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Volumn 18, Issue 3, 2005, Pages 214-219

An oxygen transporter hemocyanin can act on the late pathway of melanin synthesis

Author keywords

5,6 dihydroxyindole; 5,6 dihydroxyindole 2 carboxylic acid; Crustacean; Hemocyanin; Hemolymph; Melanin; Phenoloxidase

Indexed keywords

5,6 DIHYDROXYINDOLE; 5,6 DIHYDROXYINDOLE 2 CARBOXYLIC ACID; CARBOXYLIC ACID DERIVATIVE; DOPA; DOPAQUINONE; EUMELANIN; HEMOCYANIN; INDOLE DERIVATIVE; MELANIN; MONOPHENOL MONOOXYGENASE; OXYGENASE INHIBITOR; PIGMENT; PLASMA PROTEIN; POLYMER; QUINONE DERIVATIVE; TYROSINE; UNCLASSIFIED DRUG;

EID: 19544389349     PISSN: 08935785     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1600-0749.2005.00232.x     Document Type: Article
Times cited : (33)

References (29)
  • 1
    • 0035658416 scopus 로고    scopus 로고
    • Hemocyanin a most likely inducer of black spots in kuruma prawn Penaeus japonicus during storage
    • Adachi, K., Hirata, T., Nagai, K., and Sakaguchi, M. (2001). Hemocyanin a most likely inducer of black spots in kuruma prawn Penaeus japonicus during storage. J. Food Sci. 66, 1130-1136.
    • (2001) J. Food Sci. , vol.66 , pp. 1130-1136
    • Adachi, K.1    Hirata, T.2    Nagai, K.3    Sakaguchi, M.4
  • 3
    • 0037394528 scopus 로고    scopus 로고
    • A 160 kDa protein is essential for hemocyanin derived melanosis of prawn
    • Adachi, K., Hirata, T., Fujio, A., Nishioka, T., and Sakaguchi, M. (2003b). A 160 kDa protein is essential for hemocyanin derived melanosis of prawn. J. Food Sci, 68, 765-769.
    • (2003) J. Food Sci. , vol.68 , pp. 765-769
    • Adachi, K.1    Hirata, T.2    Fujio, A.3    Nishioka, T.4    Sakaguchi, M.5
  • 4
    • 0025003784 scopus 로고
    • Regulation of mammalian melanogenesis I: Partial purification and characterization of a dopachrome conversion factor: Dopachrome tautomerase
    • Aroca, P., Garcia-Borron, J. C., Solano, F., and Lozano, J. C. (1990). Regulation of mammalian melanogenesis I: partial purification and characterization of a dopachrome conversion factor: dopachrome tautomerase. Biochim. Biophys. Acta 1032, 266-275.
    • (1990) Biochim. Biophys. Acta , vol.1032 , pp. 266-275
    • Aroca, P.1    Garcia-Borron, J.C.2    Solano, F.3    Lozano, J.C.4
  • 5
    • 0000926038 scopus 로고    scopus 로고
    • Recent advances in research on the insect prophenoloxidase cascade
    • P.T. Brey, and D, Hultmark, ed. (London, UK: Chapman and Hall)
    • Ashida, M., and Brey, P.T. (1997). Recent advances in research on the insect prophenoloxidase cascade. In Molecular Mechanism of Immune Responses in Insects, P.T. Brey, and D, Hultmark, ed. (London, UK: Chapman and Hall), pp. 135-172.
    • (1997) Molecular Mechanism of Immune Responses in Insects , pp. 135-172
    • Ashida, M.1    Brey, P.T.2
  • 6
    • 0032212515 scopus 로고    scopus 로고
    • Cooperation of dopachrome conversion factor with phenoloxidase in the eumelanin pathway in haemolymph of Locusta migratoria (Insecta)
    • Cherqui, A., Duvic, B., Reibel, C., and Brehelm, M. (1998). Cooperation of dopachrome conversion factor with phenoloxidase in the eumelanin pathway in haemolymph of Locusta migratoria (Insecta). Insect Biochem. Mol. Biol. 28, 839-848.
    • (1998) Insect Biochem. Mol. Biol. , vol.28 , pp. 839-848
    • Cherqui, A.1    Duvic, B.2    Reibel, C.3    Brehelm, M.4
  • 7
    • 78651153791 scopus 로고
