220. Bolen, A.L.; Naren, A.P.; Yarlagadda, S.; Beranova-Giorgianni, S.; Chen, L.; Norman, D.; Baker, D.L.; Rowland, M.M.; Best, M.D.; Sano, T.; et al. The phospholipase A1 activity of lysophospholipase A-I links platelet activation to LPA production during blood coagulation. *J. Lipid Res.* **2011**, *52*, 958–970. [CrossRef]

221. Qian, L.; Xu, Y.; Hasegawa, Y.; Aoki, J.; Mills, G.B.; Prestwich, G.D. Enantioselective responses to a phosphorothioate analogue of lysophosphatidic acid with LPA3 receptor-selective agonist activity. *J. Med. Chem.* **2003**, *46*, 5575–5578. [CrossRef] [PubMed]

222. Chrencik, J.E.; Roth, C.B.; Terakado, M.; Kurata, H.; Omi, R.; Kihara, Y.; Warshaviak, D.; Nakade, S.; Asmar-Rovira, G.; Mileni, M.; et al. Crystal Structure of Antagonist Bound Human Lysophosphatidic Acid Receptor 1. *Cell* **2015**, *161*, 1633–1643. [CrossRef] [PubMed]

223. Yaginuma, S.; Kawana, H.; Aoki, J. Current Knowledge on Mammalian Phospholipase A1, Brief History, Structures, Biochemical and Pathophysiological Roles. *Molecules* **2022**, *27*, 2487. [CrossRef] [PubMed]

224. Xia, A.; Yong, X.; Zhang, C.; Lin, G.; Jia, G.; Zhao, C.; Wang, X.; Hao, Y.; Wang, Y.; Zhou, P.; et al. Cryo-EM structures of human GPR34 enable the identification of selective antagonists. *Proc. Natl. Acad. Sci. USA* **2023**, *120*, e2308435120. [CrossRef] [PubMed]

225. Blankman, J.L.; Simon, G.M.; Cravatt, B.F. A comprehensive profile of brain enzymes that hydrolyze the endocannabinoid 2-arachidonoylglycerol. *Chem. Biol.* **2007**, *14*, 1347–1356. [CrossRef] [PubMed]

226. Savinainen, J.R.; Saario, S.M.; Laitinen, J.T. The serine hydrolases MAGL, ABHD6 and ABHD12 as guardians of 2-arachidonoylglycerol signalling through cannabinoid receptors. *Acta Physiol.* **2012**, *204*, 267–276. [CrossRef] [PubMed]

227. Thomas, G.; Betters, J.L.; Lord, C.C.; Brown, A.L.; Marshall, S.; Ferguson, D.; Sawyer, J.; Davis, M.A.; Melchior, J.T.; Blume, L.C.; et al. The serine hydrolase ABHD6 Is a critical regulator of the metabolic syndrome. *Cell Rep.* **2013**, *5*, 508–520. [CrossRef] [PubMed]

228. Pribasnig, M.A.; Mrak, I.; Grabner, G.F.; Taschler, U.; Knittelfelder, O.; Scherz, B.; Eichmann, T.O.; Heier, C.; Grumet, L.; Kowaliuk, J.; et al. α/β Hydrolase Domain-containing 6 (ABHD6) Degrades the Late Endosomal/Lysosomal Lipid Bis(monoacylgycero)phosphate. *J. Biol. Chem.* **2015**, *290*, 29869–29881. [CrossRef] [PubMed]

229. Grabner, G.F.; Fawzy, N.; Pribasnig, M.A.; Trieb, M.; Taschler, U.; Holzer, M.; Schweiger, M.; Wolinski, H.; Kolb, D.; Horvath, A.; et al. Metabolic disease and ABHD6 alter the circulating bis(monoacylglycerol)phosphate profile in mice and humans. *J. Lipid Res.* **2019**, *60*, 1020–1031. [CrossRef]

230. Masquelier, J.; Alhouayek, M.; Terrasi, R.; Bottemanne, P.; Paquot, A.; Muccioli, G.G. Lysophosphatidylinositols in inflammation and macrophage activation: Altered levels and anti-inflammatory effects. *Biochim. Biophys. Acta Mol. Cell Biol. Lipids* **2018**, *1863*, 1458–1468. [CrossRef]

231. Blankman, J.L.; Long, J.Z.; Trauger, S.A.; Siuzdak, G.; Cravatt, B.F. ABHD12 controls brain lysophosphatidylserine pathways that are deregulated in a murine model of the neurodegenerative disease PHARC. *Proc. Natl. Acad. Sci. USA* **2013**, *110*, 1500–1505. [CrossRef] [PubMed]

232. Ichu, T.A.; Reed, A.; Ogasawara, D.; Ulanovskaya, O.; Roberts, A.; Aguirre, C.A.; Bar-Peled, L.; Gao, J.; Germain, J.; Barbas, S.; et al. ABHD12 and LPCAT3 Interplay Regulates a Lyso-phosphatidylserine-C20:4 Phosphatidylserine Lipid Network Implicated in Neurological Disease. *Biochemistry* **2020**, *59*, 1793–1799. [CrossRef] [PubMed]

233. Ogasawara, D.; Ichu, T.A.; Vartabedian, V.F.; Benthuysen, J.; Jing, H.; Reed, A.; Ulanovskaya, O.A.; Hulce, J.J.; Roberts, A.; Brown, S.; et al. Selective blockade of the lyso-PS lipase ABHD12 stimulates immune responses in vivo. *Nat. Chem. Biol.* **2018**, *14*, 1099–1108. [CrossRef] [PubMed]

234. Ogasawara, D.; Ichu, T.A.; Jing, H.; Hulce, J.J.; Reed, A.; Ulanovskaya, O.A.; Cravatt, B.F. Discovery and Optimization of Selective and in Vivo Active Inhibitors of the Lysophosphatidylserine Lipase α/β-Hydrolase Domain-Containing 12 (ABHD12). *J. Med. Chem.* **2019**, *62*, 1643–1656. [CrossRef] [PubMed]

235. Fauvel, J.; Bonnefis, M.J.; Sarda, L.; Chap, H.; Thouvenot, J.P.; Douste-Blazy, L. Purification of two lipases with high phospholipase A1 activity from guinea-pig pancreas. *Biochim. Biophys. Acta* **1981**, *663*, 446–456. [CrossRef] [PubMed]

236. Lowe, M.E. Properties and function of pancreatic lipase related protein 2. *Biochimie* **2000**, *82*, 997–1004. [CrossRef] [PubMed]

237. Aoki, J.; Inoue, A.; Makide, K.; Saiki, N.; Arai, H. Structure and function of extracellular phospholipase A1 belonging to the pancreatic lipase gene family. *Biochimie* **2007**, *89*, 197–204. [CrossRef] [PubMed]

238. Zhu, G.; Fang, Q.; Zhu, F.; Huang, D.; Yang, C. Structure and Function of Pancreatic Lipase-Related Protein 2 and Its Relationship With Pathological States. *Front. Genet.* **2021**, *12*, 693538. [CrossRef] [PubMed]

239. Alves, B.N.; Leong, J.; Tamang, D.L.; Elliott, V.; Edelnant, J.; Redelman, D.; Singer, C.A.; Kuhn, A.R.; Miller, R.; Lowe, M.E.; et al. Pancreatic lipase-related protein 2 (PLRP2) induction by IL-4 in cytotoxic T lymphocytes (CTLs) and reevaluation of the negative effects of its gene ablation on cytotoxicity. *J. Leukoc. Biol.* **2009**, *86*, 701–712. [CrossRef]

240. Gao, Y.; Lu, W.; Sun, Q.; Yang, X.; Liu, J.; Ge, W.; Yang, Y.; Zhao, Y.; Xu, X.; Zhang, J. Pancreatic lipase-related protein 2 is responsible for the increased hepatic retinyl ester hydrolase activity in vitamin A-deficient mice. *FEBS J.* **2019**, *286*, 4232–4244. [CrossRef]

241. Ge, W.; Gao, Y.; Zhao, Y.; Yang, Y.; Sun, Q.; Yang, X.; Xu, X.; Zhang, J. Decreased T-cell mediated hepatic injury in concanavalin A-treated PLRP2-deficient mice. *Int. Immunopharmacol.* **2020**, *85*, 106604. [CrossRef] [PubMed]

242. Kuge, H.; Miyamoto, I.; Yagyu, K.I.; Honke, K. PLRP2 selectively localizes synaptic membrane proteins via acyl-chain remodeling of phospholipids. *J. Lipid Res.* **2020**, *61*, 1747–1763. [CrossRef]
243. Ding, Z.; Cheng, R.; Liu, J.; Zhao, Y.; Ge, W.; Yang, Y.; Xu, X.; Wang, S.; Zhang, J. The suppression of pancreatic lipase-related protein 2 ameliorates experimental hepatic fibrosis in mice. *Biochim. Biophys. Acta Mol. Cell Biol. Lipids* **2022**, *1867*, 159102. [CrossRef] [PubMed]

244. Tao, H.P.; Lu, T.F.; Li, S.; Jia, G.X.; Zhang, X.N.; Yang, Q.E.; Hou, Y.P. Pancreatic lipase-related protein 2 is selectively expressed by peritubular myoid cells in the murine testis and sustains long-term spermatogenesis. *Cell. Mol. Life Sci.* **2023**, *80*, 217. [CrossRef] [PubMed]

245. Sahaka, M.; Mateos-Diaz, E.; Amara, S.; Wattanakul, J.; Gray, D.; Lafont, D.; Gontero, B.; Launay, H.; Carrière, F. In situ monitoring of galactolipid digestion by infrared spectroscopy in both model micelles and spinach chloroplasts. *Chem. Phys. Lipids* **2023**, *252*, 105291. [CrossRef]

246. Record, M.; Amara, S.; Subra, C.; Jiang, G.; Prestwich, G.D.; Ferrato, F.; Carrière, F. Bis (monoacylglycero) phosphate interfacial properties and lipolysis by pancreatic lipase-related protein 2, an enzyme present in THP-1 human monocytes. *Biochim. Biophys. Acta* **2011**, *1811*, 419–430. [CrossRef]

247. Gilleron, M.; Lepore, M.; Layre, E.; Cala-De Paepe, D.; Mebarek, N.; Shayman, J.A.; Canaan, S.; Mori, L.; Carrière, F.; Puzo, G.; et al. Lysosomal Lipases PLRP2 and LPLA2 Process Mycobacterial Multi-acylated Lipids and Generate T Cell Stimulatory Antigens. *Cell Chem. Biol.* **2016**, *23*, 1147–1156. [CrossRef]

248. Hirano, T.; Kishi, M.; Sugimoto, H.; Taguchi, R.; Obinata, H.; Ohshima, N.; Tatei, K.; Izumi, T. Thioesterase activity and subcellular localization of acylprotein thioesterase 1/lysophospholipase 1. *Biochim. Biophys. Acta* **2009**, *1791*, 797–805. [CrossRef]

249. Kamat, S.S.; Camara, K.; Parsons, W.H.; Chen, D.H.; Dix, M.M.; Bird, T.D.; Howell, A.R.; Cravatt, B.F. Immunomodulatory lysophosphatidylserines are regulated by ABHD16A and ABHD12 interplay. *Nat. Chem. Biol.* **2015**, *11*, 164–171. [CrossRef]

250. Kim, H.Y. Phospholipids: A neuroinflammation emerging target. *Nat. Chem. Biol.* **2015**, *11*, 99–100. [CrossRef]

251. Singh, S.; Joshi, A.; Kamat, S.S. Mapping the Neuroanatomy of ABHD16A, ABHD12, and Lysophosphatidylserines Provides New Insights into the Pathophysiology of the Human Neurological Disorder PHARC. *Biochemistry* **2020**, *59*, 2299–2311. [CrossRef] [PubMed]

252. Nguyen, T.T.; Voeltz, G.K. An ER phospholipid hydrolase drives ER-associated mitochondrial constriction for fission and fusion. *Elife* **2022**, *11*, e84279. [CrossRef] [PubMed]

253. Shi, X.; Li, X.; Xu, Z.; Shen, L.; Ding, Y.; Chen, S.; Mao, L.; Liu, W.; Xu, J. ABHD16A Negatively Regulates the Palmitoylation and Antiviral Function of IFITM Proteins. *mBio* **2022**, *13*, e0228922. [CrossRef] [PubMed]

254. Narayanasamy, R.; Rajasekharan, R.; Usharani, D. Molecular insights on PS-PLA1 lipase activity of human ABHD16B. *Biophys. Chem.* **2023**, *296*, 106976. [CrossRef] [PubMed]

255. Lord, C.C.; Thomas, G.; Brown, J.M. Mammalian alpha beta hydrolase domain (ABHD) proteins: Lipid metabolizing enzymes at the interface of cell signaling and energy metabolism. *Biochim. Biophys. Acta* **2013**, *1831*, 792–802. [CrossRef] [PubMed]

256. Brindley, D.N. Lipid phosphate phosphatases and related proteins: Signaling functions in development, cell division, and cancer. *J. Cell Biochem.* **2004**, *92*, 900–912. [CrossRef] [PubMed]

