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Volumn 270, Issue 17, 2003, Pages 3498-3506

Uptake and metabolism of [3H]anandamide by rabbit platelets: Lack of transporter?

Author keywords

Anandamide; Anandamide transporter; Fatty acid amidohydrolase; Rabbit platelets

Indexed keywords

ANANDAMIDE; ARACHIDONIC ACID; CARRIER PROTEIN; FATTY ACID AMIDASE; PHOSPHOLIPID DERIVATIVE; TRITIUM; AMIDASE; AMIDE; ARACHIDONIC ACID DERIVATIVE; BENZYLSULFONYL FLUORIDE; CAFFEIC ACID DERIVATIVE; CANNABINOID; ENDOCANNABINOID; ENZYME INHIBITOR; INDOMETACIN; N (2 METHYL 3 HYDROXYPHENYL) 5,8,11,14 EICOSATETRAENAMIDE; N-(2-METHYL-3-HYDROXYPHENYL)-5,8,11,14-EICOSATETRAENAMIDE;

EID: 0041823726     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1033.2003.03724.x     Document Type: Article
Times cited : (31)

References (52)
  • 2
    • 0027489995 scopus 로고
    • Two new unsaturated fatty acid ethanolamides in brain that bind to the cannabinoid receptor
    • Hanus, L., Gopher, A., Almog, S. & Mechoulam, R. (1993) Two new unsaturated fatty acid ethanolamides in brain that bind to the cannabinoid receptor. J. Med. Chem. 36, 3032-3034.
    • (1993) J. Med. Chem. , vol.36 , pp. 3032-3034
    • Hanus, L.1    Gopher, A.2    Almog, S.3    Mechoulam, R.4
  • 5
    • 0036019387 scopus 로고    scopus 로고
    • Cellular transport of anandamide, 2-arachidonoylglycerol and palmitoylethanolamide-targets for drug development?
    • Fowler, C.J. & Jacobsson, S.O.P. (2002) Cellular transport of anandamide, 2-arachidonoylglycerol and palmitoylethanolamide-targets for drug development? Prostaglandins Leukot. Essent. Fatty Acids 66, 193-200.
    • (2002) Prostaglandins Leukot. Essent. Fatty Acids , vol.66 , pp. 193-200
    • Fowler, C.J.1    Jacobsson, S.O.P.2
  • 6
    • 0028787812 scopus 로고
    • Partial purification and characterization of the porcine brain enzyme hydrolyzing and synthesizing anandamide
    • Ueda, N., Kurahashi, Y., Yamamoto, S. & Tokunaga, T. (1995) Partial purification and characterization of the porcine brain enzyme hydrolyzing and synthesizing anandamide. J. Biol. Chem. 270, 23823-23827.
    • (1995) J. Biol. Chem. , vol.270 , pp. 23823-23827
    • Ueda, N.1    Kurahashi, Y.2    Yamamoto, S.3    Tokunaga, T.4
  • 7
    • 0029904838 scopus 로고    scopus 로고
    • Molecular characterization of an enzyme that degrades neuromodulatory fatty-acid amides
    • Cravatt, B.F., Giang, D.K., Mayfield, S.P., Boger, D.L., Lerner, R.A. & Gilula, N.B. (1996) Molecular characterization of an enzyme that degrades neuromodulatory fatty-acid amides. Nature 384, 83-87.
    • (1996) Nature , vol.384 , pp. 83-87
    • Cravatt, B.F.1    Giang, D.K.2    Mayfield, S.P.3    Boger, D.L.4    Lerner, R.A.5    Gilula, N.B.6
  • 8
    • 0027180394 scopus 로고
    • Enzymatic synthesis and degradation of anandamide, a cannabinoid receptor agonist
    • Deutsch, D. & Chin, S. (1993) Enzymatic synthesis and degradation of anandamide, a cannabinoid receptor agonist. Biochem. Pharmacol. 46, 791-796.
