This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 3.0 License.
Long JZ, Cravatt BF. The metabolic hydrolases and their Functions in mammalian physiology and disease. Chem Rev 2011;111:6022–63. doi: 10.1021/cr200075yLongJZCravattBF. The metabolic hydrolases and their Functions in mammalian physiology and disease. Chem Rev2011;111:6022–63. doi: 10.1021/cr200075yOpen DOISearch in Google Scholar
Buller RB, Townsend CA. Intrinsic evolutionary constraints on protease structure, enzyme acylation, and the identity of the catalytic triad. Proc Natl Acad Sci U S A 2013;110(8):E653–61. doi: 10.1073/pnas.1221050110BullerRBTownsendCA. Intrinsic evolutionary constraints on protease structure, enzyme acylation, and the identity of the catalytic triad. Proc Natl Acad Sci U S A2013;110(8):E653–61. doi: 10.1073/pnas.1221050110Open DOISearch in Google Scholar
Botos I, Wlodawer A. The expanding diversity of serine hydrolases. Curr Opin Struct Biol 2007;17:683–90. doi: 10.1016/j.sbi.2007.08.003BotosIWlodawerA. The expanding diversity of serine hydrolases. Curr Opin Struct Biol2007;17:683–90. doi: 10.1016/j.sbi.2007.08.003Open DOISearch in Google Scholar
Kienesberger PC, Oberer M, Lass A, Zechner R. Mammalian patatin domain containing proteins: a family with diverse lipolytic activities involved in multiple biological functions. J Lipid Res 2009;50(Suppl):S63–8. doi: 10.1194/jlr.R800082-JLR200KienesbergerPCObererMLassAZechnerR. Mammalian patatin domain containing proteins: a family with diverse lipolytic activities involved in multiple biological functions. J Lipid Res2009;50(Suppl):S63–8. doi: 10.1194/jlr.R800082-JLR200Open DOISearch in Google Scholar
Wilson PA, Gardner SD, Lambie NM, Commans SA, Crowther DJ. Characterization of the human patatin-like phospholipase family. J Lipid Res 2006;47:1940–9. doi: 10.1194/jlr.M600185-JLR200WilsonPAGardnerSDLambieNMCommansSACrowtherDJ. Characterization of the human patatin-like phospholipase family. J Lipid Res2006;47:1940–9. doi: 10.1194/jlr.M600185-JLR200Open DOISearch in Google Scholar
Rydel TJ, Williams JM, Krieger E, Moshiri F, Stallings WC, Brown SM, Pershing JC, Purcell JP, Alibhai MF. The crystal structure, mutagenesis, and activity studies reveal that patatin is a lipid acyl hydrolase with a Ser-Asp catalytic dyad. Biochemistry 2003;42:6696–708. doi: 10.1021/bi027156rRydelTJWilliamsJMKriegerEMoshiriFStallingsWCBrownSMPershingJCPurcellJPAlibhaiMF. The crystal structure, mutagenesis, and activity studies reveal that patatin is a lipid acyl hydrolase with a Ser-Asp catalytic dyad. Biochemistry2003;42:6696–708. doi: 10.1021/bi027156rOpen DOISearch in Google Scholar
Wu J, Wu Q, Yang D, Zhou M, Xu J, Wen Q, Cui Y, Bai Y, Xu S, Wang Z, Wang S. Patatin primary structural properties and effects on lipid metabolism. Food Chem 2021;344:128661. doi: 10.1016/j.foodchem.2020.128661WuJWuQYangDZhouMXuJWenQCuiYBaiYXuSWangZWangS. Patatin primary structural properties and effects on lipid metabolism. Food Chem2021;344:128661. doi: 10.1016/j.foodchem.2020.128661Open DOISearch in Google Scholar
Wijeyesakere SJ, Richardson RJ, Stuckey JA. Crystal structure of patatin-17 in complex with aged and non-aged organophosphorus compounds. PLoS One 2014;9(9):e108245. doi: 10.1371/journal.pone.0108245WijeyesakereSJRichardsonRJStuckeyJA. Crystal structure of patatin-17 in complex with aged and non-aged organophosphorus compounds. PLoS One2014;9(9):e108245. doi: 10.1371/journal.pone.0108245Open DOISearch in Google Scholar
Kossiakoff AA, Spencer SA. Direct determination of the protonation states of aspartic acid-102 and Histidine-57 in the tetrahedral intermediate of the serine proteases: neutron, structure of trypsin. Biochemistry 1981;20:6462–74. doi: 10.1021/bi00525a027KossiakoffAASpencerSA. Direct determination of the protonation states of aspartic acid-102 and Histidine-57 in the tetrahedral intermediate of the serine proteases: neutron, structure of trypsin. Biochemistry1981;20:6462–74. doi: 10.1021/bi00525a027Open DOISearch in Google Scholar
Ramanadham S, Ali T, Ashley JW, Bone RN, Hancock WD, Lei X. Calcium-independent phospholipases A2 and their roles in biological processes and diseases. J Lipid Res 2015;56:1643–68. doi: 10.1194/jlr.R058701RamanadhamSAliTAshleyJWBoneRNHancockWDLeiX. Calcium-independent phospholipases A2 and their roles in biological processes and diseases. J Lipid Res2015;56:1643–68. doi: 10.1194/jlr.R058701Open DOISearch in Google Scholar
Holmes R. Comparative studies of adipose triglyceride lipase genes and proteins: an ancient gene in vertebrate evolution. Open Access Bioinformatics 2012;4:15–29. doi: 10.2147/OAB.S27508HolmesR. Comparative studies of adipose triglyceride lipase genes and proteins: an ancient gene in vertebrate evolution. Open Access Bioinformatics2012;4:15–29. doi: 10.2147/OAB.S27508Open DOISearch in Google Scholar
Dennis EA, Cao J, Hsu YH, Magrioti V, Kokotos G. Phospholipase A2 enzymes: physical structure, biological function, disease implication, chemical inhibition, and therapeutic intervention. Chem Rev 2011;111:6130–85. doi: 10.1021/cr200085wDennisEACaoJHsuYHMagriotiVKokotosG. Phospholipase A2 enzymes: physical structure, biological function, disease implication, chemical inhibition, and therapeutic intervention. Chem Rev2011;111:6130–85. doi: 10.1021/cr200085wOpen DOISearch in Google Scholar
Murakami M, Taketomi Y, Miki Y, Sato H, Hirabayashi T, Yamamoto K. Recent progress in phospholipase A2 research: from cells to animals to humans. Prog Lipid Res 2011;50:152–92. doi: 10.1016/j.plipres.2010.12.001MurakamiMTaketomiYMikiYSatoHHirabayashiTYamamotoK. Recent progress in phospholipase A2 research: from cells to animals to humans. Prog Lipid Res2011;50:152–92. doi: 10.1016/j.plipres.2010.12.001Open DOISearch in Google Scholar
Murakami M, Sato H, Taketomi Y. Updating phospholipase A2 biology. Biomolecules 2020;10(10):1457. doi: 10.3390/biom10101457MurakamiMSatoHTaketomiY. Updating phospholipase A2 biology. Biomolecules2020;10(10):1457. doi: 10.3390/biom10101457Open DOISearch in Google Scholar
Pingitore P, Romeo S. The role of PNPLA3 in health and disease. Biochim Biophys Acta Mol Cell Biol Lipids 2019;1864:900–6. doi: 10.1016/j.bbalip.2018.06.018PingitorePRomeoS. The role of PNPLA3 in health and disease. Biochim Biophys Acta Mol Cell Biol Lipids2019;1864:900–6. doi: 10.1016/j.bbalip.2018.06.018Open DOISearch in Google Scholar
Malley KR, Koroleva O, Miller I, Sanishvili R, Jenkins CM, Gross RW, Korolev S. The structure of iPLA2β reveals dimeric active sites and suggests mechanisms of regulation and localization. Nat Commun 2018;9(1):765. doi: 10.1038/s41467-018-03193-0MalleyKRKorolevaOMillerISanishviliRJenkinsCMGrossRWKorolevS. The structure of iPLA2β reveals dimeric active sites and suggests mechanisms of regulation and localization. Nat Commun2018;9(1):765. doi: 10.1038/s41467-018-03193-0Open DOISearch in Google Scholar
Chang PA, Sun YJ, Huang FF, Qin WZ, Chen YY, Zeng X, Wu YJ. Identification of human patatin-like phospholipase domain-containing protein 1 and a mutant in human cervical cancer HeLa cells. Mol Biol Rep 2013;40:5597–605. doi: 10.1007/s11033-013-2661-9ChangPASunYJHuangFFQinWZChenYYZengXWuYJ. Identification of human patatin-like phospholipase domain-containing protein 1 and a mutant in human cervical cancer HeLa cells. Mol Biol Rep2013;40:5597–605. doi: 10.1007/s11033-013-2661-9Open DOISearch in Google Scholar
Chang PA, Han LP, Sun LX, Huang FF. Identification mouse patatin-like phospholipase domain containing protein 1 as a skin-specific and membrane-associated protein. Gene 2016;591:344–50. doi: 10.1016/j.gene.2016.06.012ChangPAHanLPSunLXHuangFF. Identification mouse patatin-like phospholipase domain containing protein 1 as a skin-specific and membrane-associated protein. Gene2016;591:344–50. doi: 10.1016/j.gene.2016.06.012Open DOISearch in Google Scholar
Murugesan S, Goldberg EB, Dou E, Brown WJ. Identification of diverse lipid droplet targeting motifs in the PNPLA family of triglyceride lipases. PLoS One 2013;8(5):e64950. doi: 10.1371/journal.pone.0064950MurugesanSGoldbergEBDouEBrownWJ. Identification of diverse lipid droplet targeting motifs in the PNPLA family of triglyceride lipases. PLoS One2013;8(5):e64950. doi: 10.1371/journal.pone.0064950Open DOISearch in Google Scholar
Kien B, Grond S, Haemmerle G, Lass A, Eichmann TO, Radner FPW. ABHD5 stimulates PNPLA1-mediated ω-O-acylceramide biosynthesis essential for a functional skin permeability barrier. J Lipid Res 2018;59:2360–7. doi: 10.1194/jlr.M089771KienBGrondSHaemmerleGLassAEichmannTORadnerFPW. ABHD5 stimulates PNPLA1-mediated ω-O-acylceramide biosynthesis essential for a functional skin permeability barrier. J Lipid Res2018;59:2360–7. doi: 10.1194/jlr.M089771Open DOISearch in Google Scholar
