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Volumn 39, Issue 5, 1998, Pages 1118-1126

Synthesis of an unsaturated fatty acid analogue (18-(4'-azido-2'-hydroxybenzoylamino)-oleic acid) and its interaction with lysophosphatidylcholine: Acyl-CoA-O-acyltransferase

Author keywords

amino oleic acid; 18 (4' azido 2' hydroxybenzoylamino) oleoyl CoA; Acyl CoA analogue; Photoaffinity label

Indexed keywords

1 ACYLGLYCEROPHOSPHOCHOLINE ACYLTRANSFERASE; LYSOPHOSPHATIDYLCHOLINE; OLEIC ACID; UNSATURATED FATTY ACID;

EID: 0031898274     PISSN: 00222275     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (5)

References (48)
  • 2
    • 0024435355 scopus 로고
    • Fatty acyl-coenzyme A is required for budding of transport vesicles from Golgi cisternae
    • Pfanner, N., L. Orci, B. S. Glick, M. Amherdt, S. R. Aeden, V. Malhotra, and J. E. Rothman. 1989. Fatty acyl-coenzyme A is required for budding of transport vesicles from Golgi cisternae. Cell. 59: 95-102.
    • (1989) Cell. , vol.59 , pp. 95-102
    • Pfanner, N.1    Orci, L.2    Glick, B.S.3    Amherdt, M.4    Aeden, S.R.5    Malhotra, V.6    Rothman, J.E.7
  • 3
    • 0001787224 scopus 로고
    • Enzymes of membrane phospholipid metabolism in animals
    • 1st ed. A. Martonosi, editor. Plenum Press, New York
    • Lands, W. E., and G. C. Crawford. 1976. Enzymes of membrane phospholipid metabolism in animals. In The Enzymes of Biological Membranes. Vol. II. 1st ed. A. Martonosi, editor. Plenum Press, New York. 3-85.
    • (1976) The Enzymes of Biological Membranes , vol.2 , pp. 3-85
    • Lands, W.E.1    Crawford, G.C.2
  • 4
    • 0003018098 scopus 로고
    • Studies on the acylation of lysolecithin by rat brain
    • Webster, G. R., and R. J. Alpern. 1964. Studies on the acylation of lysolecithin by rat brain. Biochem. J. 50: 35-42.
    • (1964) Biochem. J. , vol.50 , pp. 35-42
    • Webster, G.R.1    Alpern, R.J.2
  • 5
    • 0014027841 scopus 로고
    • Studies on the role of phospholipids in phagocytosis
    • Sastry, P. S., and L. E. Hokin. 1966. Studies on the role of phospholipids in phagocytosis. J. Biol. Chem. 241: 3354-3361.
    • (1966) J. Biol. Chem. , vol.241 , pp. 3354-3361
    • Sastry, P.S.1    Hokin, L.E.2
  • 6
    • 0014338149 scopus 로고
    • Acylation of lysophosphatides by plasma membrane fractions of rat liver
    • Stein, Y., C. Widnell, and O. Stein. 1968. Acylation of lysophosphatides by plasma membrane fractions of rat liver. J. Cell. Biol. 39: 185-192.
    • (1968) J. Cell. Biol. , vol.39 , pp. 185-192
    • Stein, Y.1    Widnell, C.2    Stein, O.3
  • 7
    • 0020464876 scopus 로고
    • Selective incorporation of polyunsaturated fatty acids into phosphatidylcholine by rat liver microsomes
    • Lands, W. E., M. Inoue, Y. Sugiura, and H. Okuyama. 1982. Selective incorporation of polyunsaturated fatty acids into phosphatidylcholine by rat liver microsomes. J. Biol. Chem. 257: 14968-14972.
    • (1982) J. Biol. Chem. , vol.257 , pp. 14968-14972
    • Lands, W.E.1    Inoue, M.2    Sugiura, Y.3    Okuyama, H.4
  • 8
    • 0019961652 scopus 로고
    • How is the level of free arachidonic acid controlled in mammalian cells?
    • Irvine, R. F. 1982. How is the level of free arachidonic acid controlled in mammalian cells? Biochem. J. 204: 3-16.