    • (1993) Biochem. Pharmacol. , vol.46 , pp. 791-796
    • Deutsch, D.1    Chin, S.2
  • 10
    • 0030852614 scopus 로고    scopus 로고
    • Accumulation of N-arachidonoylethanolamine (anandamide) into cerebellar granule cells occurs via facilitated diffusion
    • Hillard, C.J., Edgemond, W.S., Jarrahian, A. & Campbell, W.B. (1997) Accumulation of N-arachidonoylethanolamine (anandamide) into cerebellar granule cells occurs via facilitated diffusion. J. Neurochem. 69, 631-638.
    • (1997) J. Neurochem. , vol.69 , pp. 631-638
    • Hillard, C.J.1    Edgemond, W.S.2    Jarrahian, A.3    Campbell, W.B.4
  • 11
    • 0030865871 scopus 로고    scopus 로고
    • Functional role of high-affinity anandamide transport, as revealed by selective inhibition
    • Beltramo, M., Stella, N., Calignano, A., Lin, S.Y., Makriyannis, A. & Piomelli, D. (1997) Functional role of high-affinity anandamide transport, as revealed by selective inhibition. Science 277, 1094-1097.
    • (1997) Science , vol.277 , pp. 1094-1097
    • Beltramo, M.1    Stella, N.2    Calignano, A.3    Lin, S.Y.4    Makriyannis, A.5    Piomelli, D.6
  • 12
    • 0031031557 scopus 로고    scopus 로고
    • Biosynthesis, uptake and degradation of anandamide and palmitoylethanolamide in leukocytes
    • Bisogno, T., Maurelli, S., Melck, D., De Petrocellis, L. & Di Marzo, V. (1997) Biosynthesis, uptake and degradation of anandamide and palmitoylethanolamide in leukocytes. J. Biol. Chem. 272, 3315-3323.
    • (1997) J. Biol. Chem. , vol.272 , pp. 3315-3323
    • Bisogno, T.1    Maurelli, S.2    Melck, D.3    De Petrocellis, L.4    Di Marzo, V.5
  • 13
    • 0032973268 scopus 로고    scopus 로고
    • Anandamide activates human platelets through a pathway independent of the arachidonate cascade
    • Maccarrone, M., Bari, M., Menichelli, A., Del Principe, D. & Finazzi Agrò, A. (1999) Anandamide activates human platelets through a pathway independent of the arachidonate cascade. FEBS Lett. 447, 277-282.
    • (1999) FEBS Lett. , vol.447 , pp. 277-282
    • Maccarrone, M.1    Bari, M.2    Menichelli, A.3    Del Principe, D.4    Finazzi Agrò, A.5
  • 14
    • 0033961214 scopus 로고    scopus 로고
    • Human mast cells take up and hydrolyze anandamide under the control of 5-lipoxygenase and do not express cannabinoid receptors
    • Maccarrone, M., Fiorucci, L., Erba, F., Bari, M., Finazzi Agrò, A. & Ascoli, F. (2000) Human mast cells take up and hydrolyze anandamide under the control of 5-lipoxygenase and do not express cannabinoid receptors. FEBS Lett. 468, 176-180.
    • (2000) FEBS Lett. , vol.468 , pp. 176-180
    • Maccarrone, M.1    Fiorucci, L.2    Erba, F.3    Bari, M.4    Finazzi Agrò, A.5    Ascoli, F.6
  • 16
    • 0033666960 scopus 로고    scopus 로고
    • The movement of N-arachidonoylethanolamine (anandamide) across cellular membranes
    • Hillard, C.J. & Jarrahian, A. (2000) The movement of N-arachidonoylethanolamine (anandamide) across cellular membranes. Chem. Phys. Lipids 108, 123-134.
    • (2000) Chem. Phys. Lipids , vol.108 , pp. 123-134
    • Hillard, C.J.1    Jarrahian, A.2
  • 19
    • 0034644842 scopus 로고    scopus 로고
    • Overlap between the ligand recognition properties of the anandamide transporter and the VRI vanilloid receptor: Inhibitors of anandamide uptake with negligible capsaicin-like activity
    • De Petrocellis, L., Bisogno, T., Davis, J.B., Pertwee, R.G. & Di Marzo, V. (2000) Overlap between the ligand recognition properties of the anandamide transporter and the VRI vanilloid receptor: inhibitors of anandamide uptake with negligible capsaicin-like activity. FEBS Lett. 483, 52-56.
