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Volumn 1441, Issue 1, 1999, Pages 77-84

Anandamide amidohydrolase of porcine brain: cDNA cloning, functional expression and site-directed mutagenesis

Author keywords

Amidohydrolase; Anandamide; Brain; Cannabinoid; Fatty acid amide hydrolase; Pig

Indexed keywords

AMIDASE; ANANDAMIDE; CANNABINOID; CANNABINOID RECEPTOR; COMPLEMENTARY DNA;

EID: 0032883310     PISSN: 13881981     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1388-1981(99)00143-2     Document Type: Article
Times cited : (50)

References (26)
  • 2
    • 0022376544 scopus 로고
    • Properties of rat liver N-acylethanolamine amidohydrolase
    • Schmid P.C., Zuzarte-Augustin M.L., Schmid H.H.O. Properties of rat liver N-acylethanolamine amidohydrolase. J. Biol. Chem. 260:1985;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
  • 3
    • 0027180394 scopus 로고
    • Enzymatic synthesis and degradation of anandamide, a cannabinoid receptor agonist
    • Deutsch D.G., Chin S.A. Enzymatic synthesis and degradation of anandamide, a cannabinoid receptor agonist. Biochem. Pharmacol. 46:1993;791-796.
    • (1993) Biochem. Pharmacol. , vol.46 , pp. 791-796
    • Deutsch, D.G.1    Chin, S.A.2
  • 4
    • 0028903996 scopus 로고
    • Anandamide amidohydrolase activity in rat brain microsomes. Identification and partial characterization
    • Desarnaud F., Cadas H., Piomelli D. Anandamide amidohydrolase activity in rat brain microsomes. Identification and partial characterization. J. Biol. Chem. 270:1995;6030-6035.
    • (1995) J. Biol. Chem. , vol.270 , pp. 6030-6035
    • Desarnaud, F.1    Cadas, H.2    Piomelli, D.3
  • 5
    • 0028787812 scopus 로고
    • Partial purification and characterization of the porcine brain enzyme hydrolyzing and synthesizing anandamide
    • Ueda N., Kurahashi Y., Yamamoto S., Tokunaga T. Partial purification and characterization of the porcine brain enzyme hydrolyzing and synthesizing anandamide. J. Biol. Chem. 270:1995;23823-23827.
    • (1995) J. Biol. Chem. , vol.270 , pp. 23823-23827
    • Ueda, N.1    Kurahashi, Y.2    Yamamoto, S.3    Tokunaga, T.4
  • 6
    • 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. Molecular characterization of an enzyme that degrades neuromodulatory fatty-acid amides. Nature. 384:1996;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
  • 7
    • 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. Two novel classes of neuroactive fatty acid amides are substrates for mouse neuroblastoma 'anandamide amidohydrolase'. FEBS Lett. 377:1995;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
  • 8
    • 0031589532 scopus 로고    scopus 로고
    • Reversible hydrolysis and synthesis of anandamide demonstrated by recombinant rat fatty-acid amide hydrolase
    • Kurahashi Y., Ueda N., Suzuki H., Suzuki M., Yamamoto S. Reversible hydrolysis and synthesis of anandamide demonstrated by recombinant rat fatty-acid amide hydrolase. Biochem. Biophys. Res. Commun. 237:1997;512-515.
    • (1997) Biochem. Biophys. Res. Commun. , vol.237 , pp. 512-515
    • Kurahashi, Y.1    Ueda, N.2    Suzuki, H.3    Suzuki, M.4    Yamamoto, S.5
  • 9
    • 0032559369 scopus 로고    scopus 로고
    • Anandamide amidohydrolase reacting with 2-arachidonoylglycerol, another cannabinoid receptor ligand
    • Goparaju S.K., Ueda N., Yamaguchi H., Yamamoto S. Anandamide amidohydrolase reacting with 2-arachidonoylglycerol, another cannabinoid receptor ligand. FEBS Lett. 422:1998;69-73.
    • (1998) FEBS Lett. , vol.422 , pp. 69-73
    • Goparaju, S.K.1    Ueda, N.2    Yamaguchi, H.3    Yamamoto, S.4
  • 10
    • 0032055496 scopus 로고    scopus 로고
    • The novel endogenous cannabinoid 2-arachidonoylglycerol is inactivated by neuronal- And basophil-like cells: Connections with anandamide
    • Di Marzo V., Bisogno T., Sugiura T., Melck D., De Petrocellis L. The novel endogenous cannabinoid 2-arachidonoylglycerol is inactivated by neuronal- and basophil-like cells: connections with anandamide. Biochem. J. 331:1998;15-19.
    • (1998) Biochem. J. , vol.331 , pp. 15-19
    • Di Marzo, V.1    Bisogno, T.2    Sugiura, T.3    Melck, D.4    De Petrocellis, L.5
  • 11
    • 0001048154 scopus 로고    scopus 로고
    • Distribution of anandamide amidohydrolase in rat tissues with special reference to small intestine
    • Katayama K., Ueda N., Kurahashi Y., Suzuki H., Yamamoto S., Kato I. Distribution of anandamide amidohydrolase in rat tissues with special reference to small intestine. Biochim. Biophys. Acta. 1347:1997;212-218.
    • (1997) Biochim. Biophys. Acta , vol.1347 , pp. 212-218
    • Katayama, K.1    Ueda, N.2    Kurahashi, Y.3    Suzuki, H.4    Yamamoto, S.5    Kato, I.6
  • 12
    • 0029800322 scopus 로고    scopus 로고
    • The uterus is a potential site for anandamide synthesis and hydrolysis: Differential profiles of anandamide synthase and hydrolase activities in the mouse uterus during the periimplantation period
