an evolutionarily conserved protein that in Drosophila is called Swiss-Cheese (SWS). Loss of SWS in the fly also leads to locomotory defects and neuronal degeneration that progressively worsen with age. This review will describe the identification of PNPLA6/NTE, its expression pattern, and normal role in lipid homeostasis, as well as the consequences of altered NPLA6/NTE function in both model systems and patients. Full article
(This article belongs to the Special Issue Multipurpose Enzymes in Lipid Metabolism)
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