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Volumn 1851, Issue 5, 2015, Pages 537-548

Glycerophosphodiesterase GDE4 as a novel lysophospholipase D: A possible involvement in bioactive N-acylethanolamine biosynthesis

Author keywords

Endocannabinoid; Glycerophosphodiesterase; Lysophosphatidic acid; Lysophospholipase D; N Acylethanolamine; Phospholipid

Indexed keywords

CARBON 14; ETHANOLAMINE; GLYCEROPHOSPHODIESTERASE 4; LYSOPHOSPHATIDIC ACID; LYSOPHOSPHATIDYLCHOLINE; LYSOPHOSPHATIDYLETHANOLAMINE; LYSOPHOSPHOLIPASE; LYSOPHOSPHOLIPID; MESSENGER RNA; N ACYLETHANOLAMINE; PALMIDROL; PHOSPHOLIPASE D; UNCLASSIFIED DRUG; ALKYLGLYCEROPHOSPHOETHANOLAMINE PHOSPHODIESTERASE; ETHANOLAMINE DERIVATIVE; GDE4 PROTEIN, MOUSE; GLYCEROPHOSPHODIESTER PHOSPHODIESTERASE; N-ACYLETHANOLAMINES; PHOSPHODIESTERASE;

EID: 84922569247     PISSN: 13881981     EISSN: 18792618     Source Type: Journal    
DOI: 10.1016/j.bbalip.2015.01.002     Document Type: Article
Times cited : (46)

References (52)
  • 1
  • 2
    • 0033661848 scopus 로고    scopus 로고
    • N-Acylethanolamines and precursor phospholipids-relation to cell injury
    • H.S. Hansen, B. Moesgaard, H.H. Hansen, and G. Petersen N-Acylethanolamines and precursor phospholipids-relation to cell injury Chem. Phys. Lipids 108 2000 135 150
    • (2000) Chem. Phys. Lipids , vol.108 , pp. 135-150
    • Hansen, H.S.1    Moesgaard, B.2    Hansen, H.H.3    Petersen, G.4
  • 5
    • 11244328917 scopus 로고    scopus 로고
    • The nuclear receptor peroxisome proliferator-activated receptor-α mediates the anti-inflammatory actions of palmitoylethanolamide
    • J. Lo Verme, J. Fu, G. Astarita, G. La Rana, R. Russo, A. Calignano, and D. Piomelli The nuclear receptor peroxisome proliferator-activated receptor-α mediates the anti-inflammatory actions of palmitoylethanolamide Mol. Pharmacol. 67 2005 15 19
    • (2005) Mol. Pharmacol. , vol.67 , pp. 15-19
    • Lo Verme, J.1    Fu, J.2    Astarita, G.3    La Rana, G.4    Russo, R.5    Calignano, A.6    Piomelli, D.7
  • 6
    • 84908619757 scopus 로고    scopus 로고
    • Harnessing the anti-inflammatory potential of palmitoylethanolamide
    • M. Alhouayek, and G.G. Muccioli Harnessing the anti-inflammatory potential of palmitoylethanolamide Drug Discov. Today 19 2014 1632 1639
    • (2014) Drug Discov. Today , vol.19 , pp. 1632-1639
    • Alhouayek, M.1    Muccioli, G.G.2
  • 9
    • 0042734414 scopus 로고    scopus 로고
    • Activation of TRPV1 by the satiety factor oleoylethanolamide
    • G.P. Ahern Activation of TRPV1 by the satiety factor oleoylethanolamide J. Biol. Chem. 278 2003 30429 30434
    • (2003) J. Biol. Chem. , vol.278 , pp. 30429-30434
    • Ahern, G.P.1
  • 11
    • 84905264880 scopus 로고    scopus 로고
    • Role of anorectic N-acylethanolamines in intestinal physiology and satiety control with respect to dietary fat
    • H.S. Hansen Role of anorectic N-acylethanolamines in intestinal physiology and satiety control with respect to dietary fat Pharmacol. Res. 86 2014 18 25