    • Disk electrophoresis II: Method and application to human serum proteins
    • Davis, B. J. (1964). Disk electrophoresis II: Method and application to human serum proteins. Ann. N. Y. Acad. Sci. 121, 404-427.
    • (1964) Ann. N. Y. Acad. Sci. , vol.121 , pp. 404-427
    • Davis, B.J.1
  • 8
    • 0035947641 scopus 로고    scopus 로고
    • SDS-induced phenoloxidase activity of hemocyanins from Limulus polyphemus, Eurypelma californicum, and Cancer magister
    • Decker, H., Ryan, M., Jaenicke, E., and Terwilliger, N. (2001). SDS-induced phenoloxidase activity of hemocyanins from Limulus polyphemus, Eurypelma californicum, and Cancer magister. J. Biol. Chem. 276, 17796-17799.
    • (2001) J. Biol. Chem. , vol.276 , pp. 17796-17799
    • Decker, H.1    Ryan, M.2    Jaenicke, E.3    Terwilliger, N.4
  • 9
    • 0035861645 scopus 로고    scopus 로고
    • Crustacean Immunity. Antifungal peptides are generated from the c terminus of shrimp hemocyanin in response to microbial challenge
    • Destoumieux-Garzon, D., Saulnier, D., Garnier, J., Jouffrey, C., Bulet, P., and Bachere, E. (2001). Crustacean Immunity. Antifungal peptides are generated from the c terminus of shrimp hemocyanin in response to microbial challenge. J. Biol. Chem. 276, 47070-47077.
    • (2001) J. Biol. Chem. , vol.276 , pp. 47070-47077
    • Destoumieux-Garzon, D.1    Saulnier, D.2    Garnier, J.3    Jouffrey, C.4    Bulet, P.5    Bachere, E.6
  • 10
    • 0036293855 scopus 로고    scopus 로고
    • Functional expression and characterization of Aedes aegypti dopachrome conversion enzyme
    • Fang, J., Man, Q., Johnson, J. K., Christensen, B. M., and Li, J. (2002). Functional expression and characterization of Aedes aegypti dopachrome conversion enzyme. Biochem. Biophys. Res. Commun. 290, 287-293.
    • (2002) Biochem. Biophys. Res. Commun. , vol.290 , pp. 287-293
    • Fang, J.1    Man, Q.2    Johnson, J.K.3    Christensen, B.M.4    Li, J.5
  • 12
    • 0040320331 scopus 로고    scopus 로고
    • Spider hemocyanin binds ecdysone and 20-OH-ecdysone
    • Jaenicke, E., Foll, R., and Decker, H. (1999). Spider hemocyanin binds ecdysone and 20-OH-ecdysone. J. Biol. Chem. 274, 34267-34271.
    • (1999) J. Biol. Chem. , vol.274 , pp. 34267-34271
    • Jaenicke, E.1    Foll, R.2    Decker, H.3
  • 14
    • 0019945365 scopus 로고
    • Mammalian tyrosinase catalyzes three reactions in the biosynthesis of melanin
    • Korner, A., and Pawelek, J. (1982). Mammalian tyrosinase catalyzes three reactions in the biosynthesis of melanin. Science 217, 1163-1165.
    • (1982) Science , vol.217 , pp. 1163-1165
    • Korner, A.1    Pawelek, J.2
  • 17
    • 0005401151 scopus 로고    scopus 로고
    • The physiological significance of respiratory proteins in invertebrates
    • Paul, R. J., and Pirow, R. (1998). The physiological significance of respiratory proteins in invertebrates. Zoology 100, 319-327.
    • (1998) Zoology , vol.100 , pp. 319-327
    • Paul, R.J.1    Pirow, R.2
  • 18
    • 0025100758 scopus 로고
    • Dopachrome conversion factor functions as an isomerase
    • Pawelek, J. (1990), Dopachrome conversion factor functions as an isomerase. Biochem. Biophys. Res, Commun. 166, 1328-1333.
    • (1990) Biochem. Biophys. Res, Commun. , vol.166 , pp. 1328-1333
    • Pawelek, J.1
  • 20
    • 0033173388 scopus 로고    scopus 로고
    • Relationship between tyrosinase inhibitory action and oxidation-reduction potential of cosmetic whitening ingredients and phenol derivatives