    • Paria B.C., Deutsch D.G., Dey S.K. The uterus is a potential site for anandamide synthesis and hydrolysis: differential profiles of anandamide synthase and hydrolase activities in the mouse uterus during the periimplantation period. Mol. Reprod. Dev. 45:1996;183-192.
    • (1996) Mol. Reprod. Dev. , vol.45 , pp. 183-192
    • Paria, B.C.1    Deutsch, D.G.2    Dey, S.K.3
  • 14
    • 0030903752 scopus 로고    scopus 로고
    • Molecular characterization of human and mouse fatty acid amide hydrolases
    • Giang D.K., Cravatt B.F. Molecular characterization of human and mouse fatty acid amide hydrolases. Proc. Natl. Acad. Sci. USA. 94:1997;2238-2242.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 2238-2242
    • Giang, D.K.1    Cravatt, B.F.2
  • 15
    • 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. 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. 234:1997;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
  • 16
    • 0032573124 scopus 로고    scopus 로고
    • Comparative characterization of a wild type and transmembrane domain-deleted fatty acid amide hydrolase: Identification of the transmembrane domain as a site for oligomerization
    • Patricelli M.P., Lashuel H.A., Giang D.K., Kelly J.W., Cravatt B.F. Comparative characterization of a wild type and transmembrane domain-deleted fatty acid amide hydrolase: identification of the transmembrane domain as a site for oligomerization. Biochemistry. 37:1998;15177-15187.
    • (1998) Biochemistry , vol.37 , pp. 15177-15187
    • Patricelli, M.P.1    Lashuel, H.A.2    Giang, D.K.3    Kelly, J.W.4    Cravatt, B.F.5
  • 18
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. 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
  • 19
    • 0023684064 scopus 로고
    • A general method of in vitro preparation and specific mutagenesis of DNA fragments: Study of protein and DNA interactions
    • Higuchi R., Krummel B., Saiki R.K. A general method of in vitro preparation and specific mutagenesis of DNA fragments: study of protein and DNA interactions. Nucleic Acids Res. 16:1988;7351-7367.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 7351-7367
    • Higuchi, R.1    Krummel, B.2    Saiki, R.K.3
  • 21
    • 0032476070 scopus 로고    scopus 로고
    • Fatty acid amide hydrolase is located preferentially in large neurons in the rat central nervous system as revealed by immunohistochemistry
    • Tsou K., Nogueron M.I., Muthian S., Sanudo-Pena M.C., Hillard C.J., Deutsch D.G., Walker J.M. Fatty acid amide hydrolase is located preferentially in large neurons in the rat central nervous system as revealed by immunohistochemistry. Neurosci. Lett. 254:1998;137-140.
    • (1998) Neurosci. Lett. , vol.254 , pp. 137-140
    • Tsou, K.1    Nogueron, M.I.2    Muthian, S.3    Sanudo-Pena, M.C.4    Hillard, C.J.5    Deutsch, D.G.6    Walker, J.M.7
  • 22
    • 0032494704 scopus 로고    scopus 로고
    • A new perspective on cannabinoid signalling: Complementary localization of fatty acid amide hydrolase and the CB1 receptor in rat brain
    • Egertova M., Giang D.K., Cravatt B.F., Elphick M.R. A new perspective on cannabinoid signalling: complementary localization of fatty acid amide hydrolase and the CB1 receptor in rat brain. Proc. R. Soc. Lond. B. 265:1998;2081-2085.
    • (1998) Proc. R. Soc. Lond. B. , vol.265 , pp. 2081-2085
    • Egertova, M.1    Giang, D.K.2    Cravatt, B.F.3    Elphick, M.R.4
  • 24
    • 0030870722 scopus 로고    scopus 로고
    • A second endogenous cannabinoid that modulates long-term potentiation
    • Stella N., Schweitzer P., Piomelli D. A second endogenous cannabinoid that modulates long-term potentiation. Nature. 388:1997;773-778.
    • (1997) Nature , vol.388 , pp. 773-778
    • Stella, N.1    Schweitzer, P.2    Piomelli, D.3
  • 25
    • 0030700490 scopus 로고    scopus 로고
    • Identification of active sites in amidase: Evolutionary relationship between amide bond- And peptide bond-cleaving enzymes
    • Kobayashi M., Fujiwara Y., Goda M., Komeda H., Shimizu S. Identification of active sites in amidase: evolutionary relationship between amide bond- and peptide bond-cleaving enzymes. Proc. Natl. Acad. Sci. USA. 94:1997;11986-11991.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 11986-11991
    • Kobayashi, M.1    Fujiwara, Y.2    Goda, M.3    Komeda, H.4    Shimizu, S.5
  • 26
    • 0342362262 scopus 로고    scopus 로고
    • Identification of residues involved in fatty acid amide hydrolase catalytic activity
    • International Cannabinoid Research Society, Burlington, Vermont
    • R. Omeir, B. Cravatt, D.G. Deutsch, Identification of residues involved in fatty acid amide hydrolase catalytic activity, in: 1998 Symposium on the Cannabinoids, International Cannabinoid Research Society, Burlington, Vermont, 1998, p. 15.
    • (1998) In: 1998 Symposium on the Cannabinoids , pp. 15
    • Omeir, R.1    Cravatt, B.2    Deutsch, D.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.