메뉴 건너뛰기




Volumn 155, Issue 3, 2010, Pages 266-271

Molecular characteristics of a single and novel form of carp (Cyprinus carpio) monoamine oxidase

Author keywords

Amino acid sequence; Carp (Cyprinus carpio); Monoamine oxidase (MAO); Non A MAO; Non B MAO; Novel form; Nucleotide sequence; Single form

Indexed keywords

AMINE OXIDASE (FLAVIN CONTAINING) ISOENZYME A; AMINE OXIDASE (FLAVIN CONTAINING) ISOENZYME B; COMPLEMENTARY DNA;

EID: 74649087329     PISSN: 10964959     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbpb.2009.11.010     Document Type: Article
Times cited : (3)

References (32)
  • 2
    • 48149111146 scopus 로고    scopus 로고
    • Zebrafish: an emerging technology for in vivo pharmacological assessment to identify potential safety liabilities in early drug discovery
    • Barros T.P., Alderton W.K., Reynolds H.M., Roach A.G., and Berghams S. Zebrafish: an emerging technology for in vivo pharmacological assessment to identify potential safety liabilities in early drug discovery. Br. J. Pharmacol. 154 (2008) 1400-1413
    • (2008) Br. J. Pharmacol. , vol.154 , pp. 1400-1413
    • Barros, T.P.1    Alderton, W.K.2    Reynolds, H.M.3    Roach, A.G.4    Berghams, S.5
  • 3
    • 0036140732 scopus 로고    scopus 로고
    • Structure of human monoamine oxidase B, a drug target for treatment of neurological disorders
    • Binda C., Newto-Vinson P., Hubalek F., Edmondson D.E., and Mattevi A. Structure of human monoamine oxidase B, a drug target for treatment of neurological disorders. Nat. Struct. Biol. 9 (2002) 22-26
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 22-26
    • Binda, C.1    Newto-Vinson, P.2    Hubalek, F.3    Edmondson, D.E.4    Mattevi, A.5
  • 4
    • 0018817743 scopus 로고
    • Molecular weight differences between human platelet and placental monoamine oxidase
    • Brown G.K., Powell J.F., and Craig I.W. Molecular weight differences between human platelet and placental monoamine oxidase. Biochem. Pharmacol. 29 (1980) 2595-2603
    • (1980) Biochem. Pharmacol. , vol.29 , pp. 2595-2603
    • Brown, G.K.1    Powell, J.F.2    Craig, I.W.3
  • 5
    • 0018703071 scopus 로고
    • Differences in A and B forms of monoamine oxidase revealed by limited proteolysis and peptide mapping
    • Cawthon R.M., and Breakefield X.O. Differences in A and B forms of monoamine oxidase revealed by limited proteolysis and peptide mapping. Nature 281 (1979) 692-694
    • (1979) Nature , vol.281 , pp. 692-694
    • Cawthon, R.M.1    Breakefield, X.O.2
  • 6
    • 0028559727 scopus 로고
    • Cloning of a novel monoamine oxidase cDNA from trout liver
    • Chen K., Wu H.F., Grimsby J., and Shih J.C. Cloning of a novel monoamine oxidase cDNA from trout liver. Mol. Pharmacol. 46 (1994) 1226-1233
    • (1994) Mol. Pharmacol. , vol.46 , pp. 1226-1233
    • Chen, K.1    Wu, H.F.2    Grimsby, J.3    Shih, J.C.4
  • 7
    • 0030027537 scopus 로고    scopus 로고
    • Influence of C terminus on monoamine oxidase A and B catalytic activity
    • Chen K., Wu H.F., and Shih J.C. Influence of C terminus on monoamine oxidase A and B catalytic activity. J. Neurochem. 66 (1996) 797-803
    • (1996) J. Neurochem. , vol.66 , pp. 797-803
    • Chen, K.1    Wu, H.F.2    Shih, J.C.3
  • 8
    • 0020374186 scopus 로고
    • Selective inhibitors of monoamine oxidase types A and B and their clinical usefulness
    • Fowler C.J. Selective inhibitors of monoamine oxidase types A and B and their clinical usefulness. Drugs Future 2 (1982) 501-507
    • (1982) Drugs Future , vol.2 , pp. 501-507
    • Fowler, C.J.1
  • 9
    • 0033624499 scopus 로고    scopus 로고
    • Phe (208) and Ile (199) in human monoamine oxidase A and B do not determine substrate and inhibitor specificities as in rat
    • Geha R.M., Chen K., and Shih J.C. Phe (208) and Ile (199) in human monoamine oxidase A and B do not determine substrate and inhibitor specificities as in rat. J. Neurochem. 75 (2000) 1304-1309