    • Sakuma, K., Ogawa, M., Sugibayashi, K., Yamada, K., and Yamamoto, K. (1999). Relationship between tyrosinase inhibitory action and oxidation-reduction potential of cosmetic whitening ingredients and phenol derivatives. Arch. Pharm. Res. 22, 335-339.
    • (1999) Arch. Pharm. Res. , vol.22 , pp. 335-339
    • Sakuma, K.1    Ogawa, M.2    Sugibayashi, K.3    Yamada, K.4    Yamamoto, K.5
  • 21
    • 0002749939 scopus 로고    scopus 로고
    • The prophenoloxidase activating system in invertebrates
    • K. Söderhäll, S. Iwanaga, and G.R. Vasata, ed. (Fair Heaven, NJ: SOS Publications)
    • Söderhäll, K., Cerenius, L., and Johansson, M.W. (1996). The prophenoloxidase activating system in invertebrates. In New Directions in Invertebrates Immunology, K. Söderhäll, S. Iwanaga, and G.R. Vasata, ed. (Fair Heaven, NJ: SOS Publications), pp. 229-254.
    • (1996) New Directions in Invertebrates Immunology , pp. 229-254
    • Söderhäll, K.1    Cerenius, L.2    Johansson, M.W.3
  • 22
    • 0002723111 scopus 로고    scopus 로고
    • Roles of the insect cuticle in host defense reactions
    • K. Söderhäll, S. Iwanaga, and G.R. Vasata, ed. (Fair Heaven, NJ: SOS Publications)
    • Sugumaran, M. (1996). Roles of the insect cuticle in host defense reactions. In New Directions in Invertebrates Immunology, K. Söderhäll, S. Iwanaga, and G.R. Vasata, ed. (Fair Heaven, NJ: SOS Publications), pp. 355-374.
    • (1996) New Directions in Invertebrates Immunology , pp. 355-374
    • Sugumaran, M.1
  • 23
    • 0035999729 scopus 로고    scopus 로고
    • Comparative biochemistry of eumelanogenesis and the protective roles of phenoloxidase and melanin in insect
    • Sugumaran, M. (2002). Comparative Biochemistry of Eumelanogenesis and the protective roles of phenoloxidase and melanin in insect. Pigment Cell Res. 15, 2-9.
    • (2002) Pigment Cell Res. , vol.15 , pp. 2-9
    • Sugumaran, M.1
  • 24
    • 0025764070 scopus 로고
    • Quinone methide as a new intermediate in eumelanin biosynthesis
    • Sugumaran, M., and Semensi, V. (1991). Quinone methide as a new intermediate in eumelanin biosynthesis. J. Biol. Chem. 266, 6073-6078.
    • (1991) J. Biol. Chem. , vol.266 , pp. 6073-6078
    • Sugumaran, M.1    Semensi, V.2
  • 25
    • 0033113298 scopus 로고    scopus 로고
    • Insect melanogenesis II. Inability of Manduca phenoloxidase to act on 5,6-dihydroxyindole-2-carboxylic acid
    • Sugumaran, M., Duggaraju, R., Generozova, F., and Ito, S. (1999). Insect melanogenesis II. Inability of Manduca phenoloxidase to act on 5,6-dihydroxyindole-2-carboxylic acid. Pigment Cell Res. 12, 118-125.
    • (1999) Pigment Cell Res. , vol.12 , pp. 118-125
    • Sugumaran, M.1    Duggaraju, R.2    Generozova, F.3    Ito, S.4
  • 26
    • 0026788345 scopus 로고
    • 5,6-Dihydroxyindole-2-carboxylic acid is incorporated in mammalian melanin
    • Tsukamoto, K., Palumbo, A., D'Ischia, M., Hearing, V. J., and Prota, G. (1992). 5,6-Dihydroxyindole-2-carboxylic acid is incorporated in mammalian melanin. Biochem. J. 286, 491-495.
    • (1992) Biochem. J. , vol.286 , pp. 491-495
    • Tsukamoto, K.1    Palumbo, A.2    D'Ischia, M.3    Hearing, V.J.4    Prota, G.5
  • 28
    • 0023891919 scopus 로고
    • Preparation of eumelanin-related metabolites 5,6-dihydroxyindole, 5,6-dihydroxyindole-2-carboxylic acid, and their O-methyl derivatives
    • Wakamatsu, K., and Ito, S. (1988). Preparation of eumelanin-related metabolites 5,6-