Onal G, Kutlu O, Ozer E, Gozuacik D, Karaduman A, Dokmeci Emre S. Impairment of lipophagy by PNPLA1 mutations causes lipid droplet accumulation in primary fibroblasts of Autosomal Recessive Congenital Ichthyosis patients. J Dermatol Sci 2019;93:50–7. doi: 10.1016/j.jdermsci.2018.11.013OnalGKutluOOzerEGozuacikDKaradumanADokmeci EmreS. Impairment of lipophagy by PNPLA1 mutations causes lipid droplet accumulation in primary fibroblasts of Autosomal Recessive Congenital Ichthyosis patients. J Dermatol Sci2019;93:50–7. doi: 10.1016/j.jdermsci.2018.11.013Open DOISearch in Google Scholar
Walther TC, Farese RV Jr. Lipid droplets and cellular lipid metabolism. Annu Rev Biochem 2012;81:687–714. doi: 10.1146/annurev-biochem-061009-102430WaltherTCFareseRVJr. Lipid droplets and cellular lipid metabolism. Annu Rev Biochem2012;81:687–714. doi: 10.1146/annurev-biochem-061009-102430Open DOISearch in Google Scholar
Ohno Y, Nara A, Nakamichi S, Kihara A. Molecular mechanism of the ichthyosis pathology of Chanarin-Dorfman syndrome: Stimulation of PNPLA1-catalyzed ω-O-acylceramide production by ABHD5. J Dermatol Sci 2018;92:245–53. doi: 10.1016/j.jdermsci.2018.11.005OhnoYNaraANakamichiSKiharaA. Molecular mechanism of the ichthyosis pathology of Chanarin-Dorfman syndrome: Stimulation of PNPLA1-catalyzed ω-O-acylceramide production by ABHD5. J Dermatol Sci2018;92:245–53. doi: 10.1016/j.jdermsci.2018.11.005Open DOISearch in Google Scholar
Grall A, Guaguère E, Planchais S, Grond S, Bourrat E, Hausser I, Hitte C, Le Gallo M, Derbois C, Kim GJ, Lagoutte L, Degorce-Rubiales F, Radner FP, Thomas A, Küry S, Bensignor E, Fontaine J, Pin D, Zimmermann R, Zechner R, Lathrop M, Galibert F, André C, Fischer J. PNPLA1 mutations cause autosomal recessive congenital ichthyosis in golden retriever dogs and humans. Nat Genet 2012;44:140–7. doi: 10.1038/ng.1056GrallAGuaguèreEPlanchaisSGrondSBourratEHausserIHitteCLe GalloMDerboisCKimGJLagoutteLDegorce-RubialesFRadnerFPThomasAKürySBensignorEFontaineJPinDZimmermannRZechnerRLathropMGalibertFAndréCFischerJ. PNPLA1 mutations cause autosomal recessive congenital ichthyosis in golden retriever dogs and humans. Nat Genet2012;44:140–7. doi: 10.1038/ng.1056Open DOISearch in Google Scholar
Hirabayashi T, Anjo T, Kaneko A, Senoo Y, Shibata A, Takama H, Yokoyama K, Nishito Y, Ono T, Taya C, Muramatsu K, Fukami K, Muñoz-Garcia A, Brash AR, Ikeda K, Arita M, Akiyama M, Murakami M. PNPLA1 has a crucial role in skin barrier function by directing acylceramide biosynthesis. Nat Commun 2017;8:14609. doi: 10.1038/ncomms14609HirabayashiTAnjoTKanekoASenooYShibataATakamaHYokoyamaKNishitoYOnoTTayaCMuramatsuKFukamiKMuñoz-GarciaABrashARIkedaKAritaMAkiyamaMMurakamiM. PNPLA1 has a crucial role in skin barrier function by directing acylceramide biosynthesis. Nat Commun2017;8:14609. doi: 10.1038/ncomms14609Open DOISearch in Google Scholar
Grond S, Eichmann TO, Dubrac S, Kolb D, Schmuth M, Fischer J, Crumrine D, Elias PM, Haemmerle G, Zechner R, Lass A, Radner FPW. PNPLA1 deficiency in mice and humans leads to a defect in the synthesis of omega-O-acylceramides. J Invest Dermatol 2017;137:394–402. doi: 10.1016/j.jid.2016.08.036GrondSEichmannTODubracSKolbDSchmuthMFischerJCrumrineDEliasPMHaemmerleGZechnerRLassARadnerFPW. PNPLA1 deficiency in mice and humans leads to a defect in the synthesis of omega-O-acylceramides. J Invest Dermatol2017;137:394–402. doi: 10.1016/j.jid.2016.08.036Open DOISearch in Google Scholar
Ohno Y, Kamiyama N, Nakamichi S, Kihara A. PNPLA1 is a transacylase essential for the generation of the skin barrier lipid ω-O-acylceramide. Nat Commun 2017;8:14610. doi: 10.1038/ncomms14610OhnoYKamiyamaNNakamichiSKiharaA. PNPLA1 is a transacylase essential for the generation of the skin barrier lipid ω-O-acylceramide. Nat Commun2017;8:14610. doi: 10.1038/ncomms14610Open DOISearch in Google Scholar
Murakami M, Yamamoto K, Taketomi Y. Phospholipase A2 in skin biology: new insights from gene-manipulated mice and lipidomics. Inflamm Regen 2018;38:31. doi: 10.1186/s41232-018-0089-2MurakamiMYamamotoKTaketomiY. Phospholipase A2 in skin biology: new insights from gene-manipulated mice and lipidomics. Inflamm Regen2018;38:31. doi: 10.1186/s41232-018-0089-2Open DOISearch in Google Scholar
Radner FP, Grond S, Haemmerle G, Lass A, Zechner R. Fat in the skin: Triacylglycerol metabolism in keratinocytes and its role in the development of neutral lipid storage disease. Dermatoendocrinology 2011;3:77–83. doi: 10.4161/derm.3.2.15472RadnerFPGrondSHaemmerleGLassAZechnerR. Fat in the skin: Triacylglycerol metabolism in keratinocytes and its role in the development of neutral lipid storage disease. Dermatoendocrinology2011;3:77–83. doi: 10.4161/derm.3.2.15472Open DOISearch in Google Scholar
Lake AC, Sun Y, Li JL, Kim JE, Johnson JW, Li D, Revett T, Shih HH, Liu W, Paulsen JE, Gimeno RE. Expression, regulation, and triglyceride hydrolase activity of Adiponutrin family members. J Lipid Res 2005;46:2477–87. doi: 10.1194/jlr.M500290-JLR200LakeACSunYLiJLKimJEJohnsonJWLiDRevettTShihHHLiuWPaulsenJEGimenoRE. Expression, regulation, and triglyceride hydrolase activity of Adiponutrin family members. J Lipid Res2005;46:2477–87. doi: 10.1194/jlr.M500290-JLR200Open DOISearch in Google Scholar
Smirnova E, Goldberg EB, Makarova KS, Lin L, Brown WJ, Jackson CL. ATGL has a key role in lipid droplet/adiposome degradation in mammalian cells. EMBO Rep 2006;7:106–13. doi: 10.1038/sj.embor.7400559SmirnovaEGoldbergEBMakarovaKSLinLBrownWJJacksonCL. ATGL has a key role in lipid droplet/adiposome degradation in mammalian cells. EMBO Rep2006;7:106–13. doi: 10.1038/sj.embor.7400559Open DOISearch in Google Scholar
Cornaciu I, Boeszoermenyi A, Lindermuth H, Nagy HM, Cerk IK, Ebner C, Salzburger B, Gruber A, Schweiger M, Zechner R, Lass A, Zimmermann R, Oberer M. The minimal domain of adipose triglyceride lipase (ATGL) ranges until leucine 254 and can be activated and inhibited by CGI-58 and G0S2, respectively. PLoS ONE 2011;6(10):e26349. doi: 10.1371/journal.pone.0026349CornaciuIBoeszoermenyiALindermuthHNagyHMCerkIKEbnerCSalzburgerBGruberASchweigerMZechnerRLassAZimmermannRObererM. The minimal domain of adipose triglyceride lipase (ATGL) ranges until leucine 254 and can be activated and inhibited by CGI-58 and G0S2, respectively. PLoS ONE2011;6(10):e26349. doi: 10.1371/journal.pone.0026349Open DOISearch in Google Scholar
Zimmermann R, Lass A, Haemmerle G, Zechner R. Fate of fat: the role of adipose triglyceride lipase in lipolysis. Biochim Biophys Acta 2009;1791:494–500. doi: 10.1016/j.bbalip.2008.10.005ZimmermannRLassAHaemmerleGZechnerR. Fate of fat: the role of adipose triglyceride lipase in lipolysis. Biochim Biophys Acta2009;1791:494–500. doi: 10.1016/j.bbalip.2008.10.005Open DOISearch in Google Scholar
Zechner R, Kienesberger PC, Haemmerle G, Zimmermann R, Lass A. Adipose triglyceride lipase and the lipolytic catabolism of cellular fat stores. J Lipid Res 2009;50:3–21. doi: 10.1194/jlr.R800031-JLR200ZechnerRKienesbergerPCHaemmerleGZimmermannRLassA. Adipose triglyceride lipase and the lipolytic catabolism of cellular fat stores. J Lipid Res2009;50:3–21. doi: 10.1194/jlr.R800031-JLR200Open DOISearch in Google Scholar
Kershaw EE, Hamm JK, Verhagen LA, Peroni O, Katic M, Flier JS. Adipose triglyceride lipase: function, regulation by insulin, and comparison with adiponutrin. Diabetes 2006;55:148–57. doi: 10.2337/diabetes.55.01.06.db05-0982KershawEEHammJKVerhagenLAPeroniOKaticMFlierJS. Adipose triglyceride lipase: function, regulation by insulin, and comparison with adiponutrin. Diabetes2006;55:148–57. doi: 10.2337/diabetes.55.01.06.db05-0982Open DOISearch in Google Scholar
Kienesberger PC, Lee D, Pulinilkunnil T, Brenner DS, Cai L, Magnes C, Koefeler HC, Streith IE, Rechberger GN, Haemmerle G, Flier JS, Zechner R, Kim YB, Kershaw EE. Adipose triglyceride lipase deficiency causes tissue-specific changes in insulin signaling. J Biol Chem 2009;284:30218–29. doi: 10.1074/jbc.M109.047787KienesbergerPCLeeDPulinilkunnilTBrennerDSCaiLMagnesCKoefelerHCStreithIERechbergerGNHaemmerleGFlierJSZechnerRKimYBKershawEE. Adipose triglyceride lipase deficiency causes tissue-specific changes in insulin signaling. J Biol Chem2009;284:30218–29. doi: 10.1074/jbc.M109.047787Open DOISearch in Google Scholar
Schreiber R, Xie H, Schweiger M. Of mice and men: The physiological role of adipose triglyceride lipase (ATGL). Biochim Biophys Acta Mol Cell Biol Lipids 2019;1864:880–99. doi: 10.1016/j.bbalip.2018.10.008SchreiberRXieHSchweigerM. Of mice and men: The physiological role of adipose triglyceride lipase (ATGL). Biochim Biophys Acta Mol Cell Biol Lipids2019;1864:880–99. doi: 10.1016/j.bbalip.2018.10.008Open DOISearch in Google Scholar
Jenkins CM, Mancuso DJ, Yan W, Sims HF, Gibson B, Gross RW. Identification, cloning, expression, and purification of three novel human calcium-independent phospholipase A2 family members possessing triacylglycerol lipase and acylglycerol transacylase activities. J Biol Chem 2004;279:48968–75. doi: 10.1074/jbc.M407841200JenkinsCMMancusoDJYanWSimsHFGibsonBGrossRW. Identification, cloning, expression, and purification of three novel human calcium-independent phospholipase A2 family members possessing triacylglycerol lipase and acylglycerol transacylase activities. J Biol Chem2004;279:48968–75. doi: 10.1074/jbc.M407841200Open DOISearch in Google Scholar