257. Sigal, Y.J.; McDermott, M.I.; Morris, A.J. Integral membrane lipid phosphatases/phosphotransferases: Common structure and diverse functions. *Biochem. J.* **2005**, *387*, 281–293. [CrossRef] [PubMed]

258. Tang, X.; Benesch, M.G.; Brindley, D.N. Lipid phosphate phosphatases and their roles in mammalian physiology and pathology. *J. Lipid Res.* **2015**, *56*, 2048–2060. [CrossRef] [PubMed]

259. Tang, X.; Brindley, D.N. Lipid Phosphate Phosphatases and Cancer. *Biomolecules* **2020**, *10*, 1263. [CrossRef]

260. Stefan, C.; Jansen, S.; Bollen, M. NPP-type ectophosphodiesterases: Unity in diversity. *Trends Biochem. Sci.* **2005**, *30*, 542–550. [CrossRef]

261. Borza, R.; Salgado-Polo, F.; Moolenaar, W.H.; Perrakis, A. Structure and function of the ecto-nucleotide pyrophosphatase/phosphodiesterase (ENPP) family: Tidying up diversity. *J. Biol. Chem.* **2022**, *298*, 101526. [CrossRef] [PubMed]

262. Sakagami, H.; Aoki, J.; Natori, Y.; Nishikawa, K.; Kakehi, Y.; Natori, Y.; Arai, H. Biochemical and molecular characterization of a novel choline-specific glycerophosphodiester phosphodiesterase belonging to the nucleotide pyrophosphatase/phosphodiesterase family. *J. Biol. Chem.* **2005**, *280*, 23084–23093. [CrossRef] [PubMed]

263. Mulder, A.M.; Cravatt, B.F. Endocannabinoid metabolism in the absence of fatty acid amide hydrolase (FAAH): Discovery of phosphorylcholine derivatives of N-acyl ethanolamines. *Biochemistry* **2006**, *45*, 11267–11277. [CrossRef] [PubMed]

264. Greiner-Tollersrud, L.; Berg, T.; Stensland, H.M.; Evjen, G.; Greiner-Tollersrud, O.K. Bovine brain myelin glycerophosphocholine choline phosphodiesterase is an alkaline lysosphingomyelinase of the eNPP-family, regulated by lysosomal sorting. *Neurochem. Res.* **2013**, *38*, 300–310. [CrossRef] [PubMed]

265. Morita, J.; Kano, K.; Kato, K.; Takita, H.; Sakagami, H.; Yamamoto, Y.; Mihara, E.; Ueda, H.; Sato, T.; Tokuyama, H.; et al. Structure and biological function of ENPP6, a choline-specific glycerophosphodiester-phosphodiesterase. *Sci. Rep.* **2016**, *6*, 20995. [CrossRef] [PubMed]

266. Corda, D.; Kudo, T.; Zizza, P.; Iurisci, C.; Kawai, E.; Kato, N.; Yanaka, N.; Mariggiò, S. The developmentally regulated osteoblast phosphodiesterase GDE3 is glycerophosphoinositol-specific and modulates cell growth. *J. Biol. Chem.* **2009**, *284*, 24848–24856. [CrossRef] [PubMed]

267. Gorelik, A.; Liu, F.; Illes, K.; Nagar, B. Crystal structure of the human alkaline sphingomyelinase provides insights into substrate recognition. *J. Biol. Chem.* **2017**, *292*, 7087–7094. [CrossRef] [PubMed]
268. Duan, R.D.; Bergman, T.; Xu, N.; Wu, J.; Cheng, Y.; Duan, J.; Nelander, S.; Palmberg, C.; Nilsson, A. Identification of human intestinal alkaline sphingomyelinase as a novel ecto-enzyme related to the nucleotide phosphodiesterase family. *J. Biol. Chem.* **2003**, *278*, 38528–38536. [CrossRef] [PubMed]

269. Wu, J.; Nilsson, A.; Jönsson, B.A.; Stenstad, H.; Agace, W.; Cheng, Y.; Duan, R.D. Intestinal alkaline sphingomyelinase hydrolyses and inactivates platelet-activating factor by a phospholipase C activity. *Biochem. J.* **2006**, *394*, 299–308. [CrossRef]

270. Tokumura, A.; Majima, E.; Kariya, Y.; Tominaga, K.; Kogure, K.; Yasuda, K.; Fukuzawa, K. Identification of human plasma lysophospholipase D, a lysophosphatidic acid-producing enzyme, as autotaxin, a multifunctional phosphodiesterase. *J. Biol. Chem.* **2002**, *277*, 39436–39442. [CrossRef]

271. Umezu-Goto, M.; Kishi, Y.; Taira, A.; Hama, K.; Dohmae, N.; Takio, K.; Yamori, T.; Mills, G.B.; Inoue, K.; Aoki, J.; et al. Autotaxin has lysophospholipase D activity leading to tumor cell growth and motility by lysophosphatidic acid production. *J. Cell Biol.* **2002**, *158*, 227–233. [CrossRef] [PubMed]

272. Nakanaga, K.; Hama, K.; Aoki, J. Autotaxin--an LPA producing enzyme with diverse functions. *J. Biochem.* **2010**, *148*, 13–24. [CrossRef] [PubMed]

273. Aoki, J.; Inoue, A.; Okudaira, S. Two pathways for lysophosphatidic acid production. *Biochim. Biophys. Acta* **2008**, *1781*, 513–518. [CrossRef] [PubMed]

274. Moolenaar, W.H.; Perrakis, A. Insights into autotaxin: How to produce and present a lipid mediator. *Nat. Rev. Mol. Cell Biol.* **2011**, *12*, 674–679. [CrossRef] [PubMed]

275. Perrakis, A.; Moolenaar, W.H. Autotaxin: Structure-function and signaling. *J. Lipid Res.* **2014**, *55*, 1010–1018. [CrossRef] [PubMed]

276. Rancoule, C.; Dusaulcy, R.; Tréguer, K.; Grès, S.; Attané, C.; Saulnier-Blache, J.S. Involvement of autotaxin/lysophosphatidic acid signaling in obesity and impaired glucose homeostasis. *Biochimie* **2014**, *96*, 140–143. [CrossRef] [PubMed]

277. Barbayianni, E.; Kaffe, E.; Aidinis, V.; Kokotos, G. Autotaxin, a secreted lysophospholipase D, as a promising therapeutic target in chronic inflammation and cancer. *Prog. Lipid Res.* **2015**, *58*, 76–96. [CrossRef] [PubMed]

278. Yung, Y.C.; Stoddard, N.C.; Mirendil, H.; Chun, J. Lysophosphatidic Acid signaling in the nervous system. *Neuron* **2015**, *85*, 669–682. [CrossRef] [PubMed]

279. Leblanc, R.; Houssin, A.; Peyruchaud, O. Platelets, autotaxin and lysophosphatidic acid signalling: Win-win factors for cancer metastasis. *Br. J. Pharmacol.* **2018**, *175*, 3100–3110. [CrossRef]

280. Tang, X.; Benesch, M.G.K.; Brindley, D.N. Role of the autotaxin-lysophosphatidate axis in the development of resistance to cancer therapy. *Biochim. Biophys. Acta Mol. Cell Biol. Lipids* **2020**, *1865*, 158716. [CrossRef]

281. Jose, A.; Kienesberger, P.C. Autotaxin-LPA-LPP3 Axis in Energy Metabolism and Metabolic Disease. *Int. J. Mol. Sci.* **2021**, *22*, 9575. [CrossRef] [PubMed]

282. Alioli, C.; Demesmay, L.; Peyruchaud, O.; Machuca-Gayet, I. Autotaxin/Lysophosphatidic Acid Axis: From Bone Biology to Bone Disorders. *Int. J. Mol. Sci.* **2022**, *23*, 3427. [CrossRef] [PubMed]

283. Karalis, T.; Poulogiannis, G. The Emerging Role of LPA as an Oncometabolite. *Cells* **2024**, *13*, 629. [CrossRef] [PubMed]

284. Benesch, M.G.K.; Tang, X.; Brindley, D.N.; Takabe, K. Autotaxin and Lysophosphatidate Signaling: Prime Targets for Mitigating Therapy Resistance in Breast Cancer. *World J. Oncol.* **2024**, *15*, 1–13. [CrossRef] [PubMed]

285. Aoki, J.; Taira, A.; Takanezawa, Y.; Kishi, Y.; Hama, K.; Kishimoto, T.; Mizuno, K.; Saku, K.; Taguchi, R.; Arai, H. Serum lysophosphatidic acid is produced through diverse phospholipase pathways. *J. Biol. Chem.* **2002**, *277*, 48737–48744. [CrossRef] [PubMed]

286. Clair, T.; Aoki, J.; Koh, E.; Bandle, R.W.; Nam, S.W.; Ptaszynska, M.M.; Mills, G.B.; Schiffmann, E.; Liotta, L.A.; Stracke, M.L. Autotaxin hydrolyzes sphingosylphosphorylcholine to produce the regulator of migration, sphingosine-1-phosphate. *Cancer Res.* **2003**, *63*, 5446–5453. [PubMed]

287. Hausmann, J.; Kamtekar, S.; Christodoulou, E.; Day, J.E.; Wu, T.; Fulkerson, Z.; Albers, H.M.; van Meeteren, L.A.; Houben, A.J.; van Zeijl, L.; et al. Structural basis of substrate discrimination and integrin binding by autotaxin. *Nat. Struct. Mol. Biol.* **2011**, *18*, 198–204. [CrossRef] [PubMed]

288. Nishimasu, H.; Okudaira, S.; Hama, K.; Mihara, E.; Dohmae, N.; Inoue, A.; Ishitani, R.; Takagi, J.; Aoki, J.; Nureki, O. Crystal structure of autotaxin and insight into GPCR activation by lipid mediators. *Nat. Struct. Mol. Biol.* **2011**, *18*, 205–212. [CrossRef] [PubMed]

289. Tabchy, A.; Tigyi, G.; Mills, G.B. Location, location, location: A crystal-clear view of autotaxin saturating LPA receptors. *Nat. Struct. Mol. Biol.* **2011**, *18*, 117–118. [CrossRef]

290. Sano, T.; Baker, D.; Virag, T.; Wada, A.; Yatomi, Y.; Kobayashi, T.; Igarashi, Y.; Tigyi, G. Multiple mechanisms linked to platelet activation result in lysophosphatidic acid and sphingosine 1-phosphate generation in blood. *J. Biol. Chem.* **2002**, *277*, 21197–21206. [CrossRef]

291. Salgado-Polo, F.; Borza, R.; Matsoukas, M.T.; Marsais, F.; Jagerschmidt, C.; Waeckel, L.; Moolenaar, W.H.; Ford, P.; Heckmann, B.; Perrakis, A. Autotaxin facilitates selective LPA receptor signaling. *Cell Chem. Biol.* **2023**, *30*, 69–84.e14. [CrossRef] [PubMed]

292. Subramanian, C.; Yun, M.K.; Frank, M.M.; Rock, C.O. Lysophosphatidylglycerol (LPG) phospholipase D maintains membrane homeostasis in Staphylococcus aureus by converting LPG to lysophosphatidic acid. *J. Biol. Chem.* **2023**, *299*, 104863. [CrossRef] [PubMed]

293. Tsuda, S.; Okudaira, S.; Moriya-Ito, K.; Shimamoto, C.; Tanaka, M.; Aoki, J.; Arai, H.; Murakami-Murofushi, K.; Kobayashi, T. Cyclic phosphatidic acid is produced by autotaxin in blood. *J. Biol. Chem.* **2006**, *371*, 26081–26088. [CrossRef] [PubMed]
294. Fukasawa, K.; Gotoh, M.; Uwamizu, A.; Hirokawa, T.; Ishikawa, M.; Shimizu, Y.; Yamamoto, S.; Iwasa, K.; Yoshikawa, K.; Aoki, J.; et al. 2-Carba-lysophosphatidic acid is a novel β-lysophosphatidic acid analogue with high potential for lysophosphatidic acid receptor activation and autotaxin inhibition. *Sci. Rep.* **2021**, *11*, 17360. [CrossRef] [PubMed]

295. Tserendavga, B.; Ohshima, N.; Fujita, C.; Yuzawa, K.; Ohshima, M.; Yanaka, N.; Minamishima, Y.A.; Izumi, T. Characterization of recombinant murine GDE4 and GDE7, enzymes producing lysophosphatidic acid and/or cyclic phosphatidic acid. *J. Biochem.* **2022**, *170*, 713–727. [CrossRef] [PubMed]

296. Kitakaze, K.; Ali, H.; Kimoto, R.; Takenouchi, Y.; Ishimaru, H.; Yamashita, A.; Ueda, N.; Tanaka, T.; Okamoto, Y.; Tsuboi, K. GDE7 produces cyclic phosphatidic acid in the ER lumen functioning as a lysophospholipid mediator. *Commun. Biol.* **2023**, *6*, 524. [CrossRef] [PubMed]

297. Ueda, H.; Kobayashi, T.; Kishimoto, M.; Tsutsumi, T.; Okuyama, H. A possible pathway of phosphoinositide metabolism through EDTA-insensitive phospholipase A1 followed by lysophosphoinositide-specific phospholipase C in rat brain. *J. Neurochem.* **1993**, *61*, 1874–1881. [CrossRef] [PubMed]