    • (2000) FEBS Lett. , vol.483 , pp. 52-56
    • De Petrocellis, L.1    Bisogno, T.2    Davis, J.B.3    Pertwee, R.G.4    Di Marzo, V.5
  • 20
    • 0035924218 scopus 로고    scopus 로고
    • Design, synthesis and biological evaluation of novel arachidonic acid detivatives as highly potent and selective endocannabinoid transporter inhibitors
    • Lopez-Rodriguez, M.L., Viso, A., Ortega-Gutierrez, S., Lastres-Becker, I., Gonzalez, S., Fernandez-Ruiz, J. & Ramos, J.A. (2001) Design, synthesis and biological evaluation of novel arachidonic acid detivatives as highly potent and selective endocannabinoid transporter inhibitors. J. Med. Chem. 44, 4505-4508.
    • (2001) J. Med. Chem. , vol.44 , pp. 4505-4508
    • Lopez-Rodriguez, M.L.1    Viso, A.2    Ortega-Gutierrez, S.3    Lastres-Becker, I.4    Gonzalez, S.5    Fernandez-Ruiz, J.6    Ramos, J.A.7
  • 21
    • 0034070409 scopus 로고    scopus 로고
    • Structure-activity relationships among N-arachidonylethanolamine (Anandamide) head group analogues for the anandamide transporter
    • Jarrahian, A., Manna, S., Edgemond, W.S., Campbell, W.B. & Hillard, C.J. (2000) Structure-activity relationships among N-arachidonylethanolamine (Anandamide) head group analogues for the anandamide transporter. J. Neurochem. 74, 2597-2606.
    • (2000) J. Neurochem. , vol.74 , pp. 2597-2606
    • Jarrahian, A.1    Manna, S.2    Edgemond, W.S.3    Campbell, W.B.4    Hillard, C.J.5
  • 24
    • 0034986485 scopus 로고    scopus 로고
    • Role of fatty acid amide hydrolase in the transport of the endogenous cannabinoid anandamide
    • Day, T.A, Rakhshan, F., Deutsch, D.G. & Barker, E.L. (2001) Role of fatty acid amide hydrolase in the transport of the endogenous cannabinoid anandamide. Mol. Pharmacol. 59, 1369-1375.
    • (2001) Mol. Pharmacol. , vol.59 , pp. 1369-1375
    • Day, T.A.1    Rakhshan, F.2    Deutsch, D.G.3    Barker, E.L.4
  • 27
    • 0029619298 scopus 로고
    • Two novel classes of neuroactive fatty acid amides are substrates for mouse neuroblastoma 'anandamide amidohydrolase'
    • Maurelli, S., Bisogno, T., De Petrocellis, L., Di Luccia, A., Marino, G. & Di Marzo, V. (1995) Two novel classes of neuroactive fatty acid amides are substrates for mouse neuroblastoma 'anandamide amidohydrolase'. FEBS Lett. 377, 82-86.
    • (1995) FEBS Lett. , vol.377 , pp. 82-86
    • Maurelli, S.1    Bisogno, T.2    De Petrocellis, L.3    Di Luccia, A.4    Marino, G.5    Di Marzo, V.6
  • 28
    • 0032559369 scopus 로고    scopus 로고
    • Anandamide amidohydrolase reacting with 2-arachidonoylglycerol, another cannabinoid receptor ligand
    • Goparaju, S.K., Ueda, N., Yamaguchi, H. & Yamamoto, S. (1998) Anandamide amidohydrolase reacting with 2-arachidonoylglycerol, another cannabinoid receptor ligand. FEBS Lett. 422, 69-73.