    • (2014) Pharmacol. Res. , vol.86 , pp. 18-25
    • Hansen, H.S.1
  • 12
    • 0019308380 scopus 로고
    • Accumulation of N-acylethanolamine glycerophospholipids in infarcted myocardium
    • D.E. Epps, V. Natarajan, P.C. Schmid, and H.H.O. Schmid Accumulation of N-acylethanolamine glycerophospholipids in infarcted myocardium Biochim. Biophys. Acta 618 1980 420 430
    • (1980) Biochim. Biophys. Acta , vol.618 , pp. 420-430
    • Epps, D.E.1    Natarajan, V.2    Schmid, P.C.3    Schmid, H.H.O.4
  • 13
    • 77957944897 scopus 로고    scopus 로고
    • Enzymological studies on the biosynthesis of N-acylethanolamines
    • N. Ueda, K. Tsuboi, and T. Uyama Enzymological studies on the biosynthesis of N-acylethanolamines Biochim. Biophys. Acta 1801 2010 1274 1285
    • (2010) Biochim. Biophys. Acta , vol.1801 , pp. 1274-1285
    • Ueda, N.1    Tsuboi, K.2    Uyama, T.3
  • 14
    • 84876951107 scopus 로고    scopus 로고
    • Metabolism of endocannabinoids and related N-acylethanolamines: Canonical and alternative pathways
    • N. Ueda, K. Tsuboi, and T. Uyama Metabolism of endocannabinoids and related N-acylethanolamines: Canonical and alternative pathways FEBS J. 280 2013 1874 1894
    • (2013) FEBS J. , vol.280 , pp. 1874-1894
    • Ueda, N.1    Tsuboi, K.2    Uyama, T.3
  • 17
    • 0020535405 scopus 로고
    • The role of cardiolipin as an acyl donor in dog heart N-acylethanolamine phospholipid biosynthesis
    • P.V. Reddy, P.C. Schmid, V. Natarajan, and H.H.O. Schmid The role of cardiolipin as an acyl donor in dog heart N-acylethanolamine phospholipid biosynthesis Biochim. Biophys. Acta 751 1983 241 246
    • (1983) Biochim. Biophys. Acta , vol.751 , pp. 241-246
    • Reddy, P.V.1    Schmid, P.C.2    Natarajan, V.3    Schmid, H.H.O.4
  • 18
    • 0030066244 scopus 로고    scopus 로고
    • Enzymatic synthesis of anandamide, an endogenous cannabinoid receptor ligand, through N-acylphosphatidylethanolamine pathway in testis: Involvement of Ca2 +-dependent transacylase and phosphodiesterase activities
    • T. Sugiura, S. Kondo, A. Sukagawa, T. Tonegawa, S. Nakane, A. Yamashita, and K. Waku Enzymatic synthesis of anandamide, an endogenous cannabinoid receptor ligand, through N-acylphosphatidylethanolamine pathway in testis: involvement of Ca2 +-dependent transacylase and phosphodiesterase activities Biochem. Biophys. Res. Commun. 218 1996 113 117
    • (1996) Biochem. Biophys. Res. Commun. , vol.218 , pp. 113-117
    • Sugiura, T.1    Kondo, S.2    Sukagawa, A.3    Tonegawa, T.4    Nakane, S.5    Yamashita, A.6    Waku, K.7
  • 19
    • 33947532254 scopus 로고    scopus 로고
    • Discovery and characterization of a Ca2 +-independent phosphatidylethanolamine N-acyltransferase generating the anandamide precursor and its congeners
    • X.-H. Jin, Y. Okamoto, J. Morishita, K. Tsuboi, T. Tonai, and N. Ueda Discovery and characterization of a Ca2 +-independent phosphatidylethanolamine N-acyltransferase generating the anandamide precursor and its congeners J. Biol. Chem. 282 2007 3614 3623