298. Mechoulam, R.; Ben-Shabat, S.; Hanus, L.; Ligumsky, M.; Kaminski, N.E.; Schatz, A.R.; Gopher, A.; Almog, S.; Martin, B.R.; Compton, D.R. Identification of an endogenous 2-monoglyceride, present in canine gut, that binds to cannabinoid receptors. *Biochem. Pharmacol.* **1995**, *50*, 83–90. [CrossRef] [PubMed]

299. Sugiura, T.; Kondo, S.; Sukagawa, A.; Nakane, S.; Shinoda, A.; Itoh, K.; Yamashita, A.; Waku, K. 2-Arachidonoylglycerol: A possible endogenous cannabinoid receptor ligand in brain. *Biochem. Biophys. Res. Commun.* **1995**, *215*, 89–97. [CrossRef]

300. Murase, S.; Okuyama, H. A membrane-bound phospholipase C with an apparent specificity for lysophosphatidylinositol in porcine platelets. *J. Biol. Chem.* **1985**, *260*, 262–265. [CrossRef]

301. Volwerk, J.J.; Birrell, G.B.; Hedberg, K.K.; Griffith, O.H. A high level of cell surface phosphatidylinositol-specific phospholipase C activity is characteristic of growth-arrested 3T3 fibroblasts but not of transformed variants. *J. Cell. Physiol.* **1992**, *151*, 613–622. [CrossRef] [PubMed]

302. Birrell, G.B.; Hedberg, K.K.; Volwerk, J.J.; Griffith, O.H. Differential expression of phospholipase C specific for inositol phospholipids at the cell surface of rat glial cells and REF52 rat embryo fibroblasts. *J. Neurochem.* **1993**, *60*, 620–625. [CrossRef] [PubMed]

303. Tsutsumi, T.; Kobayashi, T.; Ueda, H.; Yamauchi, E.; Watanabe, S.; Okuyama, H. Lysophosphoinositide-specific phospholipase C in rat brain synaptic plasma membranes. *Neurochem. Res.* **1994**, *19*, 399–406. [CrossRef] [PubMed]

304. Tsutsumi, T.; Kobayashi, T.; Miyashita, M.; Watanabe, S.; Homma, Y.; Okuyama, H. A lysophosphoinositide-specific phospholipase C distinct from other phospholipase C families in rat brain. *Arch. Biochem. Biophys.* **1995**, *317*, 331–336. [CrossRef] [PubMed]

305. Yanaka, N. Mammalian glycerophosphodiester phosphodiesterases. *Biosci. Biotechnol. Biochem.* **2007**, *71*, 1811–1818. [CrossRef] [PubMed]

306. Corda, D.; Mosca, M.G.; Ohshima, N.; Grauso, L.; Yanaka, N.; Mariggiò, S. The emerging physiological roles of the glycerophosphodiesterase family. *FEBS J.* **2014**, *281*, 998–1016. [CrossRef] [PubMed]

307. Hejazian, S.M.; Pirmoradi, S.; Zununi Vahed, S.; Kumar Roy, R.; Hosseiniyan Khatibi, S.M. An update on Glycerophosphodiester Phosphodiesterases; From Bacteria to Human. *Protein J.* **2024**, *43*, 187–199. [CrossRef] [PubMed]

308. Simon, G.M.; Cravatt, B.F. Anandamide biosynthesis catalyzed by the phosphodiesterase GDE1 and detection of glycerophospho-N-acyl ethanolamine precursors in mouse brain. *J. Biol. Chem.* **2008**, *283*, 9341–9349. [CrossRef] [PubMed]

309. Yanaka, N.; Imai, Y.; Kawai, E.; Akatsuka, H.; Wakimoto, K.; Nogusa, Y.; Kato, N.; Chiba, H.; Kotani, E.; Omori, K.; et al. Novel membrane protein containing glycerophosphodiester phosphodiesterase motif is transiently expressed during osteoblast differentiation. *J. Biol. Chem.* **2003**, *278*, 43595–43602. [CrossRef]

310. van Veen, M.; Matas-Rico, E.; van de Wetering, K.; Leyton-Puig, D.; Kedziora, K.M.; De Lorenzi, V.; Stijf-Bultsma, Y.; van den Broek, B.; Jalink, K.; Sidenius, N.; et al. Negative regulation of urokinase receptor activity by a GPI-specific phospholipase C in breast cancer cells. *Elife* **2017**, *6*, e23649. [CrossRef]

311. Dobrowolski, M.; Cave, C.; Levy-Myers, R.; Lee, C.; Park, S.; Choi, B.R.; Xiao, B.; Yang, W.; Sockanathan, S. GDE3 regulates oligodendrocyte precursor proliferation via release of soluble CNTFRα. *Development* **2020**, *147*, dev180695. [CrossRef] [PubMed]

312. Ting, A.E.; Pagano, R.E. Detection of a phosphatidylinositol-specific phospholipase C at the surface of Swiss 3T3 cells and its potential role in the regulation of cell growth. *J. Biol. Chem.* **1990**, *265*, 5337–5340. [CrossRef] [PubMed]

313. Ting, A.E.; Pagano, R.E. Density-dependent inhibition of cell growth is correlated with the activity of a cell surface phosphatidylinositol-specific phospholipase C. *Eur. J. Cell Biol.* **1991**, *56*, 401–406. [PubMed]

314. Higgs, H.N.; Han, M.H.; Johnson, G.E.; Glomset, J.A. Cloning of a phosphatidic acid-preferring phospholipase A1 from bovine testis. *J. Biol. Chem.* **1998**, *273*, 5468–5477. [CrossRef] [PubMed]

315. Yamashita, A.; Kumazawa, T.; Koga, H.; Suzuki, N.; Oka, S.; Sugiura, T. Generation of lysophosphatidylinositol by DDHD domain containing 1 (DDHD1): Possible involvement of phospholipase D/phosphatidic acid in the activation of DDHD1. *Biochim. Biophys. Acta* **2010**, *1801*, 711–720. [CrossRef] [PubMed]

316. Matsumoto, N.; Nemoto-Sasaki, Y.; Oka, S.; Arai, S.; Wada, I.; Yamashita, A. Phosphorylation of human phospholipase A1 DDHD1 at newly identified phosphosites affects its subcellular localization. *J. Biol. Chem.* **2021**, *297*, 100851. [CrossRef] [PubMed]

317. Piñeiro, R.; Maffucci, T.; Falasca, M. The putative cannabinoid receptor GPR55 defines a novel autocrine loop in cancer cell proliferation. *Oncogene* **2011**, *30*, 142–152. [CrossRef] [PubMed]
318. Emmanouilidi, A.; Casari, I.; Gokcen Akkaya, B.; Maffucci, T.; Furic, L.; Guffanti, F.; Broggini, M.; Chen, X.; Maxuitenko, Y.Y.; Keeton, A.B.; et al. Inhibition of the Lysophosphatidylinositol Transporter ABCC1 Reduces Prostate Cancer Cell Growth and Sensitizes to Chemotherapy. *Cancers* **2020**, *12*, 2022. [CrossRef] [PubMed]

319. Ross, R.A. L-α-lysophosphatidylinositol meets GPR55: A deadly relationship. *Trends Pharmacol. Sci.* **2011**, *32*, 265–269. [CrossRef] [PubMed]

320. Alhouayek, M.; Masquelier, J.; Muccioli, G.G. Lysophosphatidylinositols, from Cell Membrane Constituents to GPR55 Ligands. *Trends Pharmacol. Sci.* **2018**, *39*, 586–604. [CrossRef]

321. Zachowski, A. Phospholipids in animal eukaryotic membranes: Transverse asymmetry and movement. *Biochem. J.* **1993**, *294* Pt 1, 1–14. [CrossRef] [PubMed]

322. Lhermusier, T.; Chap, H.; Payrastre, B. Platelet membrane phospholipid asymmetry: From the characterization of a scramblase activity to the identification of an essential protein mutated in Scott syndrome. *J. Thromb. Haemost.* **2011**, *9*, 1883–1891. [CrossRef] [PubMed]

323. Kobayashi, T.; Menon, A.K. Transbilayer lipid asymmetry. *Curr. Biol.* **2018**, *28*, R386–R391. [CrossRef] [PubMed]

324. Kale, S.D.; Gu, B.; Capelluto, D.G.; Dou, D.; Feldman, E.; Rumore, A.; Arredondo, F.D.; Hanlon, R.; Fudal, I.; Rouxel, T.; et al. External lipid PI3P mediates entry of eukaryotic pathogen effectors into plant and animal host cells. *Cell* **2010**, *142*, 284–295. [CrossRef] [PubMed]

325. Yoneda, A.; Kanemaru, K.; Matsubara, A.; Takai, E.; Shimozawa, M.; Satow, R.; Yamaguchi, H.; Nakamura, Y.; Fukami, K. Phosphatidylinositol 4,5-bisphosphate is localized in the plasma membrane outer leaflet and regulates cell adhesion and motility. *Biochem. Biophys. Res. Commun.* **2020**, *527*, 1050–1056. [CrossRef] [PubMed]

326. Mujalli, A.; Viaud, J.; Severin, S.; Gratacap, M.P.; Chicanne, G.; Hnia, K.; Payrastre, B.; Terrisse, A.D. Exploring the Role of PI3P in Platelets: Insights from a Novel External PI3P Pool. *Biomolecules* **2023**, *13*, 583. [CrossRef] [PubMed]

327. Kim, O.H.; Kang, G.H.; Hur, J.; Lee, J.; Jung, Y.; Hong, I.S.; Lee, H.; Seo, S.Y.; Lee, D.H.; Lee, C.S.; et al. Externalized phosphatidylinositides on apoptotic cells are eat-me signals recognized by CD14. *Cell Death Differ.* **2022**, *29*, 1423–1432. [CrossRef] [PubMed]

328. Agarwal, S.; Kim, H.; Chan, R.B.; Agarwal, S.; Williamson, R.; Cho, W.; Paolo, G.D.; Satchell, K.J. Autophagy and endosomal trafficking inhibition by Vibrio cholerae MARTX toxin phosphatidylinositol-3-phosphate-specific phospholipase A1 activity. *Nat. Commun.* **2015**, *6*, 8745. [CrossRef] [PubMed]

329. Kargl, J.; Balenga, N.; Parzmair, G.P.; Brown, A.J.; Heinemann, A.; Waldhoer, M. The cannabinoid receptor CB1 modulates the signaling properties of the lysophosphatidylinositol receptor GPR55. *J. Biol. Chem.* **2012**, *287*, 44234–44248. [CrossRef]

330. Martínez-Pinilla, E.; Reyes-Resina, I.; Oñatibia-Astibia, A.; Zamarbide, M.; Ricobaraza, A.; Navarro, G.; Moreno, E.; Dopeso-Reyes, I.G.; Sierra, S.; Rico, A.J.; et al. CB1 and GPR55 receptors are co-expressed and form heteromers in rat and monkey striatum. *Exp. Neurol.* **2014**, *261*, 44–52. [CrossRef]

331. Martínez-Pinilla, E.; Rico, A.J.; Rivas-Santisteban, R.; Lillo, J.; Roda, E.; Navarro, G.; Franco, R.; Lanciego, J.L. Expression of cannabinoid CB1 R-GPR55 heteromers in neuronal subtypes of the Macaca fascicularis striatum. *Ann. N. Y. Acad. Sci.* **2020**, *1475*, 34–42. [CrossRef] [PubMed]

332. Martínez-Pinilla, E.; Aguinaga, D.; Navarro, G.; Rico, A.J.; Oyarzábal, J.; Sánchez-Arias, J.A.; Lanciego, J.L.; Franco, R. Targeting CB1 and GPR55 Endocannabinoid Receptors as a Potential Neuroprotective Approach for Parkinson’s Disease. *Mol. Neurobiol.* **2019**, *56*, 5900–5910. [CrossRef] [PubMed]

333. Balenga, N.A.; Aflaki, E.; Kargl, J.; Platzer, W.; Schröder, R.; Blättermann, S.; Kostenis, E.; Brown, A.J.; Heinemann, A.; Waldhoer, M. GPR55 regulates cannabinoid 2 receptor-mediated responses in human neutrophils. *Cell Res.* **2011**, *21*, 1452–1469. [CrossRef] [PubMed]

334. Moreno, E.; Andradas, C.; Medrano, M.; Caffarel, M.M.; Pérez-Gómez, E.; Blasco-Benito, S.; Gómez-Cañas, M.; Pazos, M.R.; Irving, A.J.; Lluís, C.; et al. Targeting CB2-GPR55 receptor heteromers modulates cancer cell signaling. *J. Biol. Chem.* **2014**, *289*, 21960–21972. [CrossRef] [PubMed]

335. Balenga, N.A.; Martínez-Pinilla, E.; Kargl, J.; Schröder, R.; Peinhaupt, M.; Platzer, W.; Bálint, Z.; Zamarbide, M.; Dopeso-Reyes, I.G.; Ricobaraza, A.; et al. Heteromerization of GPR55 and cannabinoid CB2 receptors modulates signalling. *Br. J. Pharmacol.* **2014**, *171*, 5387–5406. [CrossRef] [PubMed]