    • (1998) FEBS Lett. , vol.422 , pp. 69-73
    • Goparaju, S.K.1    Ueda, N.2    Yamaguchi, H.3    Yamamoto, S.4
  • 29
    • 0028317057 scopus 로고
    • Enzymatic synthesis of anandamide, an endogenous ligand for the cannabinoid receptor, by brain membranes
    • Devane, W.A. & Axelrod, J. (1994) Enzymatic synthesis of anandamide, an endogenous ligand for the cannabinoid receptor, by brain membranes. Proc. Natl Acad. Sci. USA 91, 6698-6701.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 6698-6701
    • Devane, W.A.1    Axelrod, J.2
  • 30
    • 0030866539 scopus 로고    scopus 로고
    • The cloned rat hydrolytic enzyme responsible for the breakdown of anandamide also catalyzes its formation via the condensation of arachidonic acid and ethanolamine
    • Arreaza, G., Devane, W.A., Omeir, R.L., Sajnani, G., Kunz, J., Cravatt, B.F. & Deutsch, D.G. (1997) The cloned rat hydrolytic enzyme responsible for the breakdown of anandamide also catalyzes its formation via the condensation of arachidonic acid and ethanolamine. Neurosci. Lett. 234, 59-62.
    • (1997) Neurosci. Lett. , vol.234 , pp. 59-62
    • Arreaza, G.1    Devane, W.A.2    Omeir, R.L.3    Sajnani, G.4    Kunz, J.5    Cravatt, B.F.6    Deutsch, D.G.7
  • 31
    • 0022376544 scopus 로고
    • Properties of rat liver N-acylethanolamine amidohydrolase
    • Schmid, P.C., Zuzarte-Augustin, M.L. & Schmid, H.H.O. (1985) Properties of rat liver N-acylethanolamine amidohydrolase. J. Biol. Chem. 260, 14145-14149.
    • (1985) J. Biol. Chem. , vol.260 , pp. 14145-14149
    • Schmid, P.C.1    Zuzarte-Augustin, M.L.2    Schmid, H.H.O.3
  • 32
    • 0028903996 scopus 로고
    • Anandamide amidohydrolase activity in rat brain microsomes. Identification and partial characterization
    • Desarnaud, F., Cadas, H. & Piomelli, D. (1995) Anandamide amidohydrolase activity in rat brain microsomes. Identification and partial characterization. J. Biol. Chem. 270, 6030-6035.
    • (1995) J. Biol. Chem. , vol.270 , pp. 6030-6035
    • Desarnaud, F.1    Cadas, H.2    Piomelli, D.3
  • 33
    • 0029133671 scopus 로고
    • Characterization of the kinetics and distribution of N-arachidonylethanolamine (anandamide) hydrolysis by rat brain
    • Hillard, C.J., Wilkison, D.M., Edgemond, W.S. & Campbell, W.B. (1995) Characterization of the kinetics and distribution of N-arachidonylethanolamine (anandamide) hydrolysis by rat brain. Biochim. Biophys. Acta 1257, 249-256.
    • (1995) Biochim. Biophys. Acta , vol.1257 , pp. 249-256
    • Hillard, C.J.1    Wilkison, D.M.2    Edgemond, W.S.3    Campbell, W.B.4
  • 34
    • 0035940988 scopus 로고    scopus 로고
    • Anandamide amidohydrolase activity, released in the medium by Tetrahymena pyriformis. Identification and partial characterization
    • Karava, V., Fasia, L. & Siafaka-Kapadai, A. (2001) Anandamide amidohydrolase activity, released in the medium by Tetrahymena pyriformis. Identification and partial characterization. FEBS Lett. 508, 327-331.
    • (2001) FEBS Lett. , vol.508 , pp. 327-331
    • Karava, V.1    Fasia, L.2    Siafaka-Kapadai, A.3
  • 37
    • 0031820286 scopus 로고    scopus 로고
    • Human platelets and polymorphonuclear leukocytes synthesize oxygenated derivatives of arachidonylethanolamide (anandamide): Their affinities for cannabinoid receptors and pathways of inactivation
    • Edgemond, W.S., Hillard, C.J., Falck, J.R., Kearn, C.S. & Campbell, W.B. (1998) Human platelets and polymorphonuclear leukocytes synthesize oxygenated derivatives of arachidonylethanolamide (anandamide): their affinities for cannabinoid receptors and pathways of inactivation. Mol. Pharmacol. 54, 180-188.