    • (1982) Biochem. J. , vol.204 , pp. 3-16
    • Irvine, R.F.1
  • 9
    • 0024384211 scopus 로고
    • Regulation of prostaglandin synthesis by protein kinase C in mouse peritoneal macrophages
    • Pfannkuche, H. J., V. Kaever, D. Gemsa, and K. Resch. 1989. Regulation of prostaglandin synthesis by protein kinase C in mouse peritoneal macrophages. Biochem. J. 260: 471-478.
    • (1989) Biochem. J. , vol.260 , pp. 471-478
    • Pfannkuche, H.J.1    Kaever, V.2    Gemsa, D.3    Resch, K.4
  • 10
    • 0019958103 scopus 로고
    • Phospholipid metabolism of stimulated lymphocytes. Preferential incorporation of polyunsaturated fatty acids into microsomal phospholipid upon activation with concanavalin A
    • Rode, H. N., M. Szamel, S. Schneider, and K. Resch. 1982. Phospholipid metabolism of stimulated lymphocytes. Preferential incorporation of polyunsaturated fatty acids into microsomal phospholipid upon activation with concanavalin A. Biochim. Biophys. Acta. 688: 66-74.
    • (1982) Biochim. Biophys. Acta. , vol.688 , pp. 66-74
    • Rode, H.N.1    Szamel, M.2    Schneider, S.3    Resch, K.4
  • 11
    • 0022644923 scopus 로고
    • Inhibition of T-lymphocyte activation by cyclosporin A: Interference with the early activation of plasma membrane phospholipid metabolism
    • Szamel, M., P. Berger, and K. Resch. 1986. Inhibition of T-lymphocyte activation by cyclosporin A: interference with the early activation of plasma membrane phospholipid metabolism. J. Immunol. 136: 264-269.
    • (1986) J. Immunol. , vol.136 , pp. 264-269
    • Szamel, M.1    Berger, P.2    Resch, K.3
  • 12
    • 0023200280 scopus 로고
    • Polyunsaturated fatty acids are enriched in plasma membranes of mitogen-stimulated T-lymphocytes
    • Goppelt-Strübe, M., and K. Resch. 1987. Polyunsaturated fatty acids are enriched in plasma membranes of mitogen-stimulated T-lymphocytes. Biochim. Biophys. Acta. 904: 22-28.
    • (1987) Biochim. Biophys. Acta. , vol.904 , pp. 22-28
    • Goppelt-Strübe, M.1    Resch, K.2
  • 13
    • 0024454277 scopus 로고
    • Activation signals in human lymphocytes. Incorporation of polyunsaturated fatty acids into plasma membrane phospholipids regulates IL-2 synthesis via sustained activation of protein kinase C
    • Szamel, M., B. Rehermann, B. Krebs, R. Kurrle, and K. Resch. 1989. Activation signals in human lymphocytes. Incorporation of polyunsaturated fatty acids into plasma membrane phospholipids regulates IL-2 synthesis via sustained activation of protein kinase C. J. Immunol. 143: 2806-2813.
    • (1989) J. Immunol. , vol.143 , pp. 2806-2813
    • Szamel, M.1    Rehermann, B.2    Krebs, B.3    Kurrle, R.4    Resch, K.5
  • 14
    • 0027443099 scopus 로고
    • Cyclosporin A inhibits T cell receptor-induced interleukin-2 synthesis of human T lymphocytes by selectively preventing a transmembrane signal transduction pathway leading to sustained activation of a protein kinase C isoenzyme protein kinase C-beta
    • Szamel, M., F. Bartels, and K. Resch. 1993. Cyclosporin A inhibits T cell receptor-induced interleukin-2 synthesis of human T lymphocytes by selectively preventing a transmembrane signal transduction pathway leading to sustained activation of a protein kinase C isoenzyme protein kinase C-beta. Eur. J. Immunol. 23: 3072-3081.
    • (1993) Eur. J. Immunol. , vol.23 , pp. 3072-3081
    • Szamel, M.1    Bartels, F.2    Resch, K.3
  • 15
    • 0028832018 scopus 로고
    • T-Cell antigen receptor-induced signal transduction pathways. Activation and function of protein kinases C in T lymphocytes
    • Szamel, M., and K. Resch. 1995. T-Cell antigen receptor-induced signal transduction pathways. Activation and function of protein kinases C in T lymphocytes. Eur. J. Biochem. 228: 1-15.
