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Volumn 48, Issue 10, 2007, Pages 2255-2263

The acylation of lipophilic alcohols by lysosomal phospholipase A 2

Author keywords

1 O hexadecyl 2 acetyl sn glycerol; Amiodarone; Anandamide; Ceramide; D threo 1 phenyl 2 decanoylamino 3 morpholino propanol; N acetylsphingosine

Indexed keywords

ACYLTRANSFERASE; ALCOHOL; CERAMIDE; PHOSPHATIDYLCHOLINE; PHOSPHATIDYLETHANOLAMINE; PHOSPHOLIPASE A2;

EID: 34948831118     PISSN: 00222275     EISSN: 15397262     Source Type: Journal    
DOI: 10.1194/jlr.M700277-JLR200     Document Type: Article
Times cited : (21)

References (29)
  • 1
    • 0029891058 scopus 로고    scopus 로고
    • A novel enzyme that catalyzes the esterification of N-acetylsphingosine. Metabolism of C2-ceramides
    • Abe, A., J. A. Shayman, and N. S. Radin. 1996. A novel enzyme that catalyzes the esterification of N-acetylsphingosine. Metabolism of C2-ceramides. J. Biol. Chem. 271: 14383-14389.
    • (1996) J. Biol. Chem , vol.271 , pp. 14383-14389
    • Abe, A.1    Shayman, J.A.2    Radin, N.S.3
  • 2
    • 0037155846 scopus 로고    scopus 로고
    • Cloning and characterization of a lysosomal phospholipase A2, 1-O-acylceramide synthase
    • Hiraoka, M., A. Abe, and J. A. Shayman. 2002. Cloning and characterization of a lysosomal phospholipase A2, 1-O-acylceramide synthase. J. Biol. Chem. 277: 10090-10099.
    • (2002) J. Biol. Chem , vol.277 , pp. 10090-10099
    • Hiraoka, M.1    Abe, A.2    Shayman, J.A.3
  • 3
    • 0032478741 scopus 로고    scopus 로고
    • Purification and characterization of 1-O-acylceramide synthase, a novel phospholipase A2 with transacylase activity
    • Abe, A., and J. A. Shayman. 1998. Purification and characterization of 1-O-acylceramide synthase, a novel phospholipase A2 with transacylase activity. J. Biol. Chem. 273: 8467-8474.
    • (1998) J. Biol. Chem , vol.273 , pp. 8467-8474
    • Abe, A.1    Shayman, J.A.2
  • 5
    • 27444444715 scopus 로고    scopus 로고
    • Structure and function of lysosomal phospholipase A2: Identification of the catalytic triad and the role of cysteine residues
    • Hiraoka, M., A. Abe, and J. A. Shayman. 2005. Structure and function of lysosomal phospholipase A2: identification of the catalytic triad and the role of cysteine residues. J. Lipid Res. 46: 2441-2447.
    • (2005) J. Lipid Res , vol.46 , pp. 2441-2447
    • Hiraoka, M.1    Abe, A.2    Shayman, J.A.3
  • 6
    • 33751028489 scopus 로고    scopus 로고
    • The phospholipase A2 superfamily and its group numbering system
    • Schaloske, R. H., and E. A. Dennis. 2006. The phospholipase A2 superfamily and its group numbering system. Biochim. Biophys. Acta. 1761: 1246-1259.
    • (2006) Biochim. Biophys. Acta , vol.1761 , pp. 1246-1259
    • Schaloske, R.H.1    Dennis, E.A.2
  • 7
    • 5644289431 scopus 로고    scopus 로고
    • Lysosomal phospholipase A2 is selectively expressed in alveolar macrophages
    • Abe, A., M. Hiraoka, S. Wild, S. E. Wilcoxen, R. Paine, 3rd, and J. A. Shayman. 2004. Lysosomal phospholipase A2 is selectively expressed in alveolar macrophages. J. Biol. Chem. 279: 42605-42611.
    • (2004) J. Biol. Chem , vol.279 , pp. 42605-42611
    • Abe, A.1    Hiraoka, M.2    Wild, S.3    Wilcoxen, S.E.4    Paine 3rd, R.5    Shayman, J.A.6
  • 9
    • 0028297068 scopus 로고