Lass A, Zimmermann R, Oberer M, Zechner R. Lipolysis - a highly regulated multi-enzyme complex mediates the catabolism of cellular fat stores. Prog Lipid Res 2011;50:14–27. doi: 10.1016/j.plipres.2010.10.004LassAZimmermannRObererMZechnerR. Lipolysis - a highly regulated multi-enzyme complex mediates the catabolism of cellular fat stores. Prog Lipid Res2011;50:14–27. doi: 10.1016/j.plipres.2010.10.004Open DOISearch in Google Scholar
Zechner R, Zimmermann R, Eichmann TO, Kohlwein SD, Haemmerle G, Lass A, Madeo F. FAT SIGNALS - lipases and lipolysis in lipid metabolism and signaling. Cell Metab 2012;15:279–91. doi: 10.1016/j.cmet.2011.12.018ZechnerRZimmermannREichmannTOKohlweinSDHaemmerleGLassAMadeoF. FAT SIGNALS - lipases and lipolysis in lipid metabolism and signaling. Cell Metab2012;15:279–91. doi: 10.1016/j.cmet.2011.12.018Open DOISearch in Google Scholar
Schneider G, Neuberger G, Wildpaner M, Tian S, Berezovsky I, Eisenhaber F. Application of a sensitive collection heuristic for very large protein families: evolutionary relationship between adipose triglyceride lipase (ATGL) and classic mammalian lipases. BMC Bioinformatics 2006;7:164. doi: 10.1186/1471-2105-7-164SchneiderGNeubergerGWildpanerMTianSBerezovskyIEisenhaberF. Application of a sensitive collection heuristic for very large protein families: evolutionary relationship between adipose triglyceride lipase (ATGL) and classic mammalian lipases. BMC Bioinformatics2006;7:164. doi: 10.1186/1471-2105-7-164Open DOISearch in Google Scholar
Taschler U, Schreiber R, Chitraju C, Grabner GF, Romauch M, Wolinski H, Haemmerle G, Breinbauer R, Zechner R, Lass A, Zimmermann R. Adipose triglyceride lipase is involved in the mobilization of triglyceride and retinoid stores of hepatic stellate cells. Biochim Biophys Acta 2015;1851:937–45. doi: 10.1016/j.bbalip.2015.02.017TaschlerUSchreiberRChitrajuCGrabnerGFRomauchMWolinskiHHaemmerleGBreinbauerRZechnerRLassAZimmermannR. Adipose triglyceride lipase is involved in the mobilization of triglyceride and retinoid stores of hepatic stellate cells. Biochim Biophys Acta2015;1851:937–45. doi: 10.1016/j.bbalip.2015.02.017Open DOISearch in Google Scholar
Patel R, Santoro A, Hofer P, Tan D, Oberer M, Nelson AT, Konduri S, Siegel D, Zechner R, Saghatelian A, Kahn BB. ATGL is a biosynthetic enzyme for fatty acid esters of hydroxy fatty acids. Nature 2022;606:968–75. doi: 10.1038/s41586-022-04787-xPatelRSantoroAHoferPTanDObererMNelsonATKonduriSSiegelDZechnerRSaghatelianAKahnBB. ATGL is a biosynthetic enzyme for fatty acid esters of hydroxy fatty acids. Nature2022;606:968–75. doi: 10.1038/s41586-022-04787-xOpen DOISearch in Google Scholar
Schweiger M, Lass A, Zimmermann R, Eichmann TO, Zechner R. Neutral lipid storage disease: genetic disorders caused by mutations in adipose triglyceride lipase/PNPLA2 or CGI-58/ABHD5. Am J Physiol Endocrinol Metab 2009;297(2):E289–96. doi: 10.1152/ajpendo.00099.200SchweigerMLassAZimmermannREichmannTOZechnerR. Neutral lipid storage disease: genetic disorders caused by mutations in adipose triglyceride lipase/PNPLA2 or CGI-58/ABHD5. Am J Physiol Endocrinol Metab2009;297(2):E289–96. doi: 10.1152/ajpendo.00099.200Open DOISearch in Google Scholar
Kulminskaya N, Oberer M. Protein-protein interactions regulate the activity of Adipose Triglyceride Lipase in intracellular lipolysis. Biochimie 2020;169:62–8. doi: 10.1016/j.biochi.2019.08.004KulminskayaNObererM. Protein-protein interactions regulate the activity of Adipose Triglyceride Lipase in intracellular lipolysis. Biochimie2020;169:62–8. doi: 10.1016/j.biochi.2019.08.004Open DOISearch in Google Scholar
Eichmann TO, Kumari M, Haas JT, Farese RV Jr, Zimmermann R, Lass A, Zechner R. Studies on the substrate and stereo/regioselectivity of adipose triglyceride lipase, hormone-sensitive lipase, and diacylglycerol-O-acyltransferases. J Biol Chem 2012;287:41446–57. doi: 10.1074/jbc.M112.400416EichmannTOKumariMHaasJTFareseRVJrZimmermannRLassAZechnerR. Studies on the substrate and stereo/regioselectivity of adipose triglyceride lipase, hormone-sensitive lipase, and diacylglycerol-O-acyltransferases. J Biol Chem2012;287:41446–57. doi: 10.1074/jbc.M112.400416Open DOISearch in Google Scholar
Yang A, Mottillo EP. Adipocyte lipolysis: from molecular mechanisms of regulation to disease and therapeutics. Biochem J 2020;477:985–1008. doi: 10.1042/BCJ20190468YangAMottilloEP. Adipocyte lipolysis: from molecular mechanisms of regulation to disease and therapeutics. Biochem J2020;477:985–1008. doi: 10.1042/BCJ20190468Open DOISearch in Google Scholar
Nagy HM, Paar M, Heier C, Moustafa T, Hofer P, Haemmerle G, Lass A, Zechner R, Oberer M, Zimmermann R. Adipose triglyceride lipase activity is inhibited by long-chain acyl-coenzyme A. Biochim Biophys Acta 2014;1841:588–94. doi: 10.1016/j.bbalip.2014.01.005NagyHMPaarMHeierCMoustafaTHoferPHaemmerleGLassAZechnerRObererMZimmermannR. Adipose triglyceride lipase activity is inhibited by long-chain acyl-coenzyme A. Biochim Biophys Acta2014;1841:588–94. doi: 10.1016/j.bbalip.2014.01.005Open DOISearch in Google Scholar
Granneman JG, Moore HP, Mottillo EP, Zhu Z, Zhou L. Interactions of perilipin-5 (Plin5) with adipose triglyceride lipase. J Biol Chem 2011;286:5126–35. doi: 10.1074/jbc.M110.180711GrannemanJGMooreHPMottilloEPZhuZZhouL. Interactions of perilipin-5 (Plin5) with adipose triglyceride lipase. J Biol Chem2011;286:5126–35. doi: 10.1074/jbc.M110.180711Open DOISearch in Google Scholar
Fuchs CD, Radun R, Dixon ED, Mlitz V, Timelthaler G, Halilbasic E, Herac M, Jonker JW, Ronda OAHO, Tardelli M, Haemmerle G, Zimmermann R, Scharnagl H, Stojakovic T, Verkade HJ, Trauner M. Hepatocyte-specific deletion of adipose triglyceride lipase (adipose triglyceride lipase/patatin-like phospholipase domain containing 2) ameliorates dietary induced steatohepatitis in mice. Hepatology 2022;75:125–39. doi: 10.1002/hep.32112FuchsCDRadunRDixonEDMlitzVTimelthalerGHalilbasicEHeracMJonkerJWRondaOAHOTardelliMHaemmerleGZimmermannRScharnaglHStojakovicTVerkadeHJTraunerM. Hepatocyte-specific deletion of adipose triglyceride lipase (adipose triglyceride lipase/patatin-like phospholipase domain containing 2) ameliorates dietary induced steatohepatitis in mice. Hepatology2022;75:125–39. doi: 10.1002/hep.32112Open DOISearch in Google Scholar
Xie H, Heier C, Kien B, Vesely PW, Tang Z, Sexl V, Schoiswohl G, Strießnig-Bina I, Hoefler G, Zechner R, Schweiger M. Adipose triglyceride lipase activity regulates cancer cell proliferation via AMP-kinase and mTOR signaling. Biochim Biophys Acta Mol Cell Biol Lipids 2020;1865(9):158737. doi: 10.1016/j.bbalip.2020.158737XieHHeierCKienBVeselyPWTangZSexlVSchoiswohlGStrießnig-BinaIHoeflerGZechnerRSchweigerM. Adipose triglyceride lipase activity regulates cancer cell proliferation via AMP-kinase and mTOR signaling. Biochim Biophys Acta Mol Cell Biol Lipids2020;1865(9):158737. doi: 10.1016/j.bbalip.2020.158737Open DOISearch in Google Scholar
Schweiger M, Romauch M, Schreiber R, Grabner GF, Hütter S, Kotzbeck P, Benedikt P, Eichmann TO, Yamada S, Knittelfelder O, Diwoky C, Doler C, Mayer N, De Cecco W, Breinbauer R, Zimmermann R, Zechner R. Pharmacological inhibition of adipose triglyceride lipase corrects high-fat diet-induced insulin resistance and hepatosteatosis in mice. Nat Commun 2017;8:14859. doi: 10.1038/ncomms14859SchweigerMRomauchMSchreiberRGrabnerGFHütterSKotzbeckPBenediktPEichmannTOYamadaSKnittelfelderODiwokyCDolerCMayerNDe CeccoWBreinbauerRZimmermannRZechnerR. Pharmacological inhibition of adipose triglyceride lipase corrects high-fat diet-induced insulin resistance and hepatosteatosis in mice. Nat Commun2017;8:14859. doi: 10.1038/ncomms14859Open DOISearch in Google Scholar
Yin H, Li W, Mo L, Deng S, Lin W, Ma C, Luo Z, Luo C, Hong H. Adipose triglyceride lipase promotes the proliferation of colorectal cancer cells via enhancing the lipolytic pathway. J Cell Mol Med 2021;25:3963–75. doi: 10.1111/jcmm.16349YinHLiWMoLDengSLinWMaCLuoZLuoCHongH. Adipose triglyceride lipase promotes the proliferation of colorectal cancer cells via enhancing the lipolytic pathway. J Cell Mol Med2021;25:3963–75. doi: 10.1111/jcmm.16349Open DOISearch in Google Scholar
Liu X, Liang Y, Song R, Yang G, Han J, Lan Y, Pan S, Zhu M, Liu Y, Wang Y, Meng F, Cui Y, Wang J, Zhang B, Song X, Lu Z, Zheng T, Liu L. Long non-coding RNA NEAT1-modulated abnormal lipolysis via ATGL drives hepatocellular carcinoma proliferation. Mol Cancer 2018;17(1):90. doi: 10.1186/s12943-018-0838-5LiuXLiangYSongRYangGHanJLanYPanSZhuMLiuYWangYMengFCuiYWangJZhangBSongXLuZZhengTLiuL. Long non-coding RNA NEAT1-modulated abnormal lipolysis via ATGL drives hepatocellular carcinoma proliferation. Mol Cancer2018;17(1):90. doi: 10.1186/s12943-018-0838-5Open DOISearch in Google Scholar