    • (1998) Mol. Pharmacol. , vol.54 , pp. 180-188
    • Edgemond, W.S.1    Hillard, C.J.2    Falck, J.R.3    Kearn, C.S.4    Campbell, W.B.5
  • 38
    • 0030611859 scopus 로고    scopus 로고
    • 2 ethanolamide from anandamide by cyclooxygenase-2
    • 2 ethanolamide from anandamide by cyclooxygenase-2. J. Biol. Chem. 272, 21181-21186.
    • (1997) J. Biol. Chem. , vol.272 , pp. 21181-21186
    • Yu, M.1    Ives, D.2    Ramesha, C.S.3
  • 39
    • 0018628697 scopus 로고
    • Physicochemical and functional identity of rabbit platelet-activating factor (PAF) released in vivo during IgE anaphylaxis with PAF released in vitro from IgE sensitized basophils
    • Pinckard, R.N., Farr, R.S. & Hanahan, D.J. (1979) Physicochemical and functional identity of rabbit platelet-activating factor (PAF) released in vivo during IgE anaphylaxis with PAF released in vitro from IgE sensitized basophils. J. Immunol. 123, 1847-1857.
    • (1979) J. Immunol. , vol.123 , pp. 1847-1857
    • Pinckard, R.N.1    Farr, R.S.2    Hanahan, D.J.3
  • 40
    • 0027411851 scopus 로고
    • An endogenous inhibitor of PAF-induced platelet aggregation, isolated from rat liver, has been identified as free fatty acid
    • Siafaka-Kapadai, A. & Hanahan, D.J. (1993) An endogenous inhibitor of PAF-induced platelet aggregation, isolated from rat liver, has been identified as free fatty acid. Biochim. Biophys. Acta 1166, 217-221.
    • (1993) Biochim. Biophys. Acta , vol.1166 , pp. 217-221
    • Siafaka-Kapadai, A.1    Hanahan, D.J.2
  • 41
    • 33845261493 scopus 로고
    • A rapid method of total lipid extraction and purification
    • Bligh, E.G. & Dyer, W. (1959) A rapid method of total lipid extraction and purification. Can. J. Biochem. Pharmacol. 37, 911-917.
    • (1959) Can. J. Biochem. Pharmacol. , vol.37 , pp. 911-917
    • Bligh, E.G.1    Dyer, W.2
  • 42
    • 0034616066 scopus 로고    scopus 로고
    • Activation of rabbit blood platelets by anandamide through its cleavage into arachidonic acid
    • Braud, S., Bon, C., Touqui, L. & Mounier, C. (2000) Activation of rabbit blood platelets by anandamide through its cleavage into arachidonic acid. FEBS Lett. 471, 12-16.
    • (2000) FEBS Lett. , vol.471 , pp. 12-16
    • Braud, S.1    Bon, C.2    Touqui, L.3    Mounier, C.4
  • 43
    • 0041590465 scopus 로고    scopus 로고
    • Effects of anandamide and other N-acylethanolamines on rabbit platelet function
    • May 15-17, Thessaloniki, Greece
    • Fasia, L. & Siafaka-Kapadai, A. (1997) Effects of anandamide and other N-acylethanolamines on rabbit platelet function. Proc. 11th Balkan Biochemical Biophysical Days, May 15-17, Thessaloniki, Greece, pp. 141.
    • (1997) Proc. 11th Balkan Biochemical Biophysical Days , pp. 141
    • Fasia, L.1    Siafaka-Kapadai, A.2
  • 44
    • 0024195210 scopus 로고
    • Metabolism of fatty acids by platelets and the functions of various metabolites in mediating platelet function
    • Lagarde, M. (1988) Metabolism of fatty acids by platelets and the functions of various metabolites in mediating platelet function. Prog. Lipid Res. 27, 135-152.
    • (1988) Prog. Lipid Res. , vol.27 , pp. 135-152
    • Lagarde, M.1
  • 45
    • 0024462290 scopus 로고
    • Biochemical mechanisms of platelet activation
    • Kroll, M.H. & Schafer, A.I. (1989) Biochemical mechanisms of platelet activation. Blood 74, 1181-1195.