    • The sphingomyelin pathway in tumor necrosis factor and interleukin-1 signaling
    • Kolesnick, R., and D. W. Golde. 1994. The sphingomyelin pathway in tumor necrosis factor and interleukin-1 signaling. Cell. 77: 325-328.
    • (1994) Cell , vol.77 , pp. 325-328
    • Kolesnick, R.1    Golde, D.W.2
  • 10
    • 0033974782 scopus 로고    scopus 로고
    • Ceramide in the eukaryotic stress response
    • Hannun, Y. A., and C. Luberto. 2000. Ceramide in the eukaryotic stress response. Trends Cell Biol. 10: 73-80.
    • (2000) Trends Cell Biol , vol.10 , pp. 73-80
    • Hannun, Y.A.1    Luberto, C.2
  • 11
    • 34948906396 scopus 로고    scopus 로고
    • A role for lysosomal phospholipase A2 in drug induced phospholipidosis
    • Abe, A., M. Hiraoka, and J. A. Shayman. 2007. A role for lysosomal phospholipase A2 in drug induced phospholipidosis. Drug Metabolism Letters. 1: 49-53.
    • (2007) Drug Metabolism Letters , vol.1 , pp. 49-53
    • Abe, A.1    Hiraoka, M.2    Shayman, J.A.3
  • 12
    • 0032692477 scopus 로고    scopus 로고
    • Inhibitors of glucosylceramide synthase
    • Shayman, J. A., L. Lee, A. Abe, and L. Shu. 2000. Inhibitors of glucosylceramide synthase. Methods Enzymol. 311: 373-387.
    • (2000) Methods Enzymol , vol.311 , pp. 373-387
    • Shayman, J.A.1    Lee, L.2    Abe, A.3    Shu, L.4
  • 13
    • 33845580262 scopus 로고    scopus 로고
    • Positional specificity of lysosomal phospholipase A2
    • Abe, A., M. Hiraoka, and J. A. Shayman. 2006. Positional specificity of lysosomal phospholipase A2. J. Lipid Res. 47: 2268-2279.
    • (2006) J. Lipid Res , vol.47 , pp. 2268-2279
    • Abe, A.1    Hiraoka, M.2    Shayman, J.A.3
  • 14
    • 0027192943 scopus 로고
    • Metal ion and salt effects on the phospholipase A2, lysophospholipase, and transacylase activities of human cytosolic phospholipase A2
    • Reynolds, L. J., L. L. Hughes, A. I. Louis, R. M. Kramer, and E. A. Dennis. 1993. Metal ion and salt effects on the phospholipase A2, lysophospholipase, and transacylase activities of human cytosolic phospholipase A2. Biochim. Biophys. Acta. 1167: 272-280.
    • (1993) Biochim. Biophys. Acta , vol.1167 , pp. 272-280
    • Reynolds, L.J.1    Hughes, L.L.2    Louis, A.I.3    Kramer, R.M.4    Dennis, E.A.5
  • 15
    • 0036462573 scopus 로고    scopus 로고
    • Cytosolic phospholipase A2 shows burst kinetics consistent with the slow, reversible formation of a dead-end complex
    • Guenther, M. G., M. R. Witmer, and J. R. Burke. 2002. Cytosolic phospholipase A2 shows burst kinetics consistent with the slow, reversible formation of a dead-end complex. Arch. Biochem. Biophys. 398: 101-108.
    • (2002) Arch. Biochem. Biophys , vol.398 , pp. 101-108
    • Guenther, M.G.1    Witmer, M.R.2    Burke, J.R.3
  • 16
    • 0028820956 scopus 로고
    • Interfacial enzymology of glycerolipid hydrolases: Lessons from secreted phospholipases A2
    • Gelb, M. H., M. K. Jain, A. M. Hanel, and O. G. Berg. 1995. Interfacial enzymology of glycerolipid hydrolases: lessons from secreted phospholipases A2. Annu. Rev. Biochem. 64: 653-688.
    • (1995) Annu. Rev. Biochem , vol.64 , pp. 653-688
    • Gelb, M.H.1    Jain, M.K.2    Hanel, A.M.3    Berg, O.G.4
  • 17
    • 0034612345 scopus 로고    scopus 로고
    • Phospholipid:diacylglycerol acyltransferase: An enzyme that catalyzes the acyl-CoA-independent formation of triacylglycerol in yeast and plants