Liu M, Yu X, Lin L, Deng J, Wang K, Xia Y, Tang X, Hong H. ATGL promotes the proliferation of hepatocellular carcinoma cells via the p-AKT signaling pathway. J Biochem Mol Toxicol 2019;33(11):e22391. doi: 10.1002/jbt.22391LiuMYuXLinLDengJWangKXiaYTangXHongH. ATGL promotes the proliferation of hepatocellular carcinoma cells via the p-AKT signaling pathway. J Biochem Mol Toxicol2019;33(11):e22391. doi: 10.1002/jbt.22391Open DOISearch in Google Scholar
Li P, Lu M, Shi J, Gong Z, Hua L, Li Q, Lim B, Zhang XH, Chen X, Li S, Shultz LD, Ren G. Lung mesenchymal cells elicit lipid storage in neutrophils that fuel breast cancer lung metastasis. Nat Immunol 2020;21:1444–55. doi: 10.1038/s41590-020-0783-5LiPLuMShiJGongZHuaLLiQLimBZhangXHChenXLiSShultzLDRenG. Lung mesenchymal cells elicit lipid storage in neutrophils that fuel breast cancer lung metastasis. Nat Immunol2020;21:1444–55. doi: 10.1038/s41590-020-0783-5Open DOISearch in Google Scholar
Gong Z, Li Q, Shi J, Liu ET, Shultz LD, Ren G. Lipid-laden lung mesenchymal cells foster breast cancer metastasis via metabolic reprogramming of tumor cells and natural killer cells. Cell Metab 2022;34(12):1960–1976.e9. doi: 10.1016/j.cmet.2022.11.003GongZLiQShiJLiuETShultzLDRenG. Lipid-laden lung mesenchymal cells foster breast cancer metastasis via metabolic reprogramming of tumor cells and natural killer cells. Cell Metab2022;34(12):1960–1976.e9. doi: 10.1016/j.cmet.2022.11.003Open DOISearch in Google Scholar
Kumari M, Schoiswohl G, Chitraju C, Paar M, Cornaciu I, Rangrez AY, Wongsiriroj N, Nagy HM, Ivanova PT, Scott SA, Knittelfelder O, Rechberger GN, Birner-Gruenberger R, Eder S, Brown HA, Haemmerle G, Oberer M, Lass A, Kershaw EE, Zimmermann R, Zechner R. Adiponutrin functions as a nutritionally regulated lysophosphatidic acid acyltransferase. Cell Metab 2012;15:691–702. doi: 10.1016/j.cmet.2012.04.008KumariMSchoiswohlGChitrajuCPaarMCornaciuIRangrezAYWongsirirojNNagyHMIvanovaPTScottSAKnittelfelderORechbergerGNBirner-GruenbergerREderSBrownHAHaemmerleGObererMLassAKershawEEZimmermannRZechnerR. Adiponutrin functions as a nutritionally regulated lysophosphatidic acid acyltransferase. Cell Metab2012;15:691–702. doi: 10.1016/j.cmet.2012.04.008Open DOISearch in Google Scholar
Yang A, Mottillo EP, Mladenovic-Lucas L, Zhou L, Granneman JG. Dynamic interactions of ABHD5 with PNPLA3 regulate triacylglycerol metabolism in brown adipocytes. Nat Metab 2019;1:560–9. doi: 10.1038/s42255-019-0066-3YangAMottilloEPMladenovic-LucasLZhouLGrannemanJG. Dynamic interactions of ABHD5 with PNPLA3 regulate triacylglycerol metabolism in brown adipocytes. Nat Metab2019;1:560–9. doi: 10.1038/s42255-019-0066-3Open DOISearch in Google Scholar
Chamoun Z, Vacca F, Parton RG, Gruenberg J. PNPLA3/adiponutrin functions in lipid droplet formation. Biol Cell 2013;105:219–33. doi: 10.1111/boc.201200036ChamounZVaccaFPartonRGGruenbergJ. PNPLA3/adiponutrin functions in lipid droplet formation. Biol Cell2013;105:219–33. doi: 10.1111/boc.201200036Open DOISearch in Google Scholar
Wang Y, Kory N, BasuRay S, Cohen JC, Hobbs HH. PNPLA3, CGI-58, and inhibition of hepatic triglyceride hydrolysis in mice. Hepatology 2019;69:2427–41. doi: 10.1002/hep.30583WangYKoryNBasuRaySCohenJCHobbsHH. PNPLA3, CGI-58, and inhibition of hepatic triglyceride hydrolysis in mice. Hepatology2019;69:2427–41. doi: 10.1002/hep.30583Open DOISearch in Google Scholar
Dong XC. PNPLA3-A potential therapeutic target for personalized treatment of chronic liver disease. Front Med (Lausanne) 2019;6:304. doi: 10.3389/fmed.2019.00304DongXC. PNPLA3-A potential therapeutic target for personalized treatment of chronic liver disease. Front Med (Lausanne)2019;6:304. doi: 10.3389/fmed.2019.00304Open DOISearch in Google Scholar
Winberg ME, Motlagh MK, Stenkula KG, Holm C, Jones HA. Adiponutrin: a multimeric plasma protein. Biochem Biophys Res Commun 2014;446:1114–9. doi: 10.1016/j.bbrc.2014.03.078WinbergMEMotlaghMKStenkulaKGHolmCJonesHA. Adiponutrin: a multimeric plasma protein. Biochem Biophys Res Commun2014;446:1114–9. doi: 10.1016/j.bbrc.2014.03.078Open DOISearch in Google Scholar
Ruhanen H, Perttilä J, Hölttä-Vuori M, Zhou Y, Yki-Järvinen H, Ikonen E, Käkelä R, Olkkonen VM. PNPLA3 mediates hepatocyte triacylglycerol remodeling. J Lipid Res 2014;55:739–46. doi: 10.1194/jlr.M046607RuhanenHPerttiläJHölttä-VuoriMZhouYYki-JärvinenHIkonenEKäkeläROlkkonenVM. PNPLA3 mediates hepatocyte triacylglycerol remodeling. J Lipid Res2014;55:739–46. doi: 10.1194/jlr.M046607Open DOISearch in Google Scholar
BasuRay S, Wang Y, Smagris E, Cohen JC, Hobbs HH. Accumulation of PNPLA3 on lipid droplets is the basis of associated hepatic steatosis. Proc Natl Acad Sci U S A 2019;116:9521–6. doi: 10.1073/pnas.190197411BasuRaySWangYSmagrisECohenJCHobbsHH. Accumulation of PNPLA3 on lipid droplets is the basis of associated hepatic steatosis. Proc Natl Acad Sci U S A2019;116:9521–6. doi: 10.1073/pnas.190197411Open DOISearch in Google Scholar
Yuan S, Liu H, Yuan D, Xu J, Chen Y, Xu X, Xu F, Liang H. PNPLA3 I148M mediates the regulatory effect of NF-kB on inflammation in PA-treated HepG2 cells. J Cell Mol Med 2020;24:1541–52. doi: 10.1111/jcmm.14839YuanSLiuHYuanDXuJChenYXuXXuFLiangH. PNPLA3 I148M mediates the regulatory effect of NF-kB on inflammation in PA-treated HepG2 cells. J Cell Mol Med2020;24:1541–52. doi: 10.1111/jcmm.14839Open DOISearch in Google Scholar
Park J, Zhao Y, Zhang F, Zhang S, Kwong AC, Zhang Y, Hoffmann HH, Bushweller L, Wu X, Ashbrook AW, Stefanovic B, Chen S, Branch AD, Mason CE, Jung JU, Rice CM, Wu X. IL-6/STAT3 axis dictates the PNPLA3-mediated susceptibility to non-alcoholic fatty liver disease. J Hepatol 2023;78:45–56. doi: 10.1016/j.jhep.2022.08.022ParkJZhaoYZhangFZhangSKwongACZhangYHoffmannHHBushwellerLWuXAshbrookAWStefanovicBChenSBranchADMasonCEJungJURiceCMWuX. IL-6/STAT3 axis dictates the PNPLA3-mediated susceptibility to non-alcoholic fatty liver disease. J Hepatol2023;78:45–56. doi: 10.1016/j.jhep.2022.08.022Open DOISearch in Google Scholar
BasuRay S, Smagris E, Cohen JC, Hobbs HH. The PNPLA3 variant associated with fatty liver disease (I148M) accumulates on lipid droplets by evading ubiquitylation. Hepatology 2017;66:1111–24. doi: 10.1002/hep.29273BasuRaySSmagrisECohenJCHobbsHH. The PNPLA3 variant associated with fatty liver disease (I148M) accumulates on lipid droplets by evading ubiquitylation. Hepatology2017;66:1111–24. doi: 10.1002/hep.29273Open DOISearch in Google Scholar
Witzel HR, Schwittai IMG, Hartmann N, Mueller S, Schattenberg JM, Gong XM, Backs J, Schirmacher P, Schuppan D, Roth W, Straub BK. PNPLA3(I148M) inhibits lipolysis by perilipin-5-dependent competition with ATGL. Cells 2022;12(1):73. doi: 10.3390/cells12010073WitzelHRSchwittaiIMGHartmannNMuellerSSchattenbergJMGongXMBacksJSchirmacherPSchuppanDRothWStraubBK. PNPLA3(I148M) inhibits lipolysis by perilipin-5-dependent competition with ATGL. Cells2022;12(1):73. doi: 10.3390/cells12010073Open DOISearch in Google Scholar
Valenti L, Dongiovanni P. Mutant PNPLA3 I148M protein as pharmacological target for liver disease. Hepatology 2017;66:1026–8. doi: 10.1002/hep.29298ValentiLDongiovanniP. Mutant PNPLA3 I148M protein as pharmacological target for liver disease. Hepatology2017;66:1026–8. doi: 10.1002/hep.29298Open DOISearch in Google Scholar
McHenry S, Davidson NO. Missense mutant patatin-like phospholipase domain containing 3 alters lipid droplet turnover in partnership with CGI-58. Hepatology 2019;69:2323–5. doi: 10.1002/hep.30620McHenrySDavidsonNO. Missense mutant patatin-like phospholipase domain containing 3 alters lipid droplet turnover in partnership with CGI-58. Hepatology2019;69:2323–5. doi: 10.1002/hep.30620Open DOISearch in Google Scholar
Gao J, Simon M. Identification of a novel keratinocyte retinyl ester hydrolase as a transacylase and lipase. J Invest Dermatol 2005;124:1259–66. doi: 10.1111/j.0022-202X.2005.23761.xGaoJSimonM. Identification of a novel keratinocyte retinyl ester hydrolase as a transacylase and lipase. J Invest Dermatol2005;124:1259–66. doi: 10.1111/j.0022-202X.2005.23761.xOpen DOISearch in Google Scholar
Schreiber R, Taschler U, Preiss-Landl K, Wongsiriroj N, Zimmermann R, Lass A. Retinyl ester hydrolases and their roles in vitamin A homeostasis. Biochim Biophys Acta 2012;1821:113–23. doi: 10.1016/j.bbalip.2011.05.001SchreiberRTaschlerUPreiss-LandlKWongsirirojNZimmermannRLassA. Retinyl ester hydrolases and their roles in vitamin A homeostasis. Biochim Biophys Acta2012;1821:113–23. doi: 10.1016/j.bbalip.2011.05.001Open DOISearch in Google Scholar
Gao JG, Simon M. Molecular screening for GS2 lipase regulators: inhibition of keratinocyte retinylester hydrolysis by TIP47. J Invest Dermatol 2006;126:2087–95. doi: 10.1038/sj.jid.5700327GaoJGSimonM. Molecular screening for GS2 lipase regulators: inhibition of keratinocyte retinylester hydrolysis by TIP47. J Invest Dermatol2006;126:2087–95. doi: 10.1038/sj.jid.5700327Open DOISearch in Google Scholar
Gao JG, Shih A, Gruber R, Schmuth M, Simon M. GS2 as a retinol transacylase and as a catalytic dyad independent regulator of retinylester accretion. Mol Genet Metab 2009;96:253–60. doi: 10.1016/j.ymgme.2008.12.007GaoJGShihAGruberRSchmuthMSimonM. GS2 as a retinol transacylase and as a catalytic dyad independent regulator of retinylester accretion. Mol Genet Metab2009;96:253–60. doi: 10.1016/j.ymgme.2008.12.007Open DOISearch in Google Scholar