    • (1995) Eur. J. Biochem. , vol.228 , pp. 1-15
    • Szamel, M.1    Resch, K.2
  • 17
    • 0001021169 scopus 로고
    • Metabolism of glycerolipids. VI. Specificities of acyl-CoA: Phospholipid acyltransterases
    • Lands, W. E., and P. Hart. 1965. Metabolism of glycerolipids. VI. Specificities of acyl-CoA: phospholipid acyltransterases. J. Biol. Chem. 240: 1905-1911.
    • (1965) J. Biol. Chem. , vol.240 , pp. 1905-1911
    • Lands, W.E.1    Hart, P.2
  • 18
    • 0014694709 scopus 로고
    • Effects of ethylenic bond position upon acyltransferase activity with isomeric cis-octadecenoyl coenzyme A thiol esters
    • Reitz, R. C., M. El-Sheikh, W. M. Lands, I. Ismail, and F. D. Gunstone. 1969. Effects of ethylenic bond position upon acyltransferase activity with isomeric cis-octadecenoyl coenzyme A thiol esters. Biochim. Biophys. Acta. 176: 480-490.
    • (1969) Biochim. Biophys. Acta. , vol.176 , pp. 480-490
    • Reitz, R.C.1    El-Sheikh, M.2    Lands, W.M.3    Ismail, I.4    Gunstone, F.D.5
  • 19
    • 0020554250 scopus 로고
    • The role of acyl transferase in the biosynthesis of pulmonary microsomal phosphatidylglycerol
    • Sanford, G. L., and M. F. Frosolono. 1983. The role of acyl transferase in the biosynthesis of pulmonary microsomal phosphatidylglycerol. Biochem. Biophys. Res. Commun. 116: 23-29.
    • (1983) Biochem. Biophys. Res. Commun. , vol.116 , pp. 23-29
    • Sanford, G.L.1    Frosolono, M.F.2
  • 20
    • 0020973816 scopus 로고
    • Lysophosphatidylcholine acyltransferase: Purification and applications in membrane studies
    • Gavino, V. C., and D. W. Deamer. 1983. Lysophosphatidylcholine acyltransferase: purification and applications in membrane studies. Ann. NY Acad. Sci. 414:90-96.
    • (1983) Ann. NY Acad. Sci. , vol.414 , pp. 90-96
    • Gavino, V.C.1    Deamer, D.W.2
  • 21
    • 0029875204 scopus 로고    scopus 로고
    • Formation of vesicles by the action of acyl-CoA:1-acyllysophosphatidylcholine acyltransferase from rat liver microsomes: Optimal solubilization conditions and analysis of lipid composition and enzyme activity
    • Fyrst, H., D. V. Pham, B. H. Lubin, and F. A. Kuypers. 1996. Formation of vesicles by the action of acyl-CoA:1-acyllysophosphatidylcholine acyltransferase from rat liver microsomes: optimal solubilization conditions and analysis of lipid composition and enzyme activity. Biochemistry. 35: 2644-2650.
    • (1996) Biochemistry , vol.35 , pp. 2644-2650
    • Fyrst, H.1    Pham, D.V.2    Lubin, B.H.3    Kuypers, F.A.4
  • 22
    • 0023806713 scopus 로고
    • Acylation of lysophosphatidylcholine in bovine heart muscle microsomes: Purification and kinetic properties of acyl-CoA:1-acyl-sn-glycero-3-phosphocholine O-acyltransferase
    • Sanjanwala, M., G. Y. Sun, M. A. Cutrera, and R. A. MacQuarrie. 1988: Acylation of lysophosphatidylcholine in bovine heart muscle microsomes: purification and kinetic properties of acyl-CoA:1-acyl-sn-glycero-3-phosphocholine O-acyltransferase. Arch. Biochem. Biophys. 265: 476-483.