336. Martínez-Pinilla, E.; Rabal, O.; Reyes-Resina, I.; Zamarbide, M.; Navarro, G.; Sánchez-Arias, J.A.; de Miguel, I.; Lanciego, J.L.; Oyarzábal, J.; Franco, R. Two Affinity Sites of the Cannabinoid Subtype 2 Receptor Identified by a Novel Homogeneous Binding Assay. *J. Pharmacol. Exp. Ther.* **2016**, *358*, 580–587. [CrossRef] [PubMed]

337. Akimov, M.G.; Gretskaya, N.M.; Dudina, P.V.; Sherstyanykh, G.D.; Zinchenko, G.N.; Serova, O.V.; Degtyaryova, K.O.; Deyev, I.E.; Bezuglov, V.V. The Mechanisms of GPR55 Receptor Functional Selectivity during Apoptosis and Proliferation Regulation in Cancer Cells. *Int. J. Mol. Sci.* **2023**, *24*, 5524. [CrossRef] [PubMed]

338. Cruz, S.L.; Sánchez-Miranda, E.; Castillo-Arellano, J.I.; Cervantes-Villagrana, R.D.; Ibarra-Sánchez, A.; González-Espinosa, C. Anandamide inhibits FcεRI-dependent degranulation and cytokine synthesis in mast cells through CB2 and GPR55 receptor activation. Possible involvement of CB2-GPR55 heteromers. *Int. Immunopharmacol.* **2018**, *64*, 298–307. [CrossRef] [PubMed]

339. Menéndez-Pérez, C.; Rivas-Santisteban, R.; Del Valle, E.; Tolivia, J.; Navarro, A.; Franco, R.; Martínez-Pinilla, E. Heteromers Formed by GPR55 and Either Cannabinoid CB1 or CB2 Receptors Are Upregulated in the Prefrontal Cortex of Multiple Sclerosis Patients. *Int. J. Mol. Sci.* **2024**, *25*, 4176. [CrossRef]
340. BioGPS. Available online: http://biogps.org/#goto=genereport&id=71584 (accessed on 29 December 2023).

341. The Human Protein Atlas. Available online: https://www.proteinatlas.org/ENSG00000130055-GDPD2 (accessed on 29 December 2023).

342. Inloes, J.M.; Jing, H.; Cravatt, B.F. The Spastic Paraplegia-Associated Phospholipase DDHD1 Is a Primary Brain Phosphatidylinositol Lipase. *Biochemistry* **2018**, *57*, 5759–5767. [CrossRef]

343. Morikawa, T.; Ohishi, H.; Kosaka, K.; Shimojo, T.; Nagano, A.; Taniguchi, I.; Fujioka, R.; Moriyama, K.; Unoki, M.; Takahashi, M.; et al. Ddhd1 knockout mouse as a model of locomotive and physiological abnormality in familial spastic paraplegia. *Biosci. Rep.* **2021**, *41*, BSR20204171. [CrossRef] [PubMed]

344. Morikawa, T.; Takahashi, M.; Izumi, Y.; Bamba, T.; Moriyama, K.; Hattori, G.; Fujioka, R.; Miura, S.; Shibata, H. Oleic Acid-Containing Phosphatidylinositol Is a Blood Biomarker Candidate for SPG28. *Biomedicines* **2023**, *11*, 1092. [CrossRef] [PubMed]

345. Tsutsumi, T.; Kawabata, K.; Yamazaki, N.; Tsukigawa, K.; Nishi, H.; Tokumura, A. Extracellular and intracellular productions of lysophosphatidic acids and cyclic phosphatidic acids by lysophospholipase D from exogenously added lysophosphatidylcholines to cultured NRK52E cells. *Biochim. Biophys. Acta Mol. Cell Biol. Lipids* **2023**, *1868*, 159349. [CrossRef] [PubMed]

346. Greiner-Tollersrud, O.K. The non-classical N-glycan processing pathway of bovine brain ecto-nucleotide phosphodiesterase/pyrophosphatase 6 (eNPP6) is brain specific and not due to mannose-6-phosphorylation. *Neurochem. Res.* **2014**, *39*, 2025–2029. [CrossRef] [PubMed]

347. Wu, J.; Liu, F.; Nilsson, A.; Duan, R.D. Pancreatic trypsin cleaves intestinal alkaline sphingomyelinase from mucosa and enhances the sphingomyelinase activity. *Am. J. Physiol. Gastrointest. Liver Physiol.* **2004**, *287*, G967–G973. [CrossRef] [PubMed]

348. Pinheiro, R.G.; Leal Rato, M.; Silva, C.S.; Soares, M.P.; Carvalho, V.; Guedes, L.C. A novel frameshift DDHD1 mutation in a patient with hereditary spastic paraplegia type 28: Case report and review of the literature. *Park. Relat. Disord.* **2024**, *118*, 105931. [CrossRef] [PubMed]

349. Baba, T.; Kashiwagi, Y.; Arimitsu, N.; Kogure, T.; Edo, A.; Maruyama, T.; Nakao, K.; Nakanishi, H.; Kinoshita, M.; Frohman, M.A.; et al. Phosphatidic acid (PA)-preferring phospholipase A1 regulates mitochondrial dynamics. *J. Biol. Chem.* **2014**, *289*, 11497–11511. [CrossRef]

350. Liguori, R.; Giannoccaro, M.P.; Arnoldi, A.; Citterio, A.; Tonon, C.; Lodi, R.; Bresolin, N.; Bassi, M.T. Impairment of brain and muscle energy metabolism detected by magnetic resonance spectroscopy in hereditary spastic paraparesis type 28 patients with DDHD1 mutations. *J. Neurol.* **2014**, *261*, 1789–1793. [CrossRef] [PubMed]

351. Mignarri, A.; Rubegni, A.; Tessa, A.; Stefanucci, S.; Malandrini, A.; Cardaioli, E.; Meschini, M.C.; Stromillo, M.L.; Doccini, S.; Federico, A.; et al. Mitochondrial dysfunction in hereditary spastic paraparesis with mutations in DDHD1/SPG28. *J. Neurol. Sci.* **2016**, *362*, 287–291. [CrossRef]

352. Yadav, P.K.; Rajasekharan, R. Misregulation of a DDHD Domain-containing Lipase Causes Mitochondrial Dysfunction in Yeast. *J. Biol. Chem.* **2016**, *291*, 18562–18581. [CrossRef]

353. Maemoto, Y.; Maruyama, T.; Nemoto, K.; Baba, T.; Motohashi, M.; Ito, A.; Tagaya, M.; Tani, K. DDHD1, but Not DDHD2, Suppresses Neurite Outgrowth in SH-SY5Y and PC12 Cells by Regulating Protein Transport From Recycling Endosomes. *Front. Cell Dev. Biol.* **2020**, *8*, 670. [CrossRef] [PubMed]

354. Doan, R.N.; Lim, E.T.; De Rubeis, S.; Betancur, C.; Cutler, D.J.; Chiocchetti, A.G.; Overman, L.M.; Soucy, A.; Goetze, S.; Freitag, C.M.; et al. Recessive gene disruptions in autism spectrum disorder. *Nat. Genet.* **2019**, *51*, 1092–1098. [CrossRef] [PubMed]

355. Raimondo, S.; Cristaldi, M.; Fontana, S.; Saieva, L.; Monteleone, F.; Calabrese, G.; Giavaresi, G.; Parenti, R.; Alessandro, R. The phospholipase DDHD1 as a new target in colorectal cancer therapy. *J. Exp. Clin. Cancer Res.* **2018**, *37*, 82. [CrossRef] [PubMed]

356. Yang, X.; Wu, W.; Pan, Y.; Zhou, Q.; Xu, J.; Han, S. Immune-related genes in tumor-specific CD4+ and CD8+ T cells in colon cancer. *BMC Cancer* **2020**, *20*, 585. [CrossRef] [PubMed]

357. Kitamura, C.; Sonoda, H.; Anzai, H.; Nagai, Y.; Abe, S.; Yokoyama, Y.; Ishii, H.; Kishikawa, J.; Emoto, S.; Murono, K.; et al. Expression of Lysophosphatidylinositol Signaling-relevant Molecules in Colorectal Cancer. *Anticancer Res.* **2021**, *41*, 2349–2355. [CrossRef] [PubMed]

358. Shen, G.Y.; Yang, P.J.; Zhang, W.S.; Chen, J.B.; Tian, Q.Y.; Zhang, Y.; Han, B. Identification of a Prognostic Gene Signature Based on Lipid Metabolism-Related Genes in Esophageal Squamous Cell Carcinoma. *Pharmgenomics Pers. Med.* **2023**, *16*, 959–972. [CrossRef] [PubMed]

359. Park, S.; Lee, C.; Sabharwal, P.; Zhang, M.; Meyers, C.L.; Sockanathan, S. GDE2 promotes neurogenesis by glycosylphosphatidylinositol-anchor cleavage of RECK. *Science* **2013**, *339*, 324–328. [CrossRef] [PubMed]

360. Nakamura, M.; Li, Y.; Choi, B.R.; Matas-Rico, E.; Troncoso, J.; Takahashi, C.; Sockanathan, S. GDE2-RECK controls ADAM10 α-secretase-mediated cleavage of amyloid precursor protein. *Sci. Transl. Med.* **2021**, *13*, eabe6178. [CrossRef] [PubMed]

361. Matas-Rico, E.; van Veen, M.; Leyton-Puig, D.; van den Berg, J.; Koster, J.; Kedziora, K.M.; Molenaar, B.; Weerts, M.J.; de Rink, I.; Medema, R.H.; et al. Glycerophosphodiesterase GDE2 Promotes Neuroblastoma Differentiation through Glypican Release and Is a Marker of Clinical Outcome. *Cancer Cell* **2016**, *30*, 548–562. [CrossRef]

362. Cave, C.; Park, S.; Rodriguez, M.; Nakamura, M.; Hoke, A.; Pletnikov, M.; Sockanathan, S. GDE2 is essential for neuronal survival in the postnatal mammalian spinal cord. *Mol. Neurodegener.* **2017**, *12*, 8. [CrossRef]

363. Westerhaus, A.; Joseph, T.; Meyers, A.J.; Jang, Y.; Na, C.H.; Cave, C.; Sockanathan, S. The distribution and function of GDE2, a regulator of spinal motor neuron survival, are disrupted in Amyotrophic Lateral Sclerosis. *Acta Neuropathol. Commun.* **2022**, *10*, 73. [CrossRef] [PubMed]
364. van Veen, M.; Mans, L.A.; Matas-Rico, E.; van Pelt, J.; Perrakis, A.; Moolenaar, W.H.; Haramis, A.G. Glycerophosphodiesterase GDE2/GDPD5 affects pancreas differentiation in zebrafish. *Int. J. Biochem. Cell Biol.* **2018**, *94*, 71–78. [CrossRef] [PubMed]

365. Daudelin, D.; Westerhaus, A.; Zhang, N.; Leyder, E.; Savonenko, A.; Sockanathan, S. Loss of GDE2 leads to complex behavioral changes including memory impairment. *Behav. Brain Funct.* **2024**, *20*, 7. [CrossRef] [PubMed]

366. Choi, B.R.; Cave, C.; Na, C.H.; Sockanathan, S. GDE2-Dependent Activation of Canonical Wnt Signaling in Neurons Regulates Oligodendrocyte Maturation. *Cell Rep.* **2020**, *31*, 107540. [CrossRef] [PubMed]

367. Choi, B.R.; Dobrowolski, M.; Sockanathan, S. GDE2 expression in oligodendroglia regulates the pace of oligodendrocyte maturation. *Dev. Dyn.* **2021**, *250*, 513–526. [CrossRef] [PubMed]

368. Li, M.; Zheng, J.; He, X.; Zhang, X. Tiki proteins are glycosylphosphatidylinositol-anchored proteases. *FEBS Lett.* **2022**, *596*, 1037–1046. [CrossRef] [PubMed]

369. Nogusa, Y.; Fujioka, Y.; Komatsu, R.; Kato, N.; Yanaka, N. Isolation and characterization of two serpentine membrane proteins containing glycerophosphodiester phosphodiesterase, GDE2 and GDE6. *Gene* **2004**, *337*, 173–179. [CrossRef] [PubMed]

370. McKean, M.; Napoli, F.R.; Hasan, T.; Joseph, T.; Wheeler, A.; Beebe, K.; Soriano-Cruz, S.; Kawano, M.; Cave, C. GDE6 promotes progenitor identity in the vertebrate neural tube. *Front. Neurosci.* **2023**, *17*, 1047767. [CrossRef] [PubMed]

371. Salgado-Polo, F.; van Veen, M.; van den Broek, B.; Jalink, K.; Leyton-Puig, D.; Perrakis, A.; Moolenaar, W.H.; Matas-Rico, E. Sequence-dependent trafficking and activity of GDE2, a GPI-specific phospholipase promoting neuronal differentiation. *J. Cell Sci.* **2020**, *133*, jcs235044. [CrossRef]