Holmes RS. Vertebrate patatin-like phospholipase domain-containing protein 4 (PNPLA4) genes and proteins: a gene with a role in retinol metabolism. 3 Biotech 2012;2:277–86. doi: 10.1007/s13205-012-0063-7HolmesRS. Vertebrate patatin-like phospholipase domain-containing protein 4 (PNPLA4) genes and proteins: a gene with a role in retinol metabolism. 3 Biotech2012;2:277–86. doi: 10.1007/s13205-012-0063-7Open DOISearch in Google Scholar
Yang L, Qian G, Xue Z, Lei H, Kui X, Yan-Qing H, Lan L, Yu-Lian M, Kui L. PNPLA5-knockout rats induced by CRISPR/Cas9 exhibit abnormal bleeding and lipid level. J Integr Agric 2017;16:169–80. doi: 10.1016/S2095-3119(16)61437-5YangLQianGXueZLeiHKuiXYan-QingHLanLYu-LianMKuiL. PNPLA5-knockout rats induced by CRISPR/Cas9 exhibit abnormal bleeding and lipid level. J Integr Agric2017;16:169–80. doi: 10.1016/S2095-3119(16)61437-5Open DOISearch in Google Scholar
Dupont N, Chauhan S, Arko-Mensah J, Castillo EF, Masedunskas A, Weigert R, Robenek H, Proikas-Cezanne T, Deretic V. Neutral lipid stores and lipase PNPLA5 contribute to autophagosome biogenesis. Curr Biol 2014;24:609–20. doi: 10.1016/j.cub.2014.02.008DupontNChauhanSArko-MensahJCastilloEFMasedunskasAWeigertRRobenekHProikas-CezanneTDereticV. Neutral lipid stores and lipase PNPLA5 contribute to autophagosome biogenesis. Curr Biol2014;24:609–20. doi: 10.1016/j.cub.2014.02.008Open DOISearch in Google Scholar
Ward C, Martinez-Lopez N, Otten EG, Carroll B, Maetzel D, Singh R, Sarkar S, Korolchuk VI. Autophagy, lipophagy and lysosomal lipid storage disorders. Biochim Biophys Acta 2016;1861:269–84. doi: 10.1016/j.bbalip.2016.01.006WardCMartinez-LopezNOttenEGCarrollBMaetzelDSinghRSarkarSKorolchukVI. Autophagy, lipophagy and lysosomal lipid storage disorders. Biochim Biophys Acta2016;1861:269–84. doi: 10.1016/j.bbalip.2016.01.006Open DOISearch in Google Scholar
Zhang Y, Whaley-Connell AT, Sowers JR, Ren J. Autophagy as an emerging target in cardiorenal metabolic disease: from pathophysiology to management. Pharmacol Ther 2018;191:1–22. doi: 10.1016/j.pharmthera.2018.06.004ZhangYWhaley-ConnellATSowersJRRenJ. Autophagy as an emerging target in cardiorenal metabolic disease: from pathophysiology to management. Pharmacol Ther2018;191:1–22. doi: 10.1016/j.pharmthera.2018.06.004Open DOISearch in Google Scholar
Cingolani F, Czaja MJ. Regulation and functions of autophagic lipolysis. Trends Endocrinol Metab 2016;27:696–705. doi: 10.1016/j.tem.2016.06.003CingolaniFCzajaMJ. Regulation and functions of autophagic lipolysis. Trends Endocrinol Metab2016;27:696–705. doi: 10.1016/j.tem.2016.06.003Open DOISearch in Google Scholar
Richardson RJ, Hein ND, Wijeyesakere SJ, Fink JK, Makhaeva GF. Neuropathy target esterase (NTE): overview and future. Chem Biol Interact 2013;203:238–44. doi: 10.1016/j.cbi.2012.10.024RichardsonRJHeinNDWijeyesakereSJFinkJKMakhaevaGF. Neuropathy target esterase (NTE): overview and future. Chem Biol Interact2013;203:238–44. doi: 10.1016/j.cbi.2012.10.024Open DOISearch in Google Scholar
Chang PA, Wu YJ. Neuropathy target esterase: an essential enzyme for neural development and axonal maintenance. Int J Biochem Cell Biol 2010;42:573–5. doi: 10.1016/j.biocel.2009.12.007ChangPAWuYJ. Neuropathy target esterase: an essential enzyme for neural development and axonal maintenance. Int J Biochem Cell Biol2010;42:573–5. doi: 10.1016/j.biocel.2009.12.007Open DOISearch in Google Scholar
Chen JX, Long DX, Hou WY, Li W, Wu YJ. Regulation of neuropathy target esterase by the cAMP/protein kinase A signal. Pharmacol Res 2010;62:259–64. doi: 10.1016/j.phrs.2010.03.006ChenJXLongDXHouWYLiWWuYJ. Regulation of neuropathy target esterase by the cAMP/protein kinase A signal. Pharmacol Res2010;62:259–64. doi: 10.1016/j.phrs.2010.03.006Open DOISearch in Google Scholar
Wijeyesakere SJ, Richardson RJ, Stuckey JA. Modeling the tertiary structure of the patatin domain of neuropathy target esterase. Protein J 2007;26:165–72. doi: 10.1007/s10930-006-9058-8WijeyesakereSJRichardsonRJStuckeyJA. Modeling the tertiary structure of the patatin domain of neuropathy target esterase. Protein J2007;26:165–72. doi: 10.1007/s10930-006-9058-8Open DOISearch in Google Scholar
Chang P, He L, Wang Y, Heier C, Wu Y, Huang F. Characterization of the interaction of neuropathy target esterase with the endoplasmic reticulum and lipid droplets. Biomolecules 2019;9(12):848. doi: 10.3390/biom9120848ChangPHeLWangYHeierCWuYHuangF. Characterization of the interaction of neuropathy target esterase with the endoplasmic reticulum and lipid droplets. Biomolecules2019;9(12):848. doi: 10.3390/biom9120848Open DOISearch in Google Scholar
Sogorb MA, Pamies D, Estevan C, Estévez J, Vilanova E. Roles of NTE protein and encoding gene in development and neurodevelopmental toxicity. Chem Biol Interact 2016;259(Pt B):352–7. doi: 10.1016/j.cbi.2016.07.030SogorbMAPamiesDEstevanCEstévezJVilanovaE. Roles of NTE protein and encoding gene in development and neurodevelopmental toxicity. Chem Biol Interact2016;259(Pt B):352–7. doi: 10.1016/j.cbi.2016.07.030Open DOISearch in Google Scholar
Vose SC, Fujioka K, Gulevich AG, Lin AY, Holland NT, Casida JE. Cellular function of neuropathy target esterase in lysophosphatidylcholine action. Toxicol Appl Pharmacol 2008;232:376–83. doi: 10.1016/j.taap.2008.07.015VoseSCFujiokaKGulevichAGLinAYHollandNTCasidaJE. Cellular function of neuropathy target esterase in lysophosphatidylcholine action. Toxicol Appl Pharmacol2008;232:376–83. doi: 10.1016/j.taap.2008.07.015Open DOISearch in Google Scholar
Greiner AJ, Richardson RJ, Worden RM, Ofoli RY. Influence of lysophospholipid hydrolysis by the catalytic domain of neuropathy target esterase on the fluidity of bilayer lipid membranes. Biochim Biophys Acta 2010;1798:1533–9. doi: 10.1016/j.bbamem.2010.03.015GreinerAJRichardsonRJWordenRMOfoliRY. Influence of lysophospholipid hydrolysis by the catalytic domain of neuropathy target esterase on the fluidity of bilayer lipid membranes. Biochim Biophys Acta2010;1798:1533–9. doi: 10.1016/j.bbamem.2010.03.015Open DOISearch in Google Scholar
Hein ND, Stuckey JA, Rainier SR, Fink JK, Richardson RJ. Constructs of human neuropathy target esterase catalytic domain containing mutations related to motor neuron disease have altered enzymatic properties. Toxicol Lett 2010;196:67–73. doi: 10.1016/j.toxlet.2010.03.1120HeinNDStuckeyJARainierSRFinkJKRichardsonRJ. Constructs of human neuropathy target esterase catalytic domain containing mutations related to motor neuron disease have altered enzymatic properties. Toxicol Lett2010;196:67–73. doi: 10.1016/j.toxlet.2010.03.1120Open DOISearch in Google Scholar
Pamies D, Bal-Price A, Fabbri M, Gribaldo L, Scelfo B, Harris G, Collotta A, Vilanova E, Sogorb MA. Silencing of PNPLA6, the neuropathy target esterase (NTE) codifying gene, alters neurodifferentiation of human embryonal carcinoma stem cells (NT2). Neuroscience 2014;281:54–67. doi: 10.1016/j.neuroscience.2014.08.031PamiesDBal-PriceAFabbriMGribaldoLScelfoBHarrisGCollottaAVilanovaESogorbMA. Silencing of PNPLA6, the neuropathy target esterase (NTE) codifying gene, alters neurodifferentiation of human embryonal carcinoma stem cells (NT2). Neuroscience2014;281:54–67. doi: 10.1016/j.neuroscience.2014.08.031Open DOISearch in Google Scholar
Synofzik M, Gonzalez MA, Lourenco CM, Coutelier M, Haack TB, Rebelo A, Hannequin D, Strom TM, Prokisch H, Kernstock C, Durr A, Schöls L, Lima-Martínez MM, Farooq A, Schüle R, Stevanin G, Marques W, Züchner S. PNPLA6 mutations cause Boucher-Neuhäuser and Gordon Holmes syndromes as part of a broad neurodegenerative spectrum. Brain 2014;137:69–77. doi: 10.1093/brain/awt326SynofzikMGonzalezMALourencoCMCoutelierMHaackTBRebeloAHannequinDStromTMProkischHKernstockCDurrASchölsLLima-MartínezMMFarooqASchüleRStevaninGMarquesWZüchnerS. PNPLA6 mutations cause Boucher-Neuhäuser and Gordon Holmes syndromes as part of a broad neurodegenerative spectrum. Brain2014;137:69–77. doi: 10.1093/brain/awt326Open DOISearch in Google Scholar
Shin M, Ware TB, Lee HC, Hsu KL. Lipid-metabolizing serine hydrolases in the mammalian central nervous system: endocannabinoids and beyond. Biochim Biophys Acta Mol Cell Biol Lipids 2019;1864:907–21. doi: 10.1016/j.bbalip.2018.08.007ShinMWareTBLeeHCHsuKL. Lipid-metabolizing serine hydrolases in the mammalian central nervous system: endocannabinoids and beyond. Biochim Biophys Acta Mol Cell Biol Lipids2019;1864:907–21. doi: 10.1016/j.bbalip.2018.08.007Open DOISearch in Google Scholar
Heier C, Kien B, Huang F, Eichmann TO, Xie H, Zechner R, Chang PA. The phospholipase PNPLA7 functions as a lysophosphatidylcholine hydrolase and interacts with lipid droplets through its catalytic domain. J Biol Chem 2017;292:19087–98. doi: 10.1074/jbc.M117.792978HeierCKienBHuangFEichmannTOXieHZechnerRChangPA. The phospholipase PNPLA7 functions as a lysophosphatidylcholine hydrolase and interacts with lipid droplets through its catalytic domain. J Biol Chem2017;292:19087–98. doi: 10.1074/jbc.M117.792978Open DOISearch in Google Scholar