    • (2007) J. Biol. Chem. , vol.282 , pp. 3614-3623
    • Jin, X.-H.1    Okamoto, Y.2    Morishita, J.3    Tsuboi, K.4    Tonai, T.5    Ueda, N.6
  • 21
    • 84863627966 scopus 로고    scopus 로고
    • Structural basis for the acyltransferase activity of lecithin:retinol acyltransferase-like proteins
    • M. Golczak, P.D. Kiser, A.E. Sears, D.T. Lodowski, W.S. Blaner, and K. Palczewski Structural basis for the acyltransferase activity of lecithin:retinol acyltransferase-like proteins J. Biol. Chem. 287 2012 23790 23807
    • (2012) J. Biol. Chem. , vol.287 , pp. 23790-23807
    • Golczak, M.1    Kiser, P.D.2    Sears, A.E.3    Lodowski, D.T.4    Blaner, W.S.5    Palczewski, K.6
  • 23
    • 1242294480 scopus 로고    scopus 로고
    • Molecular characterization of a phospholipase D generating anandamide and its congeners
    • Y. Okamoto, J. Morishita, K. Tsuboi, T. Tonai, and N. Ueda Molecular characterization of a phospholipase D generating anandamide and its congeners J. Biol. Chem. 279 2004 5298 5305
    • (2004) J. Biol. Chem. , vol.279 , pp. 5298-5305
    • Okamoto, Y.1    Morishita, J.2    Tsuboi, K.3    Tonai, T.4    Ueda, N.5
  • 24
    • 33645935391 scopus 로고    scopus 로고
    • Inactivation of N-acyl phosphatidylethanolamine phospholipase D reveals multiple mechanisms for the biosynthesis of endocannabinoids
    • D. Leung, A. Saghatelian, G.M. Simon, and B.F. Cravatt Inactivation of N-acyl phosphatidylethanolamine phospholipase D reveals multiple mechanisms for the biosynthesis of endocannabinoids Biochemistry 45 2006 4720 4726
    • (2006) Biochemistry , vol.45 , pp. 4720-4726
    • Leung, D.1    Saghatelian, A.2    Simon, G.M.3    Cravatt, B.F.4
  • 25
    • 79961107765 scopus 로고    scopus 로고
    • Enzymatic formation of N-acylethanolamines from N-acylethanolamine plasmalogen through N-acylphosphatidylethanolamine-hydrolyzing phospholipase D-dependent and -independent pathways
    • K. Tsuboi, Y. Okamoto, N. Ikematsu, M. Inoue, Y. Shimizu, T. Uyama, J. Wang, D.G. Deutsch, M.P. Burns, N.M. Ulloa, A. Tokumura, and N. Ueda Enzymatic formation of N-acylethanolamines from N-acylethanolamine plasmalogen through N-acylphosphatidylethanolamine-hydrolyzing phospholipase D-dependent and -independent pathways Biochim. Biophys. Acta 1811 2011 565 577
    • (2011) Biochim. Biophys. Acta , vol.1811 , pp. 565-577
    • Tsuboi, K.1    Okamoto, Y.2    Ikematsu, N.3    Inoue, M.4    Shimizu, Y.5    Uyama, T.6    Wang, J.7    Deutsch, D.G.8    Burns, M.P.9    Ulloa, N.M.10    Tokumura, A.11    Ueda, N.12
  • 27
    • 33748743637 scopus 로고    scopus 로고
    • Endocannabinoid biosynthesis proceeding through glycerophospho-N-acyl ethanolamine and a role for α/β-hydrolase 4 in this pathway
    • G.M. Simon, and B.F. Cravatt Endocannabinoid biosynthesis proceeding through glycerophospho-N-acyl ethanolamine and a role for α/β-hydrolase 4 in this pathway J. Biol. Chem. 281 2006 26465 26472
    • (2006) J. Biol. Chem. , vol.281 , pp. 26465-26472
    • Simon, G.M.1    Cravatt, B.F.2
  • 28
    • 44049087532 scopus 로고    scopus 로고