372. Levy-Myers, R.; Daudelin, D.; Na, C.H.; Sockanathan, S. An independent regulator of global release pathways in astrocytes generates a subtype of extracellular vesicles required for postsynaptic function. *Sci. Adv.* **2023**, *9*, eadg2067. [CrossRef]

373. Brindley, D.N.; Waggoner, D.W. Mammalian lipid phosphate phosphohydrolases. *J. Biol. Chem.* **1998**, *273*, 24281–24284. [CrossRef] [PubMed]

374. Song, E.; Ghil, S. Crosstalk between cannabinoid receptor 2 and lysophosphatidic acid receptor 5. *Biochem. Biophys. Res. Commun.* **2023**, *666*, 154–161. [CrossRef] [PubMed]

375. Chang, W.; Fa, H.; Xiao, D.; Wang, J. MicroRNA-184 alleviates insulin resistance in cardiac myocytes and high fat diet-induced cardiac dysfunction in mice through the LPP3/DAG pathway. *Mol. Cell. Endocrinol.* **2020**, *508*, 110793. [CrossRef] [PubMed]

376. Hooks, S.B.; Santos, W.L.; Im, D.S.; Heise, C.E.; Macdonald, T.L.; Lynch, K.R. Lysophosphatidic acid-induced mitogenesis is regulated by lipid phosphate phosphatases and is Edg-receptor independent. *J. Biol. Chem.* **2001**, *276*, 4611–4621. [CrossRef] [PubMed]

377. Smyth, S.S.; Sciorra, V.A.; Sigal, Y.J.; Pamuklar, Z.; Wang, Z.; Xu, Y.; Prestwich, G.D.; Morris, A.J. Lipid phosphate phosphatases regulate lysophosphatidic acid production and signaling in platelets: Studies using chemical inhibitors of lipid phosphate phosphatase activity. *J. Biol. Chem.* **2003**, *278*, 43214–43223. [CrossRef] [PubMed]

378. Williams, J.R.; Khandoga, A.L.; Goyal, P.; Fells, J.I.; Perygin, D.H.; Siess, W.; Parrill, A.L.; Tigyi, G.; Fujiwara, Y. Unique ligand selectivity of the GPR92/LPA5 lysophosphatidate receptor indicates role in human platelet activation. *J. Biol. Chem.* **2009**, *284*, 17304–17319. [CrossRef] [PubMed]

379. Jasinska, R.; Zhang, Q.X.; Pilquil, C.; Singh, I.; Xu, J.; Dewald, J.; Dillon, D.A.; Berthiaume, L.G.; Carman, G.M.; Waggoner, D.W.; et al. Lipid phosphate phosphohydrolase-1 degrades exogenous glycerolipid and sphingolipid phosphate esters. *Biochem. J.* **1999**, *340* Pt 3, 677–686. [CrossRef] [PubMed]

380. Pilquil, C.; Dewald, J.; Cherney, A.; Gorshkova, I.; Tigyi, G.; English, D.; Natarajan, V.; Brindley, D.N. Lipid phosphate phosphatase-1 regulates lysophosphatidate-induced fibroblast migration by controlling phospholipase D2-dependent phosphatidate generation. *J. Biol. Chem.* **2006**, *281*, 38418–38429. [CrossRef] [PubMed]

381. Long, J.S.; Yokoyama, K.; Tigyi, G.; Pyne, N.J.; Pyne, S. Lipid phosphate phosphatase-1 regulates lysophosphatidic acid- and platelet-derived-growth-factor-induced cell migration. *Biochem. J.* **2006**, *394*, 495–500. [CrossRef]

382. Yukiura, H.; Kano, K.; Kise, R.; Inoue, A.; Aoki, J. LPP3 localizes LPA6 signalling to non-contact sites in endothelial cells. *J. Cell Sci.* **2015**, *128*, 3871–3877. [CrossRef]

383. Tomsig, J.L.; Snyder, A.H.; Berdyshev, E.V.; Skobeleva, A.; Mataya, C.; Natarajan, V.; Brindley, D.N.; Lynch, K.R. Lipid phosphate phosphohydrolase type 1 (LPP1) degrades extracellular lysophosphatidic acid in vivo. *Biochem. J.* **2009**, *419*, 611–618. [CrossRef] [PubMed]

384. Mueller, P.A.; Yang, L.; Ubele, M.; Mao, G.; Brandon, J.; Vandra, J.; Nichols, T.C.; Escalante-Alcalde, D.; Morris, A.J.; Smyth, S.S. Coronary Artery Disease Risk-Associated Plpp3 Gene and Its Product Lipid Phosphate Phosphatase 3 Regulate Experimental Atherosclerosis. *Arterioscler. Thromb. Vasc. Biol.* **2019**, *39*, 2261–2272. [CrossRef] [PubMed]

385. Busnelli, M.; Manzini, S.; Hilvo, M.; Parolini, C.; Ganzetti, G.S.; Dellera, F.; Ekroos, K.; Jänis, M.; Escalante-Alcalde, D.; Sirtori, C.R.; et al. Liver-specific deletion of the Plpp3 gene alters plasma lipid composition and worsens atherosclerosis in apoE-/- mice. *Sci. Rep.* **2017**, *7*, 44503. [CrossRef] [PubMed]

386. Chandra, M.; Escalante-Alcalde, D.; Bhuiyan, M.S.; Orr, A.W.; Kevil, C.; Morris, A.J.; Nam, H.; Dominic, P.; McCarthy, K.J.; Miriyala, S.; et al. Cardiac-specific inactivation of LPP3 in mice leads to myocardial dysfunction and heart failure. *Redox Biol.* **2018**, *14*, 261–271. [CrossRef] [PubMed]

387. Yue, J.; Yokoyama, K.; Balazs, L.; Baker, D.L.; Smalley, D.; Pilquil, C.; Brindley, D.N.; Tigyi, G. Mice with transgenic overexpression of lipid phosphate phosphatase-1 display multiple organotypic deficits without alteration in circulating lysophosphatidate level. *Cell. Signal.* **2004**, *16*, 385–399. [CrossRef] [PubMed]
388. Zhang, N.; Sundberg, J.P.; Gridley, T. Mice mutant for Ppap2c, a homolog of the germ cell migration regulator wunen, are viable and fertile. *Genesis* **2000**, *27*, 137–140. [CrossRef] [PubMed]

389. Escalante-Alcalde, D.; Hernandez, L.; Le Stunff, H.; Ryu Maeda, R.; Lee, H.S.; Cheng, J.G.; Sciorra, V.A.; Daar, I.; Spiegel, S.; Morris, A.J.; et al. The lipid phosphatase LPP3 regulates extra-embryonic vasculogenesis and axis patterning. *Development* **2003**, *130*, 4623–4637. [CrossRef] [PubMed]

390. Jia, Y.J.; Kai, M.; Wada, I.; Sakane, F.; Kanoh, H. Differential localization of lipid phosphate phosphatases 1 and 3 to cell surface subdomains in polarized MDCK cells. *FEBS Lett.* **2003**, *552*, 240–246. [CrossRef] [PubMed]

391. Kai, M.; Sakane, F.; Jia, Y.J.; Imai, S.; Yasuda, S.; Kanoh, H. Lipid phosphate phosphatases 1 and 3 are localized in distinct lipid rafts. *J. Biochem.* **2006**, *140*, 677–686. [CrossRef]

392. Tang, X.; Cromwell, C.R.; Liu, R.; Godbout, R.; Hubbard, B.P.; McMullen, T.P.W.; Brindley, D.N. Lipid phosphate phosphatase-2 promotes tumor growth through increased c-Myc expression. *Theranostics* **2022**, *12*, 5675–5690. [CrossRef]

393. Benesch, M.G.K.; Wu, R.; Tang, X.; Brindley, D.N.; Ishikawa, T.; Takabe, K. Decreased Lipid Phosphate Phosphatase 1/3 and Increased Lipid Phosphate Phosphatase 2 Expression in the Human Breast Cancer Tumor Microenvironment Promotes Tumor Progression and Immune System Evasion. *Cancers* **2023**, *15*, 2299. [CrossRef] [PubMed]

394. Busnelli, M.; Manzini, S.; Parolini, C.; Escalante-Alcalde, D.; Chiesa, G. Lipid phosphate phosphatase 3 in vascular pathophysiology. *Atherosclerosis* **2018**, *271*, 156–165. [CrossRef]

395. Smyth, S.S.; Kraemer, M.; Yang, L.; Van Hoose, P.; Morris, A.J. Roles for lysophosphatidic acid signaling in vascular development and disease. *Biochim. Biophys. Acta Mol. Cell Biol. Lipids* **2020**, *1865*, 158734. [CrossRef]

396. Davidson, J.; Rotondo, D. The potential role of the lipid phosphate phosphatase 3 (Plpp3) gene in cardiovascular disease. *Curr. Opin. Lipidol.* **2020**, *31*, 258–259. [CrossRef]

397. Jose, A.; Fernando, J.; Kienesberger, P. Lysophosphatidic Acid Metabolism and Signaling in Heart Disease. *Can. J. Physiol. Pharmacol.* **2024**. [CrossRef] [PubMed]

398. Panchatcharam, M.; Salous, A.K.; Brandon, J.; Miriyala, S.; Wheeler, J.; Patil, P.; Sunkara, M.; Morris, A.J.; Escalante-Alcalde, D.; Smyth, S.S. Mice with targeted inactivation of ppap2b in endothelial and hematopoietic cells display enhanced vascular inflammation and permeability. *Arterioscler. Thromb. Vasc. Biol.* **2014**, *34*, 837–845. [CrossRef] [PubMed]

399. Chatterjee, I.; Baruah, J.; Lurie, E.E.; Wary, K.K. Endothelial lipid phosphate phosphatase-3 deficiency that disrupts the endothelial barrier function is a modifier of cardiovascular development. *Cardiovasc. Res.* **2016**, *111*, 105–118. [CrossRef]

400. Tripathi, H.; Shindo, K.; Donahue, R.R.; Gao, E.; Kuppa, A.; ElKammar, M.; Morris, A.J.; Smyth, S.S.; Abdel-Latif, A. Myeloid-Specific Deletion of Lipid Plpp3 (Phosphate Phosphatase 3) Increases Cardiac Inflammation After Myocardial Infarction. *Arterioscler. Thromb. Vasc. Biol.* **2023**, *43*, 379–381. [CrossRef]

401. Chabowski, D.S.; Hughes, W.E.; Hockenberry, J.C.; LoGiudice, J.; Beyer, A.M.; Gutterman, D.D. Lipid phosphate phosphatase 3 maintains NO-mediated flow-mediated dilatation in human adipose resistance arterioles. *J. Physiol.* **2023**, *601*, 469–481. [CrossRef]

402. Wu, C.; Huang, R.T.; Kuo, C.H.; Kumar, S.; Kim, C.W.; Lin, Y.C.; Chen, Y.J.; Birukova, A.; Birukov, K.G.; Dulin, N.O.; et al. Mechanosensitive PPAP2B Regulates Endothelial Responses to Atherorelevant Hemodynamic Forces. *Circ. Res.* **2015**, *117*, e41–e53. [CrossRef]

403. Bot, M.; de Jager, S.C.; MacAleese, L.; Lagraauw, H.M.; van Berkel, T.J.; Quax, P.H.; Kuiper, J.; Heeren, R.M.; Biessen, E.A.; Bot, I. Lysophosphatidic acid triggers mast cell-driven atherosclerotic plaque destabilization by increasing vascular inflammation. *J. Lipid Res.* **2013**, *54*, 1265–1274. [CrossRef] [PubMed]

404. Van Hoose, P.M.; Yang, L.; Kraemer, M.; Ubele, M.; Morris, A.J.; Smyth, S.S. Lipid phosphate phosphatase 3 in smooth muscle cells regulates angiotensin II-induced abdominal aortic aneurysm formation. *Sci. Rep.* **2022**, *12*, 5664. [CrossRef] [PubMed]

405. Navab, M.; Chattopadhyay, A.; Hough, G.; Meriwether, D.; Fogelman, S.I.; Wagner, A.C.; Grijalva, V.; Su, F.; Anantharamaiah, G.M.; Hwang, L.H.; et al. Source and role of intestinally derived lysophosphatidic acid in dyslipidemia and atherosclerosis. *J. Lipid Res.* **2015**, *56*, 871–887. [CrossRef] [PubMed]

406. Hiramatsu, T.; Sonoda, H.; Takanezawa, Y.; Morikawa, R.; Ishida, M.; Kasahara, K.; Sanai, Y.; Taguchi, R.; Aoki, J.; Arai, H. Biochemical and molecular characterization of two phosphatidic acid-selective phospholipase A1s, mPA-PLA1alpha and mPA-PLA1beta. *J. Biol. Chem.* **2003**, *278*, 49438–49447. [CrossRef] [PubMed]

407. Jin, W.; Broedl, U.C.; Monajemi, H.; Glick, J.M.; Rader, D.J. Lipase H, a new member of the triglyceride lipase family synthesized by the intestine. *Genomics* **2002**, *80*, 268–273. [CrossRef] [PubMed]

408. Remington, S.G.; Nelson, J.D. mRNA encoding a new lipolytic enzyme expressed in rabbit lacrimal glands. *Investig. Ophthalmol. Vis. Sci.* **2002**, *43*, 3617–3624.