Chang PA, Chen YY, Long DX, Qin WZ, Mou XL. Degradation of mouse NTE-related esterase by macroautophagy and the proteasome. Mol Biol Rep 2012;39:7125–31. doi: 10.1007/s11033-012-1544-9ChangPAChenYYLongDXQinWZMouXL. Degradation of mouse NTE-related esterase by macroautophagy and the proteasome. Mol Biol Rep2012;39:7125–31. doi: 10.1007/s11033-012-1544-9Open DOISearch in Google Scholar
Chang PA, Long DX, Wu YJ. Molecular cloning and expression of the C-terminal domain of mouse NTE-related esterase. Mol Cell Biochem 2007;306:25–32. doi: 10.1007/s11010-007-9550-2ChangPALongDXWuYJ. Molecular cloning and expression of the C-terminal domain of mouse NTE-related esterase. Mol Cell Biochem2007;306:25–32. doi: 10.1007/s11010-007-9550-2Open DOISearch in Google Scholar
Kienesberger PC, Lass A, Preiss-Landl K, Wolinski H, Kohlwein SD, Zimmermann R, Zechner R. Identification of an insulin-regulated lysophospholipase with homology to neuropathy target esterase. J Biol Chem 2008;283:5908–17. doi: 10.1074/jbc.M709598200KienesbergerPCLassAPreiss-LandlKWolinskiHKohlweinSDZimmermannRZechnerR. Identification of an insulin-regulated lysophospholipase with homology to neuropathy target esterase. J Biol Chem2008;283:5908–17. doi: 10.1074/jbc.M709598200Open DOISearch in Google Scholar
Chang P, Sun T, Heier C, Gao H, Xu H, Huang F. Interaction of the lysophospholipase PNPLA7 with lipid droplets through the catalytic region. Mol Cells 2020;43:286–97. doi: 10.14348/molcells.2020.2283ChangPSunTHeierCGaoHXuHHuangF. Interaction of the lysophospholipase PNPLA7 with lipid droplets through the catalytic region. Mol Cells2020;43:286–97. doi: 10.14348/molcells.2020.2283Open DOISearch in Google Scholar
Miš K, Lulić A-M, Marš T, Pirkmajer S, Katalinić M. Insulin, dibutyryl-cAMP, and glucose modulate expression of patatin-like domain containing protein 7 in cultured human myotubes. Front Endocrinol (Lausanne) 2023;14:1139303. doi: 10.3389/fendo.2023.1139303MišKLulićA-MMaršTPirkmajerSKatalinićM. Insulin, dibutyryl-cAMP, and glucose modulate expression of patatin-like domain containing protein 7 in cultured human myotubes. Front Endocrinol (Lausanne)2023;14:1139303. doi: 10.3389/fendo.2023.1139303Open DOISearch in Google Scholar
Vogel P, Read RW, Hansen GM, Powell DR. Histopathology is required to identify and characterize myopathies in high-throughput phenotype screening of genetically engineered mice. Vet Pathol 2021;58:1158–71. doi: 10.1177/03009858211030541VogelPReadRWHansenGMPowellDR. Histopathology is required to identify and characterize myopathies in high-throughput phenotype screening of genetically engineered mice. Vet Pathol2021;58:1158–71. doi: 10.1177/03009858211030541Open DOISearch in Google Scholar
Wang X, Guo M, Wang Q, Wang Q, Zuo S, Zhang X, Tong H, Chen J, Wang H, Chen X, Guo J, Su X, Liang H, Zhou H, Li JZ. The patatin-like phospholipase domain containing protein 7 facilitates VLDL secretion by modulating ApoE stability. Hepatology 2020;72:1569–85. doi: 10.1002/hep.31161WangXGuoMWangQWangQZuoSZhangXTongHChenJWangHChenXGuoJSuXLiangHZhouHLiJZ. The patatin-like phospholipase domain containing protein 7 facilitates VLDL secretion by modulating ApoE stability. Hepatology2020;72:1569–85. doi: 10.1002/hep.31161Open DOISearch in Google Scholar
Hirabayashi T, Kawaguchi M, Harada S, Mouri M, Takamiya R, Miki Y, Sato H, Taketomi Y, Yokoyama K, Kobayashi T, Tokuoka SM, Kita Y, Yoda E, Hara S, Mikami K, Nishito Y, Kikuchi N, Nakata R, Kaneko M, Kiyonari H, Kasahara K, Aiba T, Ikeda K, Soga T, Kurano M, Yatomi Y, Murakami M. Hepatic phosphatidylcholine catabolism driven by PNPLA7 and PNPLA8 supplies endogenous choline to replenish the methionine cycle with methyl groups. Cell Rep 2023;42(2):111940. doi: 10.1016/j.celrep.2022.111940HirabayashiTKawaguchiMHaradaSMouriMTakamiyaRMikiYSatoHTaketomiYYokoyamaKKobayashiTTokuokaSMKitaYYodaEHaraSMikamiKNishitoYKikuchiNNakataRKanekoMKiyonariHKasaharaKAibaTIkedaKSogaTKuranoMYatomiYMurakamiM. Hepatic phosphatidylcholine catabolism driven by PNPLA7 and PNPLA8 supplies endogenous choline to replenish the methionine cycle with methyl groups. Cell Rep2023;42(2):111940. doi: 10.1016/j.celrep.2022.111940Open DOISearch in Google Scholar
Tanaka H, Takeya R, Sumimoto H. A novel intracellular membrane-bound calcium-independent phospholipase A(2). Biochem Biophys Res Commun 2000;272:320–6. doi: 10.1006/bbrc.2000.2776TanakaHTakeyaRSumimotoH. A novel intracellular membrane-bound calcium-independent phospholipase A(2). Biochem Biophys Res Commun2000;272:320–6. doi: 10.1006/bbrc.2000.2776Open DOISearch in Google Scholar
Tanaka H, Minakami R, Kanaya H, Sumimoto H. Catalytic residues of group VIB calcium-independent phospholipase A2 (iPLA2gamma). Biochem Biophys Res Commun 2004;320:1284–90. doi: 10.1016/j.bbrc.2004.05.225TanakaHMinakamiRKanayaHSumimotoH. Catalytic residues of group VIB calcium-independent phospholipase A2 (iPLA2gamma). Biochem Biophys Res Commun2004;320:1284–90. doi: 10.1016/j.bbrc.2004.05.225Open DOISearch in Google Scholar
Mancuso DJ, Jenkins CM, Gross RW. The genomic organization, complete mRNA sequence, cloning, and expression of a novel human intracellular membrane-associated calcium-independent phospholipase A(2). J Biol Chem 2000;275:9937–45. doi: 10.1074/jbc.275.14.9937MancusoDJJenkinsCMGrossRW. The genomic organization, complete mRNA sequence, cloning, and expression of a novel human intracellular membrane-associated calcium-independent phospholipase A(2). J Biol Chem2000;275:9937–45. doi: 10.1074/jbc.275.14.9937Open DOISearch in Google Scholar
Jenkins CM, Cedars A, Gross RW. Eicosanoid signalling pathways in the heart. Cardiovasc Res 2009;82:240–9. doi: 10.1093/cvr/cvn346JenkinsCMCedarsAGrossRW. Eicosanoid signalling pathways in the heart. Cardiovasc Res2009;82:240–9. doi: 10.1093/cvr/cvn346Open DOISearch in Google Scholar
Yan W, Jenkins CM, Han X, Mancuso DJ, Sims HF, Yang K, Gross RW. The highly selective production of 2-arachidonoyl lysophosphatidylcholine catalyzed by purified calcium-independent phospholipase A2gamma: identification of a novel enzymatic mediator for the generation of a key branch point intermediate in eicosanoid signaling. J Biol Chem 2005;280:26669–79. doi: 10.1074/jbc.M502358200YanWJenkinsCMHanXMancusoDJSimsHFYangKGrossRW. The highly selective production of 2-arachidonoyl lysophosphatidylcholine catalyzed by purified calcium-independent phospholipase A2gamma: identification of a novel enzymatic mediator for the generation of a key branch point intermediate in eicosanoid signaling. J Biol Chem2005;280:26669–79. doi: 10.1074/jbc.M502358200Open DOISearch in Google Scholar
Rauckhorst AJ, Pfeiffer DR, Broekemeier KM. The iPLA(2)γ is identified as the membrane potential sensitive phospholipase in liver mitochondria. FEBS Lett 2015;589:2367–71. doi: 10.1016/j.febslet.2015.07.016RauckhorstAJPfeifferDRBroekemeierKM. The iPLA(2)γ is identified as the membrane potential sensitive phospholipase in liver mitochondria. FEBS Lett2015;589:2367–71. doi: 10.1016/j.febslet.2015.07.016Open DOISearch in Google Scholar
Kim KY, Jang HJ, Yang YR, Park KI, Seo J, Shin IW, Jeon TI, Ahn SC, Suh PG, Osborne TF, Seo YK. SREBP-2/PNPLA8 axis improves non-alcoholic fatty liver disease through activation of autophagy. Sci Rep 2016;6:35732. doi: 10.1038/srep35732KimKYJangHJYangYRParkKISeoJShinIWJeonTIAhnSCSuhPGOsborneTFSeoYK. SREBP-2/PNPLA8 axis improves non-alcoholic fatty liver disease through activation of autophagy. Sci Rep2016;6:35732. doi: 10.1038/srep35732Open DOISearch in Google Scholar
Mancuso DJ, Kotzbauer P, Wozniak DF, Sims HF, Jenkins CM, Guan S, Han X, Yang K, Sun G, Malik I, Conyers S, Green KG, Schmidt RE, Gross RW. Genetic ablation of calcium-independent phospholipase A2{gamma} leads to alterations in hippocampal cardiolipin content and molecular species distribution, mitochondrial degeneration, autophagy, and cognitive dysfunction. J Biol Chem 2009;284:35632–44. doi: 10.1074/jbc.M109.055194MancusoDJKotzbauerPWozniakDFSimsHFJenkinsCMGuanSHanXYangKSunGMalikIConyersSGreenKGSchmidtREGrossRW. Genetic ablation of calcium-independent phospholipase A2{gamma} leads to alterations in hippocampal cardiolipin content and molecular species distribution, mitochondrial degeneration, autophagy, and cognitive dysfunction. J Biol Chem2009;284:35632–44. doi: 10.1074/jbc.M109.055194Open DOISearch in Google Scholar
Moon SH, Jenkins CM, Liu X, Guan S, Mancuso DJ, Gross RW. Activation of mitochondrial calcium-independent phospholipase A2γ (iPLA2γ) by divalent cations mediating arachidonate release and production of downstream eicosanoids. J Biol Chem 2012;287:14880–95. doi: 10.1074/jbc.M111.336776MoonSHJenkinsCMLiuXGuanSMancusoDJGrossRW. Activation of mitochondrial calcium-independent phospholipase A2γ (iPLA2γ) by divalent cations mediating arachidonate release and production of downstream eicosanoids. J Biol Chem2012;287:14880–95. doi: 10.1074/jbc.M111.336776Open DOISearch in Google Scholar