    • Anandamide biosynthesis catalyzed by the phosphodiesterase GDE1 and detection of glycerophospho-N-acyl ethanolamine precursors in mouse brain
    • G.M. Simon, and B.F. Cravatt Anandamide biosynthesis catalyzed by the phosphodiesterase GDE1 and detection of glycerophospho-N-acyl ethanolamine precursors in mouse brain J. Biol. Chem. 283 2008 9341 9349
    • (2008) J. Biol. Chem. , vol.283 , pp. 9341-9349
    • Simon, G.M.1    Cravatt, B.F.2
  • 29
    • 77954582423 scopus 로고    scopus 로고
    • Characterization of mice lacking candidate N-acyl ethanolamine biosynthetic enzymes provides evidence for multiple pathways that contribute to endocannabinoid production in vivo
    • G.M. Simon, and B.F. Cravatt Characterization of mice lacking candidate N-acyl ethanolamine biosynthetic enzymes provides evidence for multiple pathways that contribute to endocannabinoid production in vivo Mol. BioSyst. 6 2010 1411 1418
    • (2010) Mol. BioSyst. , vol.6 , pp. 1411-1418
    • Simon, G.M.1    Cravatt, B.F.2
  • 30
    • 3042737612 scopus 로고    scopus 로고
    • Biosynthesis of anandamide and N-palmitoylethanolamine by sequential actions of phospholipase A2 and lysophospholipase D
    • Y.-X. Sun, K. Tsuboi, Y. Okamoto, T. Tonai, M. Murakami, I. Kudo, and N. Ueda Biosynthesis of anandamide and N-palmitoylethanolamine by sequential actions of phospholipase A2 and lysophospholipase D Biochem. J. 380 2004 749 756
    • (2004) Biochem. J. , vol.380 , pp. 749-756
    • Sun, Y.-X.1    Tsuboi, K.2    Okamoto, Y.3    Tonai, T.4    Murakami, M.5    Kudo, I.6    Ueda, N.7
  • 31
    • 77956394894 scopus 로고    scopus 로고
    • LPA3, a unique G protein-coupled receptor for lysophosphatidic acid
    • K. Hama, and J. Aoki LPA3, a unique G protein-coupled receptor for lysophosphatidic acid Prog. Lipid Res. 49 2010 335 342
    • (2010) Prog. Lipid Res. , vol.49 , pp. 335-342
    • Hama, K.1    Aoki, J.2
  • 33
    • 0021099820 scopus 로고
    • Metabolism of N-acylethanolamine phospholipids by a mammalian phosphodiesterase of the phospholipase D type
    • P.C. Schmid, P.V. Reddy, V. Natarajan, and H.H.O. Schmid Metabolism of N-acylethanolamine phospholipids by a mammalian phosphodiesterase of the phospholipase D type J. Biol. Chem. 258 1983 9302 9306
    • (1983) J. Biol. Chem. , vol.258 , pp. 9302-9306
    • Schmid, P.C.1    Reddy, P.V.2    Natarajan, V.3    Schmid, H.H.O.4
  • 34
    • 0028038495 scopus 로고
    • Lysophosphatidic acids induce proliferation of cultured vascular smooth muscle cells from rat aorta
    • A. Tokumura, M. Iimori, Y. Nishioka, M. Kitahara, M. Sakashita, and S. Tanaka Lysophosphatidic acids induce proliferation of cultured vascular smooth muscle cells from rat aorta Am. J. Physiol. 267 1994 C204 C210
    • (1994) Am. J. Physiol. , vol.267 , pp. C204-C210
    • Tokumura, A.1    Iimori, M.2    Nishioka, Y.3    Kitahara, M.4    Sakashita, M.5    Tanaka, S.6
  • 35
    • 33845261493 scopus 로고
    • A rapid method of total lipid extraction and purification