    • (1988) Arch. Biochem. Biophys. , vol.265 , pp. 476-483
    • Sanjanwala, M.1    Sun, G.Y.2    Cutrera, M.A.3    MacQuarrie, R.A.4
  • 23
    • 0024373013 scopus 로고
    • Purification and kinetic properties of lysophosphatidylinositol acyltransferase from bovine heart muscle microsomes and comparison with lysophosphatidylcholine acyltransferase
    • Sanjanwala, M., G. Y. Sun, and R. A. MacQuarrie. 1989. Purification and kinetic properties of lysophosphatidylinositol acyltransferase from bovine heart muscle microsomes and comparison with lysophosphatidylcholine acyltransferase. Arch. Biochem. Biophys. 271: 407-413.
    • (1989) Arch. Biochem. Biophys. , vol.271 , pp. 407-413
    • Sanjanwala, M.1    Sun, G.Y.2    MacQuarrie, R.A.3
  • 24
    • 0025103379 scopus 로고
    • 12-[(5-Iodo-4-azido-2-hydroxybenzoyl)amino]dodecanoic acid: Biological recognition by cholesterol esterase and acyl-CoA:cholesterol O-acyltransferase
    • Kinnunen, P. M., F. H. Klopf, C. A. Bastiani, C. M. Gelfman, and L. G. Lange. 1990. 12-[(5-Iodo-4-azido-2-hydroxybenzoyl)amino]dodecanoic acid: biological recognition by cholesterol esterase and acyl-CoA:cholesterol O-acyltransferase. Biochemistry. 29: 1648-1654.
    • (1990) Biochemistry , vol.29 , pp. 1648-1654
    • Kinnunen, P.M.1    Klopf, F.H.2    Bastiani, C.A.3    Gelfman, C.M.4    Lange, L.G.5
  • 25
    • 0025066382 scopus 로고
    • Determination by photoaffinity labelling of the hydrophobic part of the binding site for acyl-CoA esters on acyl-CoA-binding protein from bovine liver
    • Hach, M., S. N. Pedersen, T. Borchers, P. Hojrup, and J. Knudsen. 1990. Determination by photoaffinity labelling of the hydrophobic part of the binding site for acyl-CoA esters on acyl-CoA-binding protein from bovine liver. Biochem. J. 271: 231-236.
    • (1990) Biochem. J. , vol.271 , pp. 231-236
    • Hach, M.1    Pedersen, S.N.2    Borchers, T.3    Hojrup, P.4    Knudsen, J.5
  • 26
    • 0027323805 scopus 로고
    • Identification of high affinity membrane-bound fatty acid binding proteins using a photoreactive fatty acid
    • Gerber, G. E., D. Mangroo, and B. L. Trigatti. 1993. Identification of high affinity membrane-bound fatty acid binding proteins using a photoreactive fatty acid. Mol. Cell. Biochem. 123: 39-44.
    • (1993) Mol. Cell. Biochem. , vol.123 , pp. 39-44
    • Gerber, G.E.1    Mangroo, D.2    Trigatti, B.L.3
  • 27
    • 0027196275 scopus 로고
    • Specific labeling of Candida tropicalis peroxisomal proteins with photoreactive fatty acid derivatives
    • Mangroo, D., L. Steele, R. A. Rachubinski, and G. E. Gerber. 1993. Specific labeling of Candida tropicalis peroxisomal proteins with photoreactive fatty acid derivatives. Biochim. Biophys. Acta. 1168: 280-284.
    • (1993) Biochim. Biophys. Acta. , vol.1168 , pp. 280-284
    • Mangroo, D.1    Steele, L.2    Rachubinski, R.A.3    Gerber, G.E.4
  • 28
    • 0027322073 scopus 로고
    • Photoreactive fatty acid analogues that bind to the rat liver fatty acid binding protein: 11-(5′-aziclosalicylamido)-undecanoic acid derivatives
    • Atlasovich, F., J. A. Santome, and H. N. Fernandez. 1993. Photoreactive fatty acid analogues that bind to the rat liver fatty acid binding protein: 11-(5′-aziclosalicylamido)-undecanoic acid derivatives. Mol. Cell. Biochem. 120: 15-23.