Yoda E, Hachisu K, Taketomi Y, Yoshida K, Nakamura M, Ikeda K, Taguchi R, Nakatani Y, Kuwata H, Murakami M, Kudo I, Hara S. Mitochondrial dysfunction and reduced prostaglandin synthesis in skeletal muscle of Group VIB Ca2+-independent phospholipase A2gamma-deficient mice. J Lipid Res 2010;51:3003–15. doi: 10.1194/jlr.M008060YodaEHachisuKTaketomiYYoshidaKNakamuraMIkedaKTaguchiRNakataniYKuwataHMurakamiMKudoIHaraS. Mitochondrial dysfunction and reduced prostaglandin synthesis in skeletal muscle of Group VIB Ca2+-independent phospholipase A2gamma-deficient mice. J Lipid Res2010;51:3003–15. doi: 10.1194/jlr.M008060Open DOISearch in Google Scholar
Ye C, Shen Z, Greenberg ML. Cardiolipin remodeling: a regulatory hub for modulating cardiolipin metabolism and function. J Bioenerg Biomembr 2016;48:113–23. doi: 10.1007/s10863-014-9591-7YeCShenZGreenbergML. Cardiolipin remodeling: a regulatory hub for modulating cardiolipin metabolism and function. J Bioenerg Biomembr2016;48:113–23. doi: 10.1007/s10863-014-9591-7Open DOISearch in Google Scholar
Liu X, Sims HF, Jenkins CM, Guan S, Dilthey BG, Gross RW. 12-LOX catalyzes the oxidation of 2-arachidonoyl-lysolipids in platelets generating eicosanoid-lysolipids that are attenuated by iPLA2γ knockout. J Biol Chem 2020;295:5307–20. doi: 10.1074/jbc.RA119.012296LiuXSimsHFJenkinsCMGuanSDiltheyBGGrossRW. 12-LOX catalyzes the oxidation of 2-arachidonoyl-lysolipids in platelets generating eicosanoid-lysolipids that are attenuated by iPLA2γ knockout. J Biol Chem2020;295:5307–20. doi: 10.1074/jbc.RA119.012296Open DOISearch in Google Scholar
Saunders CJ, Moon SH, Liu X, Thiffault I, Coffman K, LePichon JB, Taboada E, Smith LD, Farrow EG, Miller N, Gibson M, Patterson M, Kingsmore SF, Gross RW. Loss of function variants in human PNPLA8 encoding calcium-independent phospholipase A2γ recapitulate the mitochondriopathy of the homologous null mouse. Hum Mutat 2015;36:301–6. doi: 10.1002/humu.22743SaundersCJMoonSHLiuXThiffaultICoffmanKLePichonJBTaboadaESmithLDFarrowEGMillerNGibsonMPattersonMKingsmoreSFGrossRW. Loss of function variants in human PNPLA8 encoding calcium-independent phospholipase A2γ recapitulate the mitochondriopathy of the homologous null mouse. Hum Mutat2015;36:301–6. doi: 10.1002/humu.22743Open DOISearch in Google Scholar
Chao H, Liu Y, Fu X, Xu X, Bao Z, Lin C, Li Z, Liu Y, Wang X, You Y, Liu N, Ji J. Lowered iPLA2γ activity causes increased mitochondrial lipid peroxidation and mitochondrial dysfunction in a rotenone-induced model of Parkinson’s disease. Exp Neurol 2018;300:74–86. doi: 10.1016/j.expneurol.2017.10.031ChaoHLiuYFuXXuXBaoZLinCLiZLiuYWangXYouYLiuNJiJ. Lowered iPLA2γ activity causes increased mitochondrial lipid peroxidation and mitochondrial dysfunction in a rotenone-induced model of Parkinson’s disease. Exp Neurol2018;300:74–86. doi: 10.1016/j.expneurol.2017.10.031Open DOISearch in Google Scholar
Moon SH, Dilthey BG, Liu X, Guan S, Sims HF, Gross RW. High-fat diet activates liver iPLA2γ generating eicosanoids that mediate metabolic stress. J Lipid Res 2021;62:100052. doi: 10.1016/j.jlr.2021.100052MoonSHDiltheyBGLiuXGuanSSimsHFGrossRW. High-fat diet activates liver iPLA2γ generating eicosanoids that mediate metabolic stress. J Lipid Res2021;62:100052. doi: 10.1016/j.jlr.2021.100052Open DOISearch in Google Scholar
Průchová P, Gotvaldová K, Smolková K, Alán L, Holendová B, Tauber J, Galkin A, Ježek P, Jabůrek M. Antioxidant role and cardiolipin remodeling by redox-activated mitochondrial Ca2+-independent phospholipase A2γ in the brain. Antioxidants (Basel) 2022;11(2):198. doi: 10.3390/antiox11020198PrůchováPGotvaldováKSmolkováKAlánLHolendováBTauberJGalkinAJežekPJabůrekM. Antioxidant role and cardiolipin remodeling by redox-activated mitochondrial Ca2+-independent phospholipase A2γ in the brain. Antioxidants (Basel)2022;11(2):198. doi: 10.3390/antiox11020198Open DOISearch in Google Scholar
Shukla A, Saneto RP, Hebbar M, Mirzaa G, Girisha KM. A neurodegenerative mitochondrial disease phenotype due to biallelic loss-of-function variants in PNPLA8 encoding calcium-independent phospholipase A2γ. Am J Med Genet A 2018;176:1232–7. doi: 10.1002/ajmg.a.38687ShuklaASanetoRPHebbarMMirzaaGGirishaKM. A neurodegenerative mitochondrial disease phenotype due to biallelic loss-of-function variants in PNPLA8 encoding calcium-independent phospholipase A2γ. Am J Med Genet A2018;176:1232–7. doi: 10.1002/ajmg.a.38687Open DOISearch in Google Scholar
Moon SH, Jenkins CM, Kiebish MA, Sims HF, Mancuso DJ, Gross RW. Genetic ablation of calcium-independent phospholipase A2γ (iPLA2γ) attenuates calcium-induced opening of the mitochondrial permeability transition pore and resultant cytochrome c release. J Biol Chem 2012;287:29837–50. doi: 10.1074/jbc.M112.373654MoonSHJenkinsCMKiebishMASimsHFMancusoDJGrossRW. Genetic ablation of calcium-independent phospholipase A2γ (iPLA2γ) attenuates calcium-induced opening of the mitochondrial permeability transition pore and resultant cytochrome c release. J Biol Chem2012;287:29837–50. doi: 10.1074/jbc.M112.373654Open DOISearch in Google Scholar
Rauckhorst AJ, Broekemeier KM, Pfeiffer DR. Regulation of the Ca2+-independent phospholipase A2 in liver mitochondria by changes in the energetic state. J Lipid Res 2014;55:826–36. doi: 10.1194/jlr.M043307RauckhorstAJBroekemeierKMPfeifferDR. Regulation of the Ca2+-independent phospholipase A2 in liver mitochondria by changes in the energetic state. J Lipid Res2014;55:826–36. doi: 10.1194/jlr.M043307Open DOISearch in Google Scholar
Moon SH, Liu X, Cedars AM, Yang K, Kiebish MA, Joseph SM, Kelley J, Jenkins CM, Gross RW. Heart failure-induced activation of phospholipase iPLA2γ generates hydroxyeicosatetraenoic acids opening the mitochondrial permeability transition pore. J Biol Chem 2018;293:115–29. doi: 10.1074/jbc.RA117.000405MoonSHLiuXCedarsAMYangKKiebishMAJosephSMKelleyJJenkinsCMGrossRW. Heart failure-induced activation of phospholipase iPLA2γ generates hydroxyeicosatetraenoic acids opening the mitochondrial permeability transition pore. J Biol Chem2018;293:115–29. doi: 10.1074/jbc.RA117.000405Open DOISearch in Google Scholar
Turk J, White TD, Nelson AJ, Lei X, Ramanadham S. iPLA2β and its role in male fertility, neurological disorders, metabolic disorders, and inflammation. Biochim Biophys Acta Mol Cell Biol Lipids 2019;1864:846–60. doi: 10.1016/j.bbalip.2018.10.010TurkJWhiteTDNelsonAJLeiXRamanadhamS. iPLA2β and its role in male fertility, neurological disorders, metabolic disorders, and inflammation. Biochim Biophys Acta Mol Cell Biol Lipids2019;1864:846–60. doi: 10.1016/j.bbalip.2018.10.010Open DOISearch in Google Scholar
Hsu YH, Bucher D, Cao J, Li S, Yang SW, Kokotos G, Woods VL Jr, McCammon JA, Dennis EA. Fluoroketone inhibition of Ca2+-independent phospholipase A2 through binding pocket association defined by hydrogen/deuterium exchange and molecular dynamics. J Am Chem Soc 2013;135:1330–7. doi: 10.1021/ja306490gHsuYHBucherDCaoJLiSYangSWKokotosGWoodsVLJrMcCammonJADennisEA. Fluoroketone inhibition of Ca2+-independent phospholipase A2 through binding pocket association defined by hydrogen/deuterium exchange and molecular dynamics. J Am Chem Soc2013;135:1330–7. doi: 10.1021/ja306490gOpen DOISearch in Google Scholar
Lei X, Barbour SE, Ramanadham S. Group VIA Ca2+-independent phospholipase A2(iPLA2β) and its role in β-cell programmed cell death. Biochimie 2010;92:627–37. doi: 10.1016/j.biochi.2010.01.005LeiXBarbourSERamanadhamS. Group VIA Ca2+-independent phospholipase A2(iPLA2β) and its role in β-cell programmed cell death. Biochimie2010;92:627–37. doi: 10.1016/j.biochi.2010.01.005Open DOISearch in Google Scholar
Song H, Rohrs H, Tan M, Wohltmann M, Ladenson JH, Turk J. Effects of endoplasmic reticulum stress on group VIA phospholipase A2 in beta cells include tyrosine phosphorylation and increased association with calnexin. J Biol Chem 2010;285:33843–57. doi: 10.1074/jbc.M110.153197SongHRohrsHTanMWohltmannMLadensonJHTurkJ. Effects of endoplasmic reticulum stress on group VIA phospholipase A2 in beta cells include tyrosine phosphorylation and increased association with calnexin. J Biol Chem2010;285:33843–57. doi: 10.1074/jbc.M110.153197Open DOISearch in Google Scholar
Morrison K, Witte K, Mayers JR, Schuh AL, Audhya A. Roles of acidic phospholipids and nucleotides in regulating membrane binding and activity of a calcium-independent phospholipase A2 isoform. J Biol Chem 2012;287:38824–34. doi: 10.1074/jbc.M112.391508MorrisonKWitteKMayersJRSchuhALAudhyaA. Roles of acidic phospholipids and nucleotides in regulating membrane binding and activity of a calcium-independent phospholipase A2 isoform. J Biol Chem2012;287:38824–34. doi: 10.1074/jbc.M112.391508Open DOISearch in Google Scholar