409. Holmes, R.S.; Cox, L.A. Review. Comparative structures and evolution of mammalian lipase I (LIPI) genes and proteins: A close relative of vertebrate phospholipase LIPH. *Nat. Sci.* **2012**, *4*, 1165–1178. [CrossRef]

410. Nanjundan, M.; Possmayer, F. Pulmonary lipid phosphate phosphohydrolase in plasma membrane signalling platforms. *Biochem. J.* **2001**, *358*, 637–646. [CrossRef] [PubMed]

411. Sciorra, V.A.; Morris, A.J. Sequential actions of phospholipase D and phosphatidic acid phosphohydrolase 2b generate diglyceride in mammalian cells. *Mol. Biol. Cell* **1999**, *10*, 3863–3876. [CrossRef]

412. Scanlan, M.J.; Gordon, C.M.; Williamson, B.; Lee, S.Y.; Chen, Y.T.; Stockert, E.; Jungbluth, A.; Ritter, G.; Jäger, D.; Jäger, E.; et al. Identification of cancer/testis genes by database mining and mRNA expression analysis. *Int. J. Cancer* **2002**, *98*, 485–492. [CrossRef]
413. Hesse, M.; Willscher, E.; Schmiedel, B.J.; Posch, S.; Golbik, R.P.; Staege, M.S. Sequence and expression of the chicken membrane-associated phospholipases A1 alpha (LIPH) and beta (LIPI). *Mol. Biol. Rep.* **2012**, *39*, 761–769. [CrossRef] [PubMed]

414. Willier, S.; Butt, E.; Grunewald, T.G. Lysophosphatidic acid (LPA) signalling in cell migration and cancer invasion: A focussed review and analysis of LPA receptor gene expression on the basis of more than 1700 cancer microarrays. *Biol. Cell* **2013**, *105*, 317–333. [CrossRef] [PubMed]

415. Wen, X.Y.; Hegele, R.A.; Wang, J.; Wang, D.Y.; Cheung, J.; Wilson, M.; Yahyapour, M.; Bai, Y.; Zhuang, L.; Skaug, J.; et al. Identification of a novel lipase gene mutated in lpd mice with hypertriglyceridemia and associated with dyslipidemia in humans. *Hum. Mol. Genet.* **2003**, *12*, 1131–1143. [CrossRef] [PubMed]

416. Seki, Y.; Yoshida, Y.; Ishimine, H.; Shinozaki-Ushiku, A.; Ito, Y.; Sumitomo, K.; Nakajima, J.; Fukayama, M.; Michiue, T.; Asashima, M.; et al. Lipase member H is a novel secreted protein selectively upregulated in human lung adenocarcinomas and bronchioloalveolar carcinomas. *Biochem. Biophys. Res. Commun.* **2014**, *443*, 1141–1147. [CrossRef] [PubMed]

417. Zhang, Y.; Zhu, X.; Qiao, X.; Gu, X.; Xue, J.; Han, Y.; Sun, L.; Cui, M.; Liu, C. LIPH promotes metastasis by enriching stem-like cells in triple-negative breast cancer. *J. Cell. Mol. Med.* **2020**, *24*, 9125–9134. [CrossRef] [PubMed]

418. Han, L.; Jiang, Y.; Shi, M.; Gan, L.; Wu, Z.; Xue, M.; Zhu, Y.; Xiong, C.; Wang, T.; Lin, X.; et al. LIPH contributes to glycolytic phenotype in pancreatic ductal adenocarcinoma by activating LPA/LPAR axis and maintaining ALDOA stability. *J. Transl. Med.* **2023**, *21*, 838. [CrossRef] [PubMed]

419. Zhang, M.; Jiang, L.; Liu, X.Y.; Liu, F.X.; Zhang, H.; Zhang, Y.J.; Tang, X.M.; Ma, Y.S.; Wu, H.Y.; Diao, X.; et al. KLK10/LIPH/PARD6B/SLC52A3 are promising molecular biomarkers for the prognosis of pancreatic cancer through a ceRNA network. *Heliyon* **2024**, *10*, e24287. [CrossRef] [PubMed]

420. Zhang, T.; Yao, H.; Wang, H.; Sui, T. Development of Woolly Hair and Hairlessness in a CRISPR-Engineered Mutant Mouse Model with KRT71 Mutations. *Cells* **2023**, *12*, 1781. [CrossRef] [PubMed]

421. Aoki, J. Mechanisms of lysophosphatidic acid production. *Semin. Cell Dev. Biol.* **2004**, *15*, 477–489. [CrossRef]

422. Fourcade, O.; Simon, M.F.; Viodé, C.; Rugani, N.; Leballe, F.; Ragab, A.; Fournié, B.; Sarda, L.; Chap, H. Secretory phospholipase A2 generates the novel lipid mediator lysophosphatidic acid in membrane microvesicles shed from activated cells. *Cell* **1995**, *80*, 919–927. [CrossRef]

423. Le Balle, F.; Simon, M.F.; Meijer, S.; Fourcade, O.; Chap, H. Membrane sidedness of biosynthetic pathways involved in the production of lysophosphatidic acid. *Adv. Enzym. Regul.* **1999**, *39*, 275–284. [CrossRef] [PubMed]

424. Bräuer, A.U.; Nitsch, R. Plasticity-related genes (PRGs/LRPs): A brain-specific class of lysophospholipid-modifying proteins. *Biochim. Biophys. Acta* **2008**, *1781*, 595–600. [CrossRef] [PubMed]

425. Strauss, U.; Bräuer, A.U. Current views on regulation and function of plasticity-related genes (PRGs/LPPRs) in the brain. *Biochim. Biophys. Acta* **2013**, *1831*, 133–138. [CrossRef] [PubMed]

426. Trimbuch, T.; Beed, P.; Vogt, J.; Schuchmann, S.; Maier, N.; Kintscher, M.; Breustedt, J.; Schuelke, M.; Streu, N.; Kieselmann, O.; et al. Synaptic PRG-1 modulates excitatory transmission via lipid phosphate-mediated signaling. *Cell* **2009**, *138*, 1222–1235. [CrossRef] [PubMed]

427. Tokumitsu, H.; Hatano, N.; Tsuchiya, M.; Yurimoto, S.; Fujimoto, T.; Ohara, N.; Kobayashi, R.; Sakagami, H. Identification and characterization of PRG-1 as a neuronal calmodulin-binding protein. *Biochem. J.* **2010**, *431*, 81–91. [CrossRef] [PubMed]

428. Vogt, J.; Yang, J.W.; Mobascher, A.; Cheng, J.; Li, Y.; Liu, X.; Baumgart, J.; Thalman, C.; Kirischuk, S.; Unichenko, P.; et al. Molecular cause and functional impact of altered synaptic lipid signaling due to a prg-1 gene SNP. *EMBO Mol. Med.* **2016**, *8*, 25–38. [CrossRef] [PubMed]

429. Liu, X.; Huai, J.; Endle, H.; Schlüter, L.; Fan, W.; Li, Y.; Richers, S.; Yurugi, H.; Rajalingam, K.; Ji, H.; et al. PRG-1 Regulates Synaptic Plasticity via Intracellular PP2A/β1-Integrin Signaling. *Dev. Cell* **2016**, *38*, 275–290. [CrossRef] [PubMed]

430. Nasseri, G.G.; Matin, N.; Wild, A.R.; Tosefsky, K.; Flibotte, S.; Stacey, R.G.; Hollman, R.B.; Foster, L.J.; Bamji, S.X. Synaptic activity-dependent changes in the hippocampal palmitoylome. *Sci. Signal.* **2022**, *15*, eadd2519. [CrossRef] [PubMed]

431. Zhang, Q.X.; Pilquil, C.S.; Dewald, J.; Berthiaume, L.G.; Brindley, D.N. Identification of structurally important domains of lipid phosphate phosphatase-1: Implications for its sites of action. *Biochem. J.* **2000**, *345 Pt 2*, 181–184. [CrossRef]

432. Bräuer, A.U.; Savaskan, N.E.; Kühn, H.; Prehn, S.; Ninnemann, O.; Nitsch, R. A new phospholipid phosphatase, PRG-1, is involved in axon growth and regenerative sprouting. *Nat. Neurosci.* **2003**, *6*, 572–578. [CrossRef]

433. McDermott, M.I.; Sigal, Y.J.; Sciorra, V.A.; Morris, A.J. Is PRG-1 a new lipid phosphatase. *Nat. Neurosci.* **2004**, *7*, 789. [CrossRef] [PubMed]

434. Pagano, R.E.; Longmuir, K.J. Phosphorylation, transbilayer movement, and facilitated intracellular transport of diacylglycerol are involved in the uptake of a fluorescent analog of phosphatidic acid by cultured fibroblasts. *J. Biol. Chem.* **1985**, *260*, 1909–1916. [CrossRef] [PubMed]

435. Roberts, R.Z.; Morris, A.J. Role of phosphatidic acid phosphatase 2a in uptake of extracellular lipid phosphate mediators. *Biochim. Biophys. Acta* **2000**, *1487*, 33–49. [CrossRef] [PubMed]

436. Renault, A.D.; Sigal, Y.J.; Morris, A.J.; Lehmann, R. Soma-germ line competition for lipid phosphate uptake regulates germ cell migration and survival. *Science* **2004**, *305*, 1963–1966. [CrossRef] [PubMed]

437. Kim, S.A.; Vacratsis, P.O.; Firestein, R.; Cleary, M.L.; Dixon, J.E. Regulation of myotubularin-related (MTMR)2 phosphatidylinositol phosphatase by MTMR5, a catalytically inactive phosphatase. *Proc. Natl. Acad. Sci. USA* **2003**, *100*, 4492–4497. [CrossRef] [PubMed]
438. Rohde, H.M.; Tronchère, H.; Payrastre, B.; Laporte, J. Detection of myotubularin phosphatases activity on phosphoinositides in vitro and ex vivo. *Methods Mol. Biol.* **2009**, *462*, 265–278. [CrossRef] [PubMed]

439. Goldberg, T.; Sreelatha, A. Emerging functions of pseudoenzymes. *Biochem. J.* **2023**, *480*, 715–728. [CrossRef] [PubMed]

440. Bitar, L.; Uphaus, T.; Thalman, C.; Muthuraman, M.; Gyr, L.; Ji, H.; Domingues, M.; Endle, H.; Groppa, S.; Steffen, F.; et al. Inhibition of the enzyme autotaxin reduces cortical excitability and ameliorates the outcome in stroke. *Sci. Transl. Med.* **2022**, *14*, eabk0135. [CrossRef] [PubMed]

441. Unichenko, P.; Kirischuk, S.; Yang, J.W.; Baumgart, J.; Roskoden, T.; Schneider, P.; Sommer, A.; Horta, G.; Radyushkin, K.; Nitsch, R.; et al. Plasticity-Related Gene 1 Affects Mouse Barrel Cortex Function via Strengthening of Glutamatergic Thalamocortical Transmission. *Cereb. Cortex* **2016**, *26*, 3260–3272. [CrossRef]

442. Schneider, P.; Petzold, S.; Sommer, A.; Nitsch, R.; Schwegler, H.; Vogt, J.; Roskoden, T. Altered synaptic phospholipid signaling in PRG-1 deficient mice induces exploratory behavior and motor hyperactivity resembling psychiatric disorders. *Behav. Brain Res.* **2018**, *336*, 1–7. [CrossRef]

443. Thalman, C.; Horta, G.; Qiao, L.; Endle, H.; Tegeder, I.; Cheng, H.; Laube, G.; Sigurdsson, T.; Hauser, M.J.; Tenzer, S.; et al. Synaptic phospholipids as a new target for cortical hyperexcitability and E/I balance in psychiatric disorders. *Mol. Psychiatry* **2018**, *23*, 1699–1710. [CrossRef] [PubMed]

444. Tüscher, O.; Muthuraman, M.; Horstmann, J.P.; Horta, G.; Radyushkin, K.; Baumgart, J.; Sigurdsson, T.; Endle, H.; Ji, H.; Kuhnhäuser, P.; et al. Altered cortical synaptic lipid signaling leads to intermediate phenotypes of mental disorders. *Mol. Psychiatry* **2024**. [CrossRef] [PubMed]

445. Fischer, C.; Endle, H.; Schumann, L.; Wilken-Schmitz, A.; Kaiser, J.; Gerber, S.; Vogelaar, C.F.; Schmidt, M.H.H.; Nitsch, R.; Snodgrass, I.; et al. Prevention of age-associated neuronal hyperexcitability with improved learning and attention upon knockout or antagonism of LPAR2. *Cell. Mol. Life Sci.* **2021**, *78*, 1029–1050. [CrossRef] [PubMed]

446. Endle, H.; Horta, G.; Stutz, B.; Muthuraman, M.; Tegeder, I.; Schreiber, Y.; Snodgrass, I.F.; Gurke, R.; Liu, Z.W.; Sestan-Pesa, M.; et al. AgRP neurons control feeding behaviour at cortical synapses via peripherally derived lysophospholipids. *Nat. Metab.* **2022**, *4*, 683–692. [CrossRef] [PubMed]