    • (1989) Blood , vol.74 , pp. 1181-1195
    • Kroll, M.H.1    Schafer, A.I.2
  • 46
    • 0026480564 scopus 로고
    • Mammalian lipoxygenases: Molecular structures and functions
    • Yamamoto, S. (1992) Mammalian lipoxygenases: molecular structures and functions. Biochim. Biophys. Acta 1128, 117-131.
    • (1992) Biochim. Biophys. Acta , vol.1128 , pp. 117-131
    • Yamamoto, S.1
  • 47
    • 0035043018 scopus 로고    scopus 로고
    • Characterization of palmitoylethanolamide transport in mouse Neuro-2a neuroblastoma and rat RBL-2H3 basophilic leukaemia cells: Comparison with anandamide
    • Jacobsson, S.O.P. & Fowler, C.J. (2001) Characterization of palmitoylethanolamide transport in mouse Neuro-2a neuroblastoma and rat RBL-2H3 basophilic leukaemia cells: comparison with anandamide. Br. J. Pharmacol. 132, 1743-1754.
    • (2001) Br. J. Pharmacol. , vol.132 , pp. 1743-1754
    • Jacobsson, S.O.P.1    Fowler, C.J.2
  • 48
    • 0035452256 scopus 로고    scopus 로고
    • Fatty acid amide hydrolase: Biochemistry, pharmacology, and therapeutic possibilities for an enzyme hydrolyzing anandamide, 2-arachidonoylglycerol, palmitoylethanolamide, and oleamide
    • Fowler, C.J., Jonsson, K.-O. & Tiger, G. (2001) Fatty acid amide hydrolase: biochemistry, pharmacology, and therapeutic possibilities for an enzyme hydrolyzing anandamide, 2-arachidonoylglycerol, palmitoylethanolamide, and oleamide. Biochem. Pharmacol. 62, 517-526.
    • (2001) Biochem. Pharmacol. , vol.62 , pp. 517-526
    • Fowler, C.J.1    Jonsson, K.-O.2    Tiger, G.3
  • 49
    • 0026443725 scopus 로고
    • Non-cyclooxygenase-derived prostanoids (F2-isoprostanes) are formed in situ on phospholipids
    • Morrow, J.D., Awad, J.A., Boss, H.J., Blair, I.A. & Roberts, L.J. (1992) Non-cyclooxygenase-derived prostanoids (F2-isoprostanes) are formed in situ on phospholipids. Proc. Natl Acad. Sci. USA 89, 10721-10725.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 10721-10725
    • Morrow, J.D.1    Awad, J.A.2    Boss, H.J.3    Blair, I.A.4    Roberts, L.J.5
  • 50
    • 0028686640 scopus 로고
    • Cyclooxygenase-dependent formation of the isoprostane 8-epi-prostaglandin F2 alpha
    • Pratico, D., Lawson, J.A. & Fitzgerald, G.A. (1994) Cyclooxygenase-dependent formation of the isoprostane 8-epi-prostaglandin F2 alpha. Ann. N.Y. Acad. Sci. 744, 139-145.
    • (1994) Ann. N.Y. Acad. Sci. , vol.744 , pp. 139-145
    • Pratico, D.1    Lawson, J.A.2    Fitzgerald, G.A.3
  • 52
    • 0033567190 scopus 로고    scopus 로고
    • Biosynthesis and inactivation of the endocannabinoid 2-arachidonoylglycerol in circulating and tumoral macrophages
    • Di Marzo, V., Bisogno, T., De Petrocellis, L., Melck, D., Orlando, P., Wagner, J.A. & Kunos, G. (1999) Biosynthesis and inactivation of the endocannabinoid 2-arachidonoylglycerol in circulating and tumoral macrophages Eur. J. Biochem. 264, 258-267.
    • (1999) Eur. J. Biochem. , vol.264 , pp. 258-267
    • Di Marzo, V.1    Bisogno, T.2    De Petrocellis, L.3    Melck, D.4    Orlando, P.5    Wagner, J.A.6    Kunos, G.7


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