    • E.G. Bligh, and W.J. Dyer A rapid method of total lipid extraction and purification Can. J. Biochem. Physiol. 37 1959 911 917
    • (1959) Can. J. Biochem. Physiol. , vol.37 , pp. 911-917
    • Bligh, E.G.1    Dyer, W.J.2
  • 36
    • 0016273430 scopus 로고
    • Purification and properties of a membrane-bound phospholipase A1 from Mycobacterium phlei
    • M. Nishijima, Y. Akamatsu, and S. Nojima Purification and properties of a membrane-bound phospholipase A1 from Mycobacterium phlei J. Biol. Chem. 249 1974 5658 5667
    • (1974) J. Biol. Chem. , vol.249 , pp. 5658-5667
    • Nishijima, M.1    Akamatsu, Y.2    Nojima, S.3
  • 37
    • 80054100966 scopus 로고    scopus 로고
    • Enzymological analysis of the tumor suppressor A-C1 reveals a novel group of phospholipid-metabolizing enzymes
    • N. Shinohara, T. Uyama, X.-H. Jin, K. Tsuboi, T. Tonai, H. Houchi, and N. Ueda Enzymological analysis of the tumor suppressor A-C1 reveals a novel group of phospholipid-metabolizing enzymes J. Lipid Res. 52 2011 1927 1935
    • (2011) J. Lipid Res. , vol.52 , pp. 1927-1935
    • Shinohara, N.1    Uyama, T.2    Jin, X.-H.3    Tsuboi, K.4    Tonai, T.5    Houchi, H.6    Ueda, N.7
  • 38
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M.M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 72 1976 248 254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 40
    • 4744354729 scopus 로고    scopus 로고
    • Cyclohexylcarbamic acid 3'- or 4'-substituted biphenyl-3-yl esters as fatty acid amide hydrolase inhibitors: Synthesis, quantitative structure-activity relationships, and molecular modeling studies
    • M. Mor, S. Rivara, A. Lodola, P.V. Plazzi, G. Tarzia, A. Duranti, A. Tontini, G. Piersanti, S. Kathuria, and D. Piomelli Cyclohexylcarbamic acid 3'- or 4'-substituted biphenyl-3-yl esters as fatty acid amide hydrolase inhibitors: synthesis, quantitative structure-activity relationships, and molecular modeling studies J. Med. Chem. 47 2004 4998 5008
    • (2004) J. Med. Chem. , vol.47 , pp. 4998-5008
    • Mor, M.1    Rivara, S.2    Lodola, A.3    Plazzi, P.V.4    Tarzia, G.5    Duranti, A.6    Tontini, A.7    Piersanti, G.8    Kathuria, S.9    Piomelli, D.10
  • 43
    • 26444525004 scopus 로고    scopus 로고
    • Involvement of N-acylethanolamine-hydrolyzing acid amidase in the degradation of anandamide and other N-acylethanolamines in macrophages
    • Y.-X. Sun, K. Tsuboi, L.-Y. Zhao, Y. Okamoto, D.M. Lambert, and N. Ueda Involvement of N-acylethanolamine-hydrolyzing acid amidase in the degradation of anandamide and other N-acylethanolamines in macrophages Biochim. Biophys. Acta 1736 2005 211 220
    • (2005) Biochim. Biophys. Acta , vol.1736 , pp. 211-220
    • Sun, Y.-X.1    Tsuboi, K.2    Zhao, L.-Y.3    Okamoto, Y.4    Lambert, D.M.5    Ueda, N.6
  • 45
    • 77954391618 scopus 로고    scopus 로고
    • Autotaxin-an LPA producing enzyme with diverse functions
    • K. Nakanaga, K. Hama, and J. Aoki Autotaxin-an LPA producing enzyme with diverse functions J. Biochem. 148 2010 13 24