447. Knierim, E.; Vogt, J.; Kintscher, M.; Ponomarenko, A.; Baumgart, J.; Beed, P.; Korotkova, T.; Trimbuch, T.; Panzer, A.; Steinlein, O.K.; et al. Mutations in plasticity-related-gene-1 (PRG-1) protein contribute to hippocampal seizure susceptibility and modify epileptic phenotype. *Cereb. Cortex* **2023**, *33*, 7454–7467. [CrossRef] [PubMed]

448. Zang, D.; Zhang, C.; Li, C.; Fan, Y.; Li, Z.; Hou, K.; Che, X.; Liu, Y.; Qu, X. LPPR4 promotes peritoneal metastasis via Sp1/integrin α/FAK signaling in gastric cancer. *Am. J. Cancer Res.* **2020**, *10*, 1026–1044. [PubMed]

449. Gaaya, A.; Poirier, O.; Mougenot, N.; Hery, T.; Atassi, F.; Marchand, A.; Saulnier-Blache, J.S.; Amour, J.; Vogt, J.; Lompré, A.M.; et al. Plasticity-related gene-1 inhibits lysophosphatidic acid-induced vascular smooth muscle cell migration and proliferation and prevents neointima formation. *Am. J. Physiol. Cell Physiol.* **2012**, *303*, C1104–C1114. [CrossRef] [PubMed]

450. García-Morales, V.; Montero, F.; González-Forero, D.; Rodríguez-Bey, G.; Gómez-Pérez, L.; Medialdea-Wandossell, M.J.; Domínguez-Vías, G.; García-Verdugo, J.M.; Moreno-López, B. Membrane-derived phospholipids control synaptic neurotransmission and plasticity. *PLoS Biol.* **2015**, *13*, e1002153. [CrossRef] [PubMed]

451. Roza, C.; Campos-Sandoval, J.A.; Gómez-García, M.C.; Peñalver, A.; Márquez, J. Lysophosphatidic Acid and Glutamatergic Transmission. *Front. Mol. Neurosci.* **2019**, *12*, 138. [CrossRef]

452. Croset, M.; Brossard, N.; Polette, A.; Lagarde, M. Characterization of plasma unsaturated lysophosphatidylcholines in human and rat. *Biochem. J.* **2000**, *345* Pt 1, 61–67. [CrossRef]

453. Ojala, P.J.; Hirvonen, T.E.; Hermansson, M.; Somerharju, P.; Parkkinen, J. Acyl chain-dependent effect of lysophosphatidylcholine on human neutrophils. *J. Leukoc. Biol.* **2007**, *82*, 1501–1509. [CrossRef] [PubMed]

454. Paapstel, K.; Kals, J.; Eha, J.; Tootsi, K.; Ottas, A.; Piir, A.; Jakobson, M.; Lieberg, J.; Zilmer, M. Inverse relations of serum phosphatidylcholines and lysophosphatidylcholines with vascular damage and heart rate in patients with atherosclerosis. *Nutr. Metab. Cardiovasc. Dis.* **2018**, *28*, 44–52. [CrossRef] [PubMed]

455. Kurano, M.; Kano, K.; Hara, M.; Tsukamoto, K.; Aoki, J.; Yatomi, Y. Regulation of plasma glycero-lysophospholipid levels by lipoprotein metabolism. *Biochem. J.* **2019**, *476*, 3565–3581. [CrossRef] [PubMed]

456. Sekas, G.; Patton, G.M.; Lincoln, E.C.; Robins, S.J. Origin of plasma lysophosphatidylcholine: Evidence for direct hepatic secretion in the rat. *J. Lab. Clin. Med.* **1985**, *105*, 190–194. [PubMed]

457. Brindley, D.N. Hepatic secretion of lysophosphatidylcholine: A novel transport system for polyunsaturated fatty acids and choline. *J. Nutr. Biochem.* **1993**, *4*, 442–449. [CrossRef]

458. Sugasini, D.; Yang, P.; Ng, D.; Khetarpal, S.A.; Vitali, C.; Rader, D.J.; Subbaiah, P.V. Potential role of hepatic lipase in the accretion of docosahexaenoic acid (DHA) by the brain. *Biochim. Biophys. Acta Mol. Cell Biol. Lipids* **2021**, *1866*, 159002. [CrossRef] [PubMed]

459. Thukkani, A.K.; McHowat, J.; Hsu, F.F.; Brennan, M.L.; Hazen, S.L.; Ford, D.A. Identification of alpha-chloro fatty aldehydes and unsaturated lysophosphatidylcholine molecular species in human atherosclerotic lesions. *Circulation* **2003**, *108*, 3128–3133. [CrossRef] [PubMed]

460. Kurano, M.; Sumitani, M.; Akiyama, Y.; Yamada, M.; Fujimura, D.; Yamaki, S.; Kano, K.; Aoki, J.; Hayakawa, K.; Takahashi, T.; et al. Usefulness of lysophosphatidylcholine measurement in the cerebrospinal fluid for differential diagnosis of neuropathic pain: Possible introduction into clinical laboratory testing. *Clin. Chim. Acta* **2023**, *541*, 117249. [CrossRef] [PubMed]
461. Thiés, F.; Delachambre, M.C.; Bentejac, M.; Lagarde, M.; Lecerf, J. Unsaturated fatty acids esterified in 2-acyl-l-lysophosphatidylcholine bound to albumin are more efficiently taken up by the young rat brain than the unesterified form. *J. Neurochem.* **1992**, *59*, 1110–1116. [CrossRef]

462. Nguyen, L.N.; Ma, D.; Shui, G.; Wong, P.; Cazenave-Gassiot, A.; Zhang, X.; Wenk, M.R.; Goh, E.L.; Silver, D.L. Mfsd2a is a transporter for the essential omega-3 fatty acid docosahexaenoic acid. *Nature* **2014**, *509*, 503–506. [CrossRef]

463. Cater, R.J.; Chua, G.L.; Erramilli, S.K.; Keener, J.E.; Choy, B.C.; Tokarz, P.; Chin, C.F.; Quek, D.Q.Y.; Kloss, B.; Pepe, J.G.; et al. Structural basis of omega-3 fatty acid transport across the blood-brain barrier. *Nature* **2021**, *595*, 315–319. [CrossRef] [PubMed]

464. Wood, C.A.P.; Zhang, J.; Aydin, D.; Xu, Y.; Andreone, B.J.; Langen, U.H.; Dror, R.O.; Gu, C.; Feng, L. Structure and mechanism of blood-brain-barrier lipid transporter MFSD2A. *Nature* **2021**, *596*, 444–448. [CrossRef] [PubMed]

465. Kurano, M.; Sakai, E.; Yatomi, Y. Understanding modulations of lipid mediators in cancer using a murine model of carcinomatous peritonitis. *Cancer Med.* **2022**, *11*, 3491–3507. [CrossRef] [PubMed]

466. Yasuda, D.; Hamano, F.; Masuda, K.; Dahlström, M.; Kobayashi, D.; Sato, N.; Hamakubo, T.; Shimizu, T.; Ishii, S. Inverse agonism of lysophospholipids with cationic head groups at Gi-coupled receptor GPR82. *Eur. J. Pharmacol.* **2023**, *954*, 175893. [CrossRef] [PubMed]

467. Xu, P.; Huang, S.; Guo, S.; Yun, Y.; Cheng, X.; He, X.; Cai, P.; Lan, Y.; Zhou, H.; Jiang, H.; et al. Structural identification of lysophosphatidylcholines as activating ligands for orphan receptor GPR119. *Nat. Struct. Mol. Biol.* **2022**, *29*, 863–870. [CrossRef] [PubMed]

468. Soga, T.; Ohishi, T.; Matsui, T.; Saito, T.; Matsumoto, M.; Takasaki, J.; Matsumoto, S.; Kamohara, M.; Hiyama, H.; Yoshida, S.; et al. Lysophosphatidylcholine enhances glucose-dependent insulin secretion via an orphan G-protein-coupled receptor. *Biochem. Biophys. Res. Commun.* **2005**, *326*, 744–751. [CrossRef] [PubMed]

469. Drzazga, A.; Kristinsson, H.; Sałaga, M.; Zatorski, H.; Koziółkiewicz, M.; Gendaszewska-Darmach, E.; Bergsten, P. Lysophosphatidylcholine and its phosphorothioate analogues potentiate insulin secretion via GPR40 (FFAR1), GPR55 and GPR119 receptors in a different manner. *Mol. Cell. Endocrinol.* **2018**, *472*, 117–125. [CrossRef] [PubMed]

470. Szustak, M.; Korkus, E.; Madaj, R.; Chworos, A.; Dąbrowski, G.; Czaplicki, S.; Tabandeh, E.; Maciejewska, G.; Koziółkiewicz, M.; Konopka, I.; et al. Lysophosphatidylcholines Enriched with cis and trans Palmitoleic Acid Regulate Insulin Secretion via GPR119 Receptor. *ACS Med. Chem. Lett.* **2024**, *15*, 197–204. [CrossRef] [PubMed]

471. Qian, Y.; Wang, J.; Yang, L.; Liu, Y.; Wang, L.; Liu, W.; Lin, Y.; Yang, H.; Ma, L.; Ye, S.; et al. Activation and signaling mechanism revealed by GPR119-Gs complex structures. *Nat. Commun.* **2022**, *13*, 7033. [CrossRef]

472. Kabarowski, J.H. G2A and LPC: Regulatory functions in immunity. *Prostaglandins Other Lipid Mediat.* **2009**, *89*, 73–81. [CrossRef]

473. Sisignano, M.; Fischer, M.J.M.; Geisslinger, G. Proton-Sensing GPCRs in Health and Disease. *Cells* **2021**, *10*, 2050. [CrossRef] [PubMed]

474. Chen, P.; Zuo, H.; Xiong, H.; Kolar, M.J.; Chu, Q.; Saghatelian, A.; Siegwart, D.J.; Wan, Y. Gpr132 sensing of lactate mediates tumor-macrophage interplay to promote breast cancer metastasis. *Proc. Natl. Acad. Sci. USA* **2017**, *114*, 580–585. [CrossRef] [PubMed]

475. Ngai, D.; Schilperoort, M.; Tabas, I. Efferocytosis-induced lactate enables the proliferation of pro-resolving macrophages to mediate tissue repair. *Nat. Metab.* **2023**, *5*, 2206–2219. [CrossRef] [PubMed]

476. Qiao, J.; Huang, F.; Naikawadi, R.P.; Kim, K.S.; Said, T.; Lum, H. Lysophosphatidylcholine impairs endothelial barrier function through the G protein-coupled receptor GPR4. *Am. J. Physiol. Lung Cell Mol. Physiol.* **2006**, *291*, L91–L101. [CrossRef] [PubMed]

477. Murakami, N.; Yokomizo, T.; Okuno, T.; Shimizu, T. G2A is a proton-sensing G-protein-coupled receptor antagonized by lysophosphatidylcholine. *J. Biol. Chem.* **2004**, *279*, 42484–42491. [CrossRef] [PubMed]

478. Radu, C.G.; Yang, L.V.; Riedinger, M.; Au, M.; Witte, O.N. T cell chemotaxis to lysophosphatidylcholine through the G2A receptor. *Proc. Natl. Acad. Sci. USA* **2004**, *101*, 245–250. [CrossRef]

479. Yang, L.V.; Radu, C.G.; Wang, L.; Riedinger, M.; Witte, O.N. Gi-independent macrophage chemotaxis to lysophosphatidylcholine via the immunoregulatory GPCR G2A. *Blood* **2005**, *105*, 1127–1134. [CrossRef] [PubMed]

480. Frasch, S.C.; Zemski-Berry, K.; Murphy, R.C.; Borregaard, N.; Henson, P.M.; Bratton, D.L. Lysophospholipids of different classes mobilize neutrophil secretory vesicles and induce redundant signaling through G2A. *J. Immunol.* **2007**, *178*, 6540–6548. [CrossRef] [PubMed]

481. Zhang, Q.; Zhang, W.; Liu, J.; Yang, H.; Hu, Y.; Zhang, M.; Bai, T.; Chang, F. Lysophosphatidylcholine promotes intercellular adhesion molecule-1 and vascular cell adhesion molecule-1 expression in human umbilical vein endothelial cells via an orphan G protein receptor 2-mediated signaling pathway. *Bioengineered* **2021**, *12*, 4520–4535. [CrossRef]

482. Le, L.Q.; Kabarowski, J.H.; Weng, Z.; Satterthwaite, A.B.; Harvill, E.T.; Jensen, E.R.; Miller, J.F.; Witte, O.N. Mice lacking the orphan G protein-coupled receptor G2A develop a late-onset autoimmune syndrome. *Immunity* **2001**, *14*, 561–571. [CrossRef]

483. Bolick, D.T.; Skaflen, M.D.; Johnson, L.E.; Kwon, S.C.; Howatt, D.; Daugherty, A.; Ravichandran, K.S.; Hedrick, C.C. G2A deficiency in mice promotes macrophage activation and atherosclerosis. *Circ. Res.* **2009**, *104*, 318–327. [CrossRef] [PubMed]