    • (2000) J. Neurochem. , vol.75 , pp. 1304-1309
    • Geha, R.M.1    Chen, K.2    Shih, J.C.3
  • 10
    • 0030071754 scopus 로고    scopus 로고
    • Identification of a region important for human monoamine oxidase B substrate and inhibitor selectivity
    • Grimsby J., Zenter M., and Shih J.C. Identification of a region important for human monoamine oxidase B substrate and inhibitor selectivity. Life Sci. 58 (1996) 777-787
    • (1996) Life Sci. , vol.58 , pp. 777-787
    • Grimsby, J.1    Zenter, M.2    Shih, J.C.3
  • 11
    • 0019949917 scopus 로고
    • Effects of inhibitors on monoamine oxidase activity in perch (Perca flavescens) brain in vitro
    • Hall T.R., Olcese J.M., Figueroa H.R., and de Valming V.L. Effects of inhibitors on monoamine oxidase activity in perch (Perca flavescens) brain in vitro. Comp. Biochem. Physiol., Part C 71 (1982) 141-144
    • (1982) Comp. Biochem. Physiol., Part C , vol.71 , pp. 141-144
    • Hall, T.R.1    Olcese, J.M.2    Figueroa, H.R.3    de Valming, V.L.4
  • 13
    • 0022507437 scopus 로고
    • Brain dialysis: in vivo metabolism of dopamine and serotonin by monoamine oxidase A but not B in the striatum of unrestrained rats
    • Kato T., Dong B., Ishii K., and Kinemuchi H. Brain dialysis: in vivo metabolism of dopamine and serotonin by monoamine oxidase A but not B in the striatum of unrestrained rats. J. Neurochem. 46 (1986) 1277-1282
    • (1986) J. Neurochem. , vol.46 , pp. 1277-1282
    • Kato, T.1    Dong, B.2    Ishii, K.3    Kinemuchi, H.4
  • 14
    • 0015186769 scopus 로고
    • The covalently-bound flavin of hepatic monoamine oxidase: 1. Isolation and sequence of a flavin peptide and evidence for binding at the 8α position
    • Kearney E.B., Salach J.T., Walker W.H., Seung R.L., Kenney W., Zeslotek E., and Singer T.P. The covalently-bound flavin of hepatic monoamine oxidase: 1. Isolation and sequence of a flavin peptide and evidence for binding at the 8α position. Eur. J. Biochem. 24 (1971) 321-327
    • (1971) Eur. J. Biochem. , vol.24 , pp. 321-327
    • Kearney, E.B.1    Salach, J.T.2    Walker, W.H.3    Seung, R.L.4    Kenney, W.5    Zeslotek, E.6    Singer, T.P.7
  • 15
    • 0020693596 scopus 로고
    • A new type of mitochondrial monoamine oxidase distinct from type-A and type-B
    • Kinemuchi H., Sudo M., Yoshino M., Kawaguchi T., Sunami Y., and Kamijo K. A new type of mitochondrial monoamine oxidase distinct from type-A and type-B. Life Sci. 32 (1983) 517-524
    • (1983) Life Sci. , vol.32 , pp. 517-524
    • Kinemuchi, H.1    Sudo, M.2    Yoshino, M.3    Kawaguchi, T.4    Sunami, Y.5    Kamijo, K.6
  • 17
    • 0020619369 scopus 로고
    • Inhibition of carp liver monoamine oxidase by some commonly-used detergents
    • Kinemuchi H., Sunami Y., Ueda T., Morikawa F., and Kamijo K. Inhibition of carp liver monoamine oxidase by some commonly-used detergents. Jpn. J. Pharmacol. 33 (1983) 1007-1015
    • (1983) Jpn. J. Pharmacol. , vol.33 , pp. 1007-1015
    • Kinemuchi, H.1    Sunami, Y.2    Ueda, T.3    Morikawa, F.4    Kamijo, K.5
  • 18
    • 0025069406 scopus 로고
    • Primary structure of rat monoamine oxidase A deduced from cDNA and its expression in rat tissues
    • Kuwahara T., Takamoto S., and Ito A. Primary structure of rat monoamine oxidase A deduced from cDNA and its expression in rat tissues. Agr. Biol. Chem. 54 (1990) 253-257
    • (1990) Agr. Biol. Chem. , vol.54 , pp. 253-257
    • Kuwahara, T.1    Takamoto, S.2    Ito, A.3
  • 19
    • 0019562512 scopus 로고
    • Identity of the active site flavin-peptide fragments from the human "A"-form and the bovine "B"-form of monoamine oxidase
    • Nagy J., and Salach J.I. Identity of the active site flavin-peptide fragments from the human "A"-form and the bovine "B"-form of monoamine oxidase. Arch. Biochem. Biophys. 208 (1981) 388-394