    • Dahlqvist, A., U. Stahl, M. Lenman, A. Banas, M. Lee, L. Sandager, H. Ronne, and S. Stymne. 2000. Phospholipid:diacylglycerol acyltransferase: an enzyme that catalyzes the acyl-CoA-independent formation of triacylglycerol in yeast and plants. Proc. Natl. Acad. Sci. USA. 97: 6487-6492.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 6487-6492
    • Dahlqvist, A.1    Stahl, U.2    Lenman, M.3    Banas, A.4    Lee, M.5    Sandager, L.6    Ronne, H.7    Stymne, S.8
  • 18
    • 10344262633 scopus 로고    scopus 로고
    • Identification, cloning, expression, and purification of three novel human calcium-independent phospholipase A2 family members possessing triacylglycerol lipase and acylglycerol transacylase activities
    • Jenkins, C. M., D. J. Mancuso, W. Yan, H. F. Sims, B. Gibson, and R. W. Gross. 2004. Identification, cloning, expression, and purification of three novel human calcium-independent phospholipase A2 family members possessing triacylglycerol lipase and acylglycerol transacylase activities. J. Biol. Chem. 279: 48968-48975.
    • (2004) J. Biol. Chem , vol.279 , pp. 48968-48975
    • Jenkins, C.M.1    Mancuso, D.J.2    Yan, W.3    Sims, H.F.4    Gibson, B.5    Gross, R.W.6
  • 19
    • 0031941433 scopus 로고    scopus 로고
    • Purification and characterization of a catalytic domain of rat intestinal phospholipase B/lipase associated with brush border membranes
    • Tojo, H., T. Ichida, and M. Okamoto. 1998. Purification and characterization of a catalytic domain of rat intestinal phospholipase B/lipase associated with brush border membranes. J. Biol. Chem. 273: 2214-2221.
    • (1998) J. Biol. Chem , vol.273 , pp. 2214-2221
    • Tojo, H.1    Ichida, T.2    Okamoto, M.3
  • 20
    • 0037113994 scopus 로고    scopus 로고
    • Purification and properties of a phospholipase A2/lipase preferring phosphatidic acid, bis(monoacylglycerol) phosphate, and monoacylglycerol from rat testis
    • Ito, M., U. Tchoua, M. Okamoto, and H. Tojo. 2002. Purification and properties of a phospholipase A2/lipase preferring phosphatidic acid, bis(monoacylglycerol) phosphate, and monoacylglycerol from rat testis. J. Biol. Chem. 277: 43674-43681.
    • (2002) J. Biol. Chem , vol.277 , pp. 43674-43681
    • Ito, M.1    Tchoua, U.2    Okamoto, M.3    Tojo, H.4
  • 21
    • 0029011876 scopus 로고    scopus 로고
    • Warne, T. R., F. G. Buchanan, and M. Robinson. 1995. Growth-dependent accumulation of monoalkylglycerol in Madin-Darby canine kidney cells. Evidence for a role in the regulation of protein kinase C. J. Biol. Chem. 270: 11147-11154.
    • Warne, T. R., F. G. Buchanan, and M. Robinson. 1995. Growth-dependent accumulation of monoalkylglycerol in Madin-Darby canine kidney cells. Evidence for a role in the regulation of protein kinase C. J. Biol. Chem. 270: 11147-11154.
  • 22
    • 0030049758 scopus 로고    scopus 로고
    • Biosynthesis of N-acetylsphingosine by platelet-activating factor: Sphingosine CoA-independent transacetylase in HL-60 cells
    • Lee, T. C., M. C. Ou, K. Shinozaki, B. Malone, and F. Snyder. 1996. Biosynthesis of N-acetylsphingosine by platelet-activating factor: sphingosine CoA-independent transacetylase in HL-60 cells. J. Biol. Chem. 271: 209-217.
    • (1996) J. Biol. Chem , vol.271 , pp. 209-217