Malik I, Turk J, Mancuso DJ, Montier L, Wohltmann M, Wozniak DF, Schmidt RE, Gross RW, Kotzbauer PT. Disrupted membrane homeostasis and accumulation of ubiquitinated proteins in a mouse model of infantile neuroaxonal dystrophy caused by PLA2G6 mutations. Am J Pathol 2008;172:406–16. doi: 10.2353/ajpath.2008.070823MalikITurkJMancusoDJMontierLWohltmannMWozniakDFSchmidtREGrossRWKotzbauerPT. Disrupted membrane homeostasis and accumulation of ubiquitinated proteins in a mouse model of infantile neuroaxonal dystrophy caused by PLA2G6 mutations. Am J Pathol2008;172:406–16. doi: 10.2353/ajpath.2008.070823Open DOISearch in Google Scholar
Bao S, Jacobson DA, Wohltmann M, Bohrer A, Jin W, Philipson LH, Turk J. Glucose homeostasis, insulin secretion, and islet phospholipids in mice that overexpress iPLA2β in pancreatic β-cells and in iPLA2β-null mice. Am J Physiol Endocrinol Metab 2008;294(2):E217–29. doi: 10.1152/ajpendo.00474.2007BaoSJacobsonDAWohltmannMBohrerAJinWPhilipsonLHTurkJ. Glucose homeostasis, insulin secretion, and islet phospholipids in mice that overexpress iPLA2β in pancreatic β-cells and in iPLA2β-null mice. Am J Physiol Endocrinol Metab2008;294(2):E217–29. doi: 10.1152/ajpendo.00474.2007Open DOISearch in Google Scholar
Song H, Bao S, Lei X, Jin C, Zhang S, Turk J, Ramanadham S. Evidence for proteolytic processing and stimulated organelle redistribution of iPLA2β. Biochim Biophys Acta 2010;1801:547–58. doi: 10.1016/j.bbalip.2010.01.006SongHBaoSLeiXJinCZhangSTurkJRamanadhamS. Evidence for proteolytic processing and stimulated organelle redistribution of iPLA2β. Biochim Biophys Acta2010;1801:547–58. doi: 10.1016/j.bbalip.2010.01.006Open DOISearch in Google Scholar
Cheon Y, Kim HW, Igarashi M, Modi HR, Chang L, Ma K, Greenstein D, Wohltmann M, Turk J, Rapoport SI, Taha AY. Disturbed brain phospholipid and docosahexaenoic acid metabolism in calcium-independent phospholipase A2-VIA (iPLA2β)-knockout mice. Biochim Biophys Acta 2012;1821:1278–86. doi: 10.1016/j.bbalip.2012.02.003CheonYKimHWIgarashiMModiHRChangLMaKGreensteinDWohltmannMTurkJRapoportSITahaAY. Disturbed brain phospholipid and docosahexaenoic acid metabolism in calcium-independent phospholipase A2-VIA (iPLA2β)-knockout mice. Biochim Biophys Acta2012;1821:1278–86. doi: 10.1016/j.bbalip.2012.02.003Open DOISearch in Google Scholar
Astudillo AM, Balboa MA, Balsinde J. Selectivity of phospholipid hydrolysis by phospholipase A2 enzymes in activated cells leading to polyunsaturated fatty acid mobilization. Biochim Biophys Acta Mol Cell Biol Lipids 2019;1864:772–83. doi: 10.1016/j.bbalip.2018.07.002AstudilloAMBalboaMABalsindeJ. Selectivity of phospholipid hydrolysis by phospholipase A2 enzymes in activated cells leading to polyunsaturated fatty acid mobilization. Biochim Biophys Acta Mol Cell Biol Lipids2019;1864:772–83. doi: 10.1016/j.bbalip.2018.07.002Open DOISearch in Google Scholar
Chiu CC, Lu CS, Weng YH, Chen YL, Huang YZ, Chen RS, Cheng YC, Huang YC, Liu YC, Lai SC, Lin KJ, Lin YW, Chen YJ, Chen CL, Yeh TH, Wang HL. PARK14 (D331Y) PLA2G6 causes early-onset degeneration of substantia nigra dopaminergic neurons by inducing mitochondrial dysfunction, ER stress, mitophagy impairment and transcriptional dysregulation in a knockin mouse model. Mol Neurobiol 2019;56:3835–53. doi: 10.1007/s12035-018-1118-5ChiuCCLuCSWengYHChenYLHuangYZChenRSChengYCHuangYCLiuYCLaiSCLinKJLinYWChenYJChenCLYehTHWangHL. PARK14 (D331Y) PLA2G6 causes early-onset degeneration of substantia nigra dopaminergic neurons by inducing mitochondrial dysfunction, ER stress, mitophagy impairment and transcriptional dysregulation in a knockin mouse model. Mol Neurobiol2019;56:3835–53. doi: 10.1007/s12035-018-1118-5Open DOISearch in Google Scholar
Gregory A, Westaway SK, Holm IE, Kotzbauer PT, Hogarth P, Sonek S, Coryell JC, Nguyen TM, Nardocci N, Zorzi G, Rodriguez D, Desguerre I, Bertini E, Simonati A, Levinson B, Dias C, Barbot C, Carrilho I, Santos M, Malik I, Gitschier J, Hayflick SJ. Neurodegeneration associated with genetic defects in phospholipase A2. Neurology 2008;71:1402–9. doi: 10.1212/01.wnl.0000327094.67726.28GregoryAWestawaySKHolmIEKotzbauerPTHogarthPSonekSCoryellJCNguyenTMNardocciNZorziGRodriguezDDesguerreIBertiniESimonatiALevinsonBDiasCBarbotCCarrilhoISantosMMalikIGitschierJHayflickSJ. Neurodegeneration associated with genetic defects in phospholipase A2. Neurology2008;71:1402–9. doi: 10.1212/01.wnl.0000327094.67726.28Open DOISearch in Google Scholar
Deng X, Wang J, Jiao L, Utaipan T, Tuma-Kellner S, Schmitz G, Liebisch G, Stremmel W, Chamulitrat W. iPLA2β deficiency attenuates obesity and hepatic steatosis in ob/ob mice through hepatic fatty-acyl phospholipid remodeling. Biochim Biophys Acta 2016;1861:449–61. doi: 10.1016/j.bbalip.2016.02.004DengXWangJJiaoLUtaipanTTuma-KellnerSSchmitzGLiebischGStremmelWChamulitratW. iPLA2β deficiency attenuates obesity and hepatic steatosis in ob/ob mice through hepatic fatty-acyl phospholipid remodeling. Biochim Biophys Acta2016;1861:449–61. doi: 10.1016/j.bbalip.2016.02.004Open DOISearch in Google Scholar
Turk J, Song H, Wohltmann M, Frankfater C, Lei X, Ramanadham S. Metabolic effects of selective deletion of group VIA phospholipase A2 from macrophages or pancreatic islet β-cells. Biomolecules 2020;10(10):1455. doi: 10.3390/biom10101455TurkJSongHWohltmannMFrankfaterCLeiXRamanadhamS. Metabolic effects of selective deletion of group VIA phospholipase A2 from macrophages or pancreatic islet β-cells. Biomolecules2020;10(10):1455. doi: 10.3390/biom10101455Open DOISearch in Google Scholar
Ali T, Lei X, Barbour SE, Koizumi A, Chalfant CE, Ramanadham S. Alterations in β-cell sphingolipid profile associated with ER stress and iPLA2β: another contributor to β-cell apoptosis in type 1 diabetes. Molecules 2021;26(21):6361. doi: 10.3390/molecules26216361AliTLeiXBarbourSEKoizumiAChalfantCERamanadhamS. Alterations in β-cell sphingolipid profile associated with ER stress and iPLA2β: another contributor to β-cell apoptosis in type 1 diabetes. Molecules2021;26(21):6361. doi: 10.3390/molecules26216361Open DOISearch in Google Scholar
Jin T, Lin J, Gong Y, Bi X, Hu S, Lv Q, Chen J, Li X, Chen J, Zhang W, Wang M, Fu G. iPLA2β contributes to ER stress-induced apoptosis during myocardial ischemia/reperfusion injury. Cells 2021;10(6):1446. doi: 10.3390/cells10061446JinTLinJGongYBiXHuSLvQChenJLiXChenJZhangWWangMFuG. iPLA2β contributes to ER stress-induced apoptosis during myocardial ischemia/reperfusion injury. Cells2021;10(6):1446. doi: 10.3390/cells10061446Open DOISearch in Google Scholar
Chen D, Chu B, Yang X, Liu Z, Jin Y, Kon N, Rabadan R, Jiang X, Stockwell BR, Gu W. iPLA2β-mediated lipid detoxification controls p53-driven ferroptosis independent of GPX4. Nat Commun 2021;12(1):3644. doi: 10.1038/s41467-021-23902-6ChenDChuBYangXLiuZJinYKonNRabadanRJiangXStockwellBRGuW. iPLA2β-mediated lipid detoxification controls p53-driven ferroptosis independent of GPX4. Nat Commun2021;12(1):3644. doi: 10.1038/s41467-021-23902-6Open DOISearch in Google Scholar
Lin G, Lee PT, Chen K, Mao D, Tan KL, Zuo Z, Lin WW, Wang L, Bellen HJ. Phospholipase PLA2G6, a parkinsonism-associated gene, affects Vps26 and Vps35, retromer function, and ceramide levels, similar to α-synuclein gain. Cell Metab 2018;28:605–618.e6. doi: 10.1016/j.cmet.2018.05.019LinGLeePTChenKMaoDTanKLZuoZLinWWWangLBellenHJ. Phospholipase PLA2G6, a parkinsonism-associated gene, affects Vps26 and Vps35, retromer function, and ceramide levels, similar to α-synuclein gain. Cell Metab2018;28:605–618.e6. doi: 10.1016/j.cmet.2018.05.019Open DOISearch in Google Scholar
Marš T, Miš K, Pirkmajer S, Katalinić M, Grubić Z. The effects of organophosphates in the early stages of human muscle regeneration. In: Gupta RC, editor: Handbook of toxicology of chemical warfare agents. 2nd ed. Chapter 51. Cambridge, Massachusetts (USA): Academic Press; 2020. p. 751–9. doi: 10.1016/B978-0-12-800159-2.00051-8MaršTMišKPirkmajerSKatalinićMGrubićZ. The effects of organophosphates in the early stages of human muscle regeneration. In: GuptaRCeditor: Handbook of toxicology of chemical warfare agents. 2nd ed.Chapter 51. Cambridge, Massachusetts (USA): Academic Press; 2020. p. 751–9. doi: 10.1016/B978-0-12-800159-2.00051-8Open DOISearch in Google Scholar
Kulminskaya N, Radler C, Viertlmayr R, Heier C, Hofer P, Colaço-Gaspar M, Owens RJ, Zimmermann R, Schreiber R, Zechner R, Oberer M. Optimized expression and purification of adipose triglyceride lipase improved hydrolytic and transacylation activities in vitro. J Biol Chem 2021;297(4):101206. doi: 10.1016/j.jbc.2021.101206KulminskayaNRadlerCViertlmayrRHeierCHoferPColaço-GasparMOwensRJZimmermannRSchreiberRZechnerRObererM. Optimized expression and purification of adipose triglyceride lipase improved hydrolytic and transacylation activities in vitro. J Biol Chem2021;297(4):101206. doi: 10.1016/j.jbc.2021.101206Open DOISearch in Google Scholar
Racusen D, Weller DL. Molecular weight of patatin, a major potato tuber protein. J Food Biochem 1984;8:103–7. doi: 10.1111/j.1745-4514.1984.tb00318.xRacusenDWellerDL. Molecular weight of patatin, a major potato tuber protein. J Food Biochem1984;8:103–7. doi: 10.1111/j.1745-4514.1984.tb00318.xOpen DOISearch in Google Scholar