    • (1981) Arch. Biochem. Biophys. , vol.208 , pp. 388-394
    • Nagy, J.1    Salach, J.I.2
  • 20
    • 0027525536 scopus 로고
    • Targeting of Bcl-2 to the mitochondrial outer membrane by a COOH-terminal signal anchor sequence
    • Nguyen M., Miller D.G., Yong V.W., Korsmeyer S.J., and Shore G.C. Targeting of Bcl-2 to the mitochondrial outer membrane by a COOH-terminal signal anchor sequence. J. Biol. Chem. 268 (1993) 25265-25268
    • (1993) J. Biol. Chem. , vol.268 , pp. 25265-25268
    • Nguyen, M.1    Miller, D.G.2    Yong, V.W.3    Korsmeyer, S.J.4    Shore, G.C.5
  • 21
    • 44949267004 scopus 로고
    • Isoelectric analysis of 3H-pargyline-labelled monoamine oxidase in rat and carp
    • Obata T., Yamanaka Y., Sho S., and Kinemuchi H. Isoelectric analysis of 3H-pargyline-labelled monoamine oxidase in rat and carp. Comp. Biochem. Physiol., Part C 96 (1990) 91-98
    • (1990) Comp. Biochem. Physiol., Part C , vol.96 , pp. 91-98
    • Obata, T.1    Yamanaka, Y.2    Sho, S.3    Kinemuchi, H.4
  • 22
    • 0015762505 scopus 로고
    • Pig liver monoamine oxidase: studies on the subunit structure
    • Oreland L., Kinemuchi H., and Stigbrand T. Pig liver monoamine oxidase: studies on the subunit structure. Arch. Biochem. Biophys. 159 (1973) 854-860
    • (1973) Arch. Biochem. Biophys. , vol.159 , pp. 854-860
    • Oreland, L.1    Kinemuchi, H.2    Stigbrand, T.3
  • 23
    • 0015766368 scopus 로고
    • The mechanism of action of the monoamine oxidase inhibitor pargyline
    • Oreland L., Kinemuchi H., and Yoo B.Y. The mechanism of action of the monoamine oxidase inhibitor pargyline. Life Sci. 13 (1973) 1533-1541
    • (1973) Life Sci. , vol.13 , pp. 1533-1541
    • Oreland, L.1    Kinemuchi, H.2    Yoo, B.Y.3
  • 27
    • 0032914318 scopus 로고    scopus 로고
    • Monoamine oxidase: from genes to behavior
    • Shih J.C., Chen K., and Ridd M.J. Monoamine oxidase: from genes to behavior. Annu. Rev. Neurosci. 22 (1999) 197-217
    • (1999) Annu. Rev. Neurosci. , vol.22 , pp. 197-217
    • Shih, J.C.1    Chen, K.2    Ridd, M.J.3
  • 28
    • 0030974340 scopus 로고    scopus 로고
    • A key amino acid responsible for substrate selectivity of monoamine oxidase A and B
    • Tsugeno Y., and Ito A. A key amino acid responsible for substrate selectivity of monoamine oxidase A and B. J. Biol. Chem. 272 (1997) 14033-14036
    • (1997) J. Biol. Chem. , vol.272 , pp. 14033-14036
    • Tsugeno, Y.1    Ito, A.2
  • 29
    • 0028785562 scopus 로고
    • Regions of the molecule responsible for substrate specificity of monoamine oxidase A and B: a chimeric enzyme analysis
    • Tsugeno Y., Hirashiki L., Ogata F., and Ito A. Regions of the molecule responsible for substrate specificity of monoamine oxidase A and B: a chimeric enzyme analysis. J. Biochem. (Tokyo) 118 (1995) 974-980
    • (1995) J. Biochem. (Tokyo) , vol.118 , pp. 974-980
    • Tsugeno, Y.1    Hirashiki, L.2    Ogata, F.3    Ito, A.4
  • 31
    • 0021250696 scopus 로고
    • Enzymic and molecular characteristics of a new form of monoamine oxidase, distinct from form-A and form-B
    • Yoshino M., Obata T., Sho S., and Kinemuchi H. Enzymic and molecular characteristics of a new form of monoamine oxidase, distinct from form-A and form-B. J. Pharmacol. 35 (1984) 105-115
    • (1984) J. Pharmacol. , vol.35 , pp. 105-115
    • Yoshino, M.1    Obata, T.2    Sho, S.3    Kinemuchi, H.4
  • 32
    • 0027245885 scopus 로고
    • Site-directed mutagenesis of monoamine oxidase A and B: role of cysteines
    • Wu H.F., Chen K., and Shih J.C. Site-directed mutagenesis of monoamine oxidase A and B: role of cysteines. Mol. Pharmacol. 43 (1993) 888-893
    • (1993) Mol. Pharmacol. , vol.43 , pp. 888-893
    • Wu, H.F.1    Chen, K.2    Shih, J.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.