    • (2010) J. Biochem. , vol.148 , pp. 13-24
    • Nakanaga, K.1    Hama, K.2    Aoki, J.3
  • 46
    • 0037452765 scopus 로고    scopus 로고
    • GDE1/MIR16 is a glycerophosphoinositol phosphodiesterase regulated by stimulation of G protein-coupled receptors
    • B. Zheng, C.P. Berrie, D. Corda, and M.G. Farquhar GDE1/MIR16 is a glycerophosphoinositol phosphodiesterase regulated by stimulation of G protein-coupled receptors Proc. Natl. Acad. Sci. U. S. A. 100 2003 1745 1750
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 1745-1750
    • Zheng, B.1    Berrie, C.P.2    Corda, D.3    Farquhar, M.G.4
  • 47
    • 77956043214 scopus 로고    scopus 로고
    • The glycerophospho metabolome and its influence on amino acid homeostasis revealed by brain metabolomics of GDE1(-/-) mice
    • F. Kopp, T. Komatsu, D.K. Nomura, S.A. Trauger, J.R. Thomas, G. Siuzdak, G.M. Simon, and B.F. Cravatt The glycerophospho metabolome and its influence on amino acid homeostasis revealed by brain metabolomics of GDE1(-/-) mice Chem. Biol. 17 2010 831 840
    • (2010) Chem. Biol. , vol.17 , pp. 831-840
    • Kopp, F.1    Komatsu, T.2    Nomura, D.K.3    Trauger, S.A.4    Thomas, J.R.5    Siuzdak, G.6    Simon, G.M.7    Cravatt, B.F.8
  • 49
    • 36148963665 scopus 로고    scopus 로고
    • Mammalian glycerophosphodiester phosphodiesterases
    • N. Yanaka Mammalian glycerophosphodiester phosphodiesterases Biosci. Biotechnol. Biochem. 71 2007 1811 1818
    • (2007) Biosci. Biotechnol. Biochem. , vol.71 , pp. 1811-1818
    • Yanaka, N.1
  • 50
    • 56849095532 scopus 로고    scopus 로고
    • Isolation, characterization and molecular 3D model of human GDE4, a novel membrane protein containing glycerophosphodiester phosphodiesterase domain
    • P.A. Chang, H.B. Shao, D.X. Long, Q. Sun, and Y.J. Wu Isolation, characterization and molecular 3D model of human GDE4, a novel membrane protein containing glycerophosphodiester phosphodiesterase domain Mol. Membr. Biol. 25 2008 557 566
    • (2008) Mol. Membr. Biol. , vol.25 , pp. 557-566
    • Chang, P.A.1    Shao, H.B.2    Long, D.X.3    Sun, Q.4    Wu, Y.J.5
  • 51
    • 84894252491 scopus 로고    scopus 로고
    • The emerging physiological roles of the glycerophosphodiesterase family
    • D. Corda, M.G. Mosca, N. Ohshima, L. Grauso, N. Yanaka, and S. Mariggiò The emerging physiological roles of the glycerophosphodiesterase family FEBS J. 281 2014 998 1016
    • (2014) FEBS J. , vol.281 , pp. 998-1016
    • Corda, D.1    Mosca, M.G.2    Ohshima, N.3    Grauso, L.4    Yanaka, N.5    Mariggiò, S.6
  • 52
    • 0034635962 scopus 로고    scopus 로고
    • MIR16, a putative membrane glycerophosphodiester phosphodiesterase, interacts with RGS16
    • B. Zheng, D. Chen, and M.G. Farquhar MIR16, a putative membrane glycerophosphodiester phosphodiesterase, interacts with RGS16 Proc. Natl. Acad. Sci. U. S. A. 97 2000 3999 4004
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 3999-4004
    • Zheng, B.1    Chen, D.2    Farquhar, M.G.3


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