    • (1993) Mol. Cell. Biochem. , vol.120 , pp. 15-23
    • Atlasovich, F.1    Santome, J.A.2    Fernandez, H.N.3
  • 29
    • 0029040175 scopus 로고
    • Photo-affinity labeling of cottonseed microsomal N-acylphosphatidylethanolamine synthase protein with a substrate analogue, 12-[(4-azidosalicyl)amino]dodecanoic acid
    • McAndrew, R. S., B. P. Leonard, and K. D. Chapman. 1995. Photo-affinity labeling of cottonseed microsomal N-acylphosphatidylethanolamine synthase protein with a substrate analogue, 12-[(4-azidosalicyl)amino]dodecanoic acid. Biochim. Biophys. Acta. 1256: 310-318.
    • (1995) Biochim. Biophys. Acta. , vol.1256 , pp. 310-318
    • McAndrew, R.S.1    Leonard, B.P.2    Chapman, K.D.3
  • 30
    • 0028827114 scopus 로고
    • Photolabeling acyl CoA binding proteins in microsome preparations
    • Hare, J. F. 1995. Photolabeling acyl CoA binding proteins in microsome preparations. FEBS Lett. 375: 188-192.
    • (1995) FEBS Lett. , vol.375 , pp. 188-192
    • Hare, J.F.1
  • 31
    • 0030590212 scopus 로고    scopus 로고
    • Identification of two different lysophosphatidylcholine:acyl-CoA acyltransferases (LAT) in pig spleen with putative distinct topological localization
    • Kerkhoff, C., L. Gehring, K. Habben, K. Resch, and V. Kaever. 1996. Identification of two different lysophosphatidylcholine:acyl-CoA acyltransferases (LAT) in pig spleen with putative distinct topological localization. Biochim. Biophys. Acta. 1302: 249-256.
    • (1996) Biochim. Biophys. Acta. , vol.1302 , pp. 249-256
    • Kerkhoff, C.1    Gehring, L.2    Habben, K.3    Resch, K.4    Kaever, V.5
  • 32
    • 84982335277 scopus 로고
    • Ueber den Sexuallockstoff des Seidenspinners. IV. Die Synthese des Bombykols und der cis/trans-isomeren Hexadecadien-(10.12)ole (1)
    • Butenand, A., E. Hecker, M. Hopp, and W. Koch. 1962. Ueber den Sexuallockstoff des Seidenspinners. IV. Die Synthese des Bombykols und der cis/trans-isomeren Hexadecadien-(10.12)ole (1). Liebigs Ann. Chem. 658: 39-64.
    • (1962) Liebigs Ann. Chem. , vol.658 , pp. 39-64
    • Butenand, A.1    Hecker, E.2    Hopp, M.3    Koch, W.4
  • 33
    • 0022355363 scopus 로고
    • A facile synthesis of 1,4-benzochinones having a hydroxylalkyl side chain
    • Goto, G., K. Okamoto, T. Okutani, and I. Imada. 1985. A facile synthesis of 1,4-benzochinones having a hydroxylalkyl side chain. Chem. Pharm. Bull. 33: 4422-4431.
    • (1985) Chem. Pharm. Bull. , vol.33 , pp. 4422-4431
    • Goto, G.1    Okamoto, K.2    Okutani, T.3    Imada, I.4
  • 34
    • 0005244598 scopus 로고
    • Stereoselective synthesis of (2;E)-9,11-tetradecadienyl-1-acetate, a major component of the sex pheromone of Spodoptera litura
    • Goto, G., T. Shima, H. Masuya, Y. Masuoka, and K. Hiraga. 1975. Stereoselective synthesis of (2;E)-9,11-tetradecadienyl-1-acetate, a major component of the sex pheromone of Spodoptera litura. Chem. Lett. 1975: 103-106.
    • (1975) Chem. Lett. , vol.1975 , pp. 103-106
    • Goto, G.1    Shima, T.2    Masuya, H.3    Masuoka, Y.4    Hiraga, K.5
  • 35
    • 84982485191 scopus 로고
    • Darstellung lithiumsalzfreier Ylidlösungen mit Natrium-bis(trimethylsilyl)amid als Base
    • Bestmann, H. J., W. Stransky, and O. Vostrowsky. 1976. Darstellung lithiumsalzfreier Ylidlösungen mit Natrium-bis(trimethylsilyl)amid als Base. Chem. Ber. 109: 1694-1700.