    • Lee, T.C.1    Ou, M.C.2    Shinozaki, K.3    Malone, B.4    Snyder, F.5
  • 23
    • 0025295176 scopus 로고
    • Regulation of the synthesis of platelet-activating factor and its inactive storage precursor (1-alkyl-2-acyl-sn-glycero-3-phosphocholine) from 1-alkyl-2-acetyl-sn-glycerol by rabbit platelets
    • Lee, T. C., B. Malone, M. L. Blank, V. Fitzgerald, and F. Snyder. 1990. Regulation of the synthesis of platelet-activating factor and its inactive storage precursor (1-alkyl-2-acyl-sn-glycero-3-phosphocholine) from 1-alkyl-2-acetyl-sn-glycerol by rabbit platelets. J. Biol. Chem. 265: 9181-9187.
    • (1990) J. Biol. Chem , vol.265 , pp. 9181-9187
    • Lee, T.C.1    Malone, B.2    Blank, M.L.3    Fitzgerald, V.4    Snyder, F.5
  • 25
    • 0024268342 scopus 로고    scopus 로고
    • Bass, D. A., L. C. McPhail, J. D. Schmitt, S. Morris-Natschke, C. E. McCall, and R. L. Wykle. 1988. Selective priming of rate and duration of the respiratory burst of neutrophils by 1,2-diacyl and 1-O-alkyl-2-acyl diglycerides. Possible relation to effects on protein kinase C. J. Biol. Chem. 263: 19610-19617.
    • Bass, D. A., L. C. McPhail, J. D. Schmitt, S. Morris-Natschke, C. E. McCall, and R. L. Wykle. 1988. Selective priming of rate and duration of the respiratory burst of neutrophils by 1,2-diacyl and 1-O-alkyl-2-acyl diglycerides. Possible relation to effects on protein kinase C. J. Biol. Chem. 263: 19610-19617.
  • 26
    • 0021284810 scopus 로고
    • 1-O-Hexadecyl-2-acetyl-sn-glycerol stimulates differentiation of HL-60 human promyelocytic leukemia cells to macrophage-like cells
    • McNamara, M. J., J. D. Schmitt, R. L. Wykle, and L. W. Daniel. 1984. 1-O-Hexadecyl-2-acetyl-sn-glycerol stimulates differentiation of HL-60 human promyelocytic leukemia cells to macrophage-like cells. Biochem. Biophys. Res. Commun. 122: 824-830.
    • (1984) Biochem. Biophys. Res. Commun , vol.122 , pp. 824-830
    • McNamara, M.J.1    Schmitt, J.D.2    Wykle, R.L.3    Daniel, L.W.4
  • 27
    • 0021745955 scopus 로고
    • Metabolism of 1-O-alkyl-2-acetyl-sn-glycerol by washed rabbit platelets: Formation of platelet activating factor
    • Satouchi, K., M. Oda, K. Saito, and D. J. Hanahan. 1984. Metabolism of 1-O-alkyl-2-acetyl-sn-glycerol by washed rabbit platelets: formation of platelet activating factor. Arch. Biochem. Biophys. 234: 318-321.
    • (1984) Arch. Biochem. Biophys , vol.234 , pp. 318-321
    • Satouchi, K.1    Oda, M.2    Saito, K.3    Hanahan, D.J.4
  • 28
    • 0032459475 scopus 로고    scopus 로고
    • Biochemistry of the endogenous ligands of cannabinoid receptors
    • Di Marzo, V., and D. G. Deutsch. 1998. Biochemistry of the endogenous ligands of cannabinoid receptors. Neurobiol. Dis. 5: 386-404.
    • (1998) Neurobiol. Dis , vol.5 , pp. 386-404
    • Di Marzo, V.1    Deutsch, D.G.2
  • 29
    • 0016682741 scopus 로고
    • Ceramidase and ceramide synthesis in human kidney and cerebellum. Description of a new alkaline ceramidase
    • Sugita, M., M. Willians, J. T. Dulaney, and H. W. Moser. 1975. Ceramidase and ceramide synthesis in human kidney and cerebellum. Description of a new alkaline ceramidase. Biochim. Biophys. Acta. 398: 125-131.
    • (1975) Biochim. Biophys. Acta , vol.398 , pp. 125-131
    • Sugita, M.1    Willians, M.2    Dulaney, J.T.3    Moser, H.W.4


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