484. Yan, J.J.; Jung, J.S.; Lee, J.E.; Lee, J.; Huh, S.O.; Kim, H.S.; Jung, K.C.; Cho, J.Y.; Nam, J.S.; Suh, H.W.; et al. Therapeutic effects of lysophosphatidylcholine in experimental sepsis. *Nat. Med.* **2004**, *10*, 161–167. [CrossRef] [PubMed]

485. Li, H.M.; Jang, J.H.; Jung, J.S.; Shin, J.; Park, C.O.; Kim, Y.J.; Ahn, W.G.; Nam, J.S.; Hong, C.W.; Lee, J.; et al. G2A Protects Mice against Sepsis by Modulating Kupffer Cell Activation: Cooperativity with Adenosine Receptor 2b. *J. Immunol.* **2019**, *202*, 527–538. [CrossRef] [PubMed]
486. Wang, L.; Radu, C.G.; Yang, L.V.; Bentolila, L.A.; Riedinger, M.; Witte, O.N. Lysophosphatidylcholine-induced surface redissociation regulates signaling of the murine G protein-coupled receptor G2A. *Mol. Biol. Cell* **2005**, *16*, 2234–2247. [CrossRef] [PubMed]

487. Obinata, H.; Hattori, T.; Nakane, S.; Tatei, K.; Izumi, T. Identification of 9-hydroxyoctadecadienoic acid and other oxidized free fatty acids as ligands of the G protein-coupled receptor G2A. *J. Biol. Chem.* **2005**, *280*, 40676–40683. [CrossRef] [PubMed]

488. Foster, J.R.; Ueno, S.; Chen, M.X.; Harvey, J.; Dowell, S.J.; Irving, A.J.; Brown, A.J. N-Palmitoylglycine and other N-acylamides activate the lipid receptor G2A/GPR132. *Pharmacol. Res. Perspect.* **2019**, *7*, e00542. [CrossRef] [PubMed]

489. Cohen, L.J.; Kang, H.S.; Chu, J.; Huang, Y.H.; Gordon, E.A.; Reddy, B.V.; Ternei, M.A.; Craig, J.W.; Brady, S.F. Functional metagenomic discovery of bacterial effectors in the human microbiome and isolation of commendamide, a GPCR G2A/132 agonist. *Proc. Natl. Acad. Sci. USA* **2015**, *112*, E4825–E4834. [CrossRef] [PubMed]

490. Lahvic, J.L.; Ammerman, M.; Li, P.; Blair, M.C.; Stillman, E.R.; Fast, E.M.; Robertson, A.L.; Christodoulou, C.; Perlin, J.R.; Yang, S.; et al. Specific oxylipins enhance vertebrate hematopoiesis via the receptor GPR132. *Proc. Natl. Acad. Sci. USA* **2018**, *115*, 9252–9257. [CrossRef] [PubMed]

491. Wang, J.L.; Dou, X.D.; Cheng, J.; Gao, M.X.; Xu, G.F.; Ding, W.; Ding, J.H.; Li, Y.; Wang, S.H.; Ji, Z.W.; et al. Functional screening and rational design of compounds targeting GPR132 to treat diabetes. *Nat. Metab.* **2023**, *5*, 1726–1746. [CrossRef]

492. Carneiro, A.B.; Iaciura, B.M.; Nohara, L.L.; Lopes, C.D.; Veas, E.M.; Mariano, V.S.; Bozza, P.T.; Lopes, U.G.; Atella, G.C.; Almeida, I.C.; et al. Lysophosphatidylcholine triggers TLR2- and TLR4-mediated signaling pathways but counteracts LPS-induced NO synthesis in peritoneal macrophages by inhibiting NF-κB translocation and MAPK/ERK phosphorylation. *PLoS ONE* **2013**, *8*, e76233. [CrossRef]

493. The Human Protein Atlas. Available online: https://www.proteinatlas.org/ENSG00000164303-ENPP6 (accessed on 9 April 2024).

494. Xiao, L.; Ohayon, D.; McKenzie, I.A.; Sinclair-Wilson, A.; Wright, J.L.; Fudge, A.D.; Emery, B.; Li, H.; Richardson, W.D. Rapid production of new oligodendrocytes is required in the earliest stages of motor-skill learning. *Nat. Neurosci.* **2016**, *19*, 1210–1217. [CrossRef]

495. DeMichele-Sweet, M.A.A.; Klei, L.; Creese, B.; Harwood, J.C.; Weamer, E.A.; McClain, L.; Sims, R.; Hernandez, I.; Moreno-Grau, S.; Tárraga, L.; et al. Genome-wide association identifies the first risk loci for psychosis in Alzheimer disease. *Mol. Psychiatry* **2021**, *26*, 5797–5811. [CrossRef] [PubMed]

496. Tandon, R.; Levey, A.I.; Lah, J.J.; Seyfried, N.T.; Mitchell, C.S. Machine Learning Selection of Most Predictive Brain Proteins Suggests Role of Sugar Metabolism in Alzheimer’s Disease. *J. Alzheimers Dis.* **2023**, *92*, 411–424. [CrossRef]

497. Stewart, A.J.; Leong, D.T.K.; Farquharson, C. PLA2 and ENPP6 may act in concert to generate phosphocholine from the matrix vesicle membrane during skeletal mineralization. *FASEB J.* **2018**, *32*, 20–25. [CrossRef] [PubMed]

498. Dillon, S.; Suchacki, K.; Hsu, S.N.; Stephen, L.A.; Wang, R.; Cawthorn, W.P.; Stewart, A.J.; Nudelman, F.; Morton, N.M.; Farquharson, C. Ablation of Enpp6 Results in Transient Bone Hypomineralization. *JBMR Plus* **2021**, *5*, e10439. [CrossRef]

499. Chen, Y.; Zhang, P.; Xu, S.C.; Yang, L.; Voss, U.; Ekblad, E.; Wu, Y.; Min, Y.; Hertervig, E.; Nilsson, Å.; et al. Enhanced colonic tumorigenesis in alkaline sphingomyelinase (NPP7) knockout mice. *Mol. Cancer Ther.* **2015**, *14*, 259–267. [CrossRef]

500. Zhang, Y.; Cheng, Y.; Hansen, G.H.; Niels-Christiansen, L.L.; Koentgen, F.; Ohlsson, L.; Nilsson, A.; Duan, R.D. Crucial role of alkaline sphingomyelinase in sphingomyelin digestion: A study on enzyme knockout mice. *J. Lipid Res.* **2011**, *52*, 771–781. [CrossRef]

501. Tian, Y.; Li, X.; Wang, X.; Pei, S.T.; Pan, H.X.; Cheng, Y.Q.; Li, Y.C.; Cao, W.T.; Petersen, J.D.; Zhang, P. Alkaline sphingomyelinase deficiency impairs intestinal mucosal barrier integrity and reduces antioxidant capacity in dextran sulfate sodium-induced colitis. *World J. Gastroenterol.* **2024**, *30*, 1405–1419. [CrossRef] [PubMed]

502. Andersson, D.; Kotarsky, K.; Wu, J.; Agace, W.; Duan, R.D. Expression of alkaline sphingomyelinase in yeast cells and anti-inflammatory effects of the expressed enzyme in a rat colitis model. *Dig. Dis. Sci.* **2009**, *54*, 1440–1448. [CrossRef]

503. Duan, R.D. Alkaline sphingomyelinase (NPP7) in hepatobiliary diseases: A field that needs to be closely studied. *World J. Hepatol.* **2018**, *10*, 246–253. [CrossRef]

504. Zhu, J.; Wang, L.; Guo, Z.; Zhang, T.; Zhang, P. Transcriptome analysis of intestine from alk-SMase knockout mice reveals the effect of alk-SMase. *Cancer Cell Int.* **2022**, *22*, 344. [CrossRef] [PubMed]

505. Zhu, J.; Wang, L.; Li, X.; Lan, D.; Song, L.; Li, Y.; Cheng, Y.; Zhang, P. Transcriptome analysis alk-SMase knockout mice reveals the effect of alkaline sphingomyelinase on liver. *Biochem. Biophys. Rep.* **2022**, *30*, 101240. [CrossRef] [PubMed]

506. Alyamani, M.; Kadivar, M.; Erjefält, J.; Johansson-Lindbom, B.; Duan, R.D.; Nilsson, Å.; Marsal, J. Alkaline sphingomyelinase (NPP7) impacts the homeostasis of intestinal T lymphocyte populations. *Front. Immunol.* **2022**, *13*, 1050625. [CrossRef] [PubMed]

507. Slieker, R.C.; Donnelly, L.A.; Akalestou, E.; Lopez-Noriega, L.; Melhem, R.; Güneş, A.; Abou Azar, F.; Efanov, A.; Georgiadou, E.; Muniangi-Muhitu, H.; et al. Identification of biomarkers for glycaemic deterioration in type 2 diabetes. *Nat. Commun.* **2023**, *14*, 2533. [CrossRef] [PubMed]

508. Zhu, L.; Ma, M.; Zhang, L.; Wang, S.; Guo, Y.; Ling, X.; Lin, H.; Lai, N.; Lin, S.; Du, L.; et al. System Analysis Based on Lipid-Metabolism-Related Genes Identifies AGT as a Novel Therapy Target for Gastric Cancer with Neoadjuvant Chemotherapy. *Pharmaceutics* **2023**, *15*, 810. [CrossRef] [PubMed]

509. Takagi, Y.; Nishikado, S.; Omi, J.; Aoki, J. The Many Roles of Lysophospholipid Mediators and Japanese Contributions to This Field. *Biol. Pharm. Bull.* **2022**, *45*, 1008–1021. [CrossRef] [PubMed]
510. Bottemanne, P.; Paquot, A.; Ameraoui, H.; Alhouayek, M.; Muccioli, G.G. The α/β-hydrolase domain 6 inhibitor WWL70 decreases endotoxin-induced lung inflammation in mice, potential contribution of 2-arachidonoylglycerol, and lysoglycerophospholipids. *FASEB J.* **2019**, *33*, 7635–7646. [CrossRef] [PubMed]

511. Yue, Q.; Li, K.; Song, Z.; Wang, Q.; Wang, J.; Li, X.; Li, Y.; Zhang, Q.; Zhu, Y.; Chen, H. Nitric oxide hinders club cell proliferation through Gdpd2 during allergic airway inflammation. *FEBS Open Bio* **2023**, *13*, 1041–1055. [CrossRef] [PubMed]

512. Cronin, A.; Mowbray, S.; Dürk, H.; Homburg, S.; Fleming, I.; Fisslthaler, B.; Oesch, F.; Arand, M. The N-terminal domain of mammalian soluble epoxide hydrolase is a phosphatase. *Proc. Natl. Acad. Sci. USA* **2003**, *100*, 1552–1557. [CrossRef]

513. Newman, J.W.; Morisseau, C.; Harris, T.R.; Hammock, B.D. The soluble epoxide hydrolase encoded by EPXH2 is a bifunctional enzyme with novel lipid phosphate phosphatase activity. *Proc. Natl. Acad. Sci. USA* **2003**, *100*, 1558–1563. [CrossRef]

514. Oguro, A.; Imaoka, S. Lysophosphatidic acids are new substrates for the phosphatase domain of soluble epoxide hydrolase. *J. Lipid Res.* **2012**, *53*, 505–512. [CrossRef] [PubMed]

515. Oguro, A.; Kaga, Y.; Sato, H.; Fujiyama, T.; Fujimoto, S.; Nagai, S.; Matsuyama, M.; Miyara, M.; Ishihara, Y.; Yamazaki, T.; et al. Mice deficient in the phosphatase activity of sEH show decreased levels of the endocannabinoid 2-AG in the olfactory bulb and depressive-like behavior. *FEBS Lett* **2024**. [CrossRef] [PubMed]

516. Leuillier, M.; Duflot, T.; Ménoret, S.; Messaoudi, H.; Djerada, Z.; Groussard, D.; Denis, R.G.P.; Chevalier, L.; Karoui, A.; Panthu, B.; et al. CRISPR/Cas9-mediated inactivation of the phosphatase activity of soluble epoxide hydrolase prevents obesity and cardiac ischemic injury. *J. Adv. Res.* **2023**, *43*, 163–174. [CrossRef] [PubMed]

517. Su, W.M.; Gu, X.J.; Dou, M.; Duan, Q.Q.; Jiang, Z.; Yin, K.F.; Cai, W.C.; Cao, B.; Wang, Y.; Chen, Y.P. Systematic druggable genome-wide Mendelian randomisation identifies therapeutic targets for Alzheimer's disease. *J. Neurol. Neurosurg. Psychiatry* **2023**, *94*, 954–961. [CrossRef] [PubMed]

**Disclaimer/Publisher's Note:** The statements, opinions and data contained in all publications are solely those of the individual author(s) and contributor(s) and not of MDPI and/or the editor(s). MDPI and/or the editor(s) disclaim responsibility for any injury to people or property resulting from any ideas, methods, instructions or products referred to in the content.