    • (1976) Chem. Ber. , vol.109 , pp. 1694-1700
    • Bestmann, H.J.1    Stransky, W.2    Vostrowsky, O.3
  • 36
    • 0026355216 scopus 로고
    • Cyclische Ether als Edukte zur Synthese von Schmetterlings-Pheromonen
    • Poleschner, H., M. Heydenreich, and D. Martin. 1991. Cyclische Ether als Edukte zur Synthese von Schmetterlings-Pheromonen. Synthesis. 1991: 1231-1235.
    • (1991) Synthesis , vol.1991 , pp. 1231-1235
    • Poleschner, H.1    Heydenreich, M.2    Martin, D.3
  • 37
    • 0019051169 scopus 로고
    • 14C-labeled fatty acyl coenzyme A's of high specific activity
    • 14C-labeled fatty acyl coenzyme A's of high specific activity. Anal. Biochem. 106: 344-350.
    • (1980) Anal. Biochem. , vol.106 , pp. 344-350
    • Bishop, J.E.1    Hajra, A.K.2
  • 39
    • 0021355340 scopus 로고
    • A method for the quantitative recovery of protein in dilute solution in the presence of detergents and lipids
    • Wessel, D., and U. I. Flügge. 1984. A method for the quantitative recovery of protein in dilute solution in the presence of detergents and lipids. Anal. Biochem. 138: 141-143.
    • (1984) Anal. Biochem. , vol.138 , pp. 141-143
    • Wessel, D.1    Flügge, U.I.2
  • 40
    • 0021701812 scopus 로고
    • Coomassie brillant blue staining of lipids on thin-layer plates
    • Nakamura, K., and S. Handa. 1984. Coomassie brillant blue staining of lipids on thin-layer plates. Anal. Biochem. 142: 406-10.
    • (1984) Anal. Biochem. , vol.142 , pp. 406-410
    • Nakamura, K.1    Handa, S.2
  • 41
    • 0027491516 scopus 로고
    • Photoaffinity labeling of acyl-CoA oxidase with 12-azidooleoyl-CoA and 12-[(4-azidosalicyl)amino]dodecanoyl-CoA
    • Rajasekharan, R., R. C. Marians, J. M. Shockey, and J. D. Kemp. 1993. Photoaffinity labeling of acyl-CoA oxidase with 12-azidooleoyl-CoA and 12-[(4-azidosalicyl)amino]dodecanoyl-CoA. Biochemistry. 32: 12386-12391.
    • (1993) Biochemistry , vol.32 , pp. 12386-12391
    • Rajasekharan, R.1    Marians, R.C.2    Shockey, J.M.3    Kemp, J.D.4
  • 42
    • 0028343306 scopus 로고
    • Use of photoreactive substrates for characterization of lysophosphatidate acyltransferases from developing soybean cotyledons
    • Rajasekharan, R., and V. Nachiappan. 1994. Use of photoreactive substrates for characterization of lysophosphatidate acyltransferases from developing soybean cotyledons. Arch. Biochem. Biophys. 311: 389-394.
    • (1994) Arch. Biochem. Biophys. , vol.311 , pp. 389-394
    • Rajasekharan, R.1    Nachiappan, V.2
  • 43
    • 0028269867 scopus 로고
    • Photolabeling of soybean microsomal membrane proteins with photoreactive acyl-CoA analogs
    • Rajasekharan, R., V. Nachiappan, and H. S. Roychowdhury. 1994. Photolabeling of soybean microsomal membrane proteins with photoreactive acyl-CoA analogs. Eur. J. Biochem. 220: 1013-1018.
    • (1994) Eur. J. Biochem. , vol.220 , pp. 1013-1018
    • Rajasekharan, R.1    Nachiappan, V.2    Roychowdhury, H.S.3
  • 44
    • 0030010058 scopus 로고    scopus 로고
    • Photoactivated azido fatty acid irreversibly inhibits anion and proton transport through the mitochondrial incoupling protein
    • Jezek, P., J. Hanus, C. Semrad, and K. D. Garlid. 1996. Photoactivated azido fatty acid irreversibly inhibits anion and proton transport through the mitochondrial incoupling protein. J. Biol. Chem. 271: 6199-6205.
    • (1996) J. Biol. Chem. , vol.271 , pp. 6199-6205
    • Jezek, P.1    Hanus, J.2    Semrad, C.3    Garlid, K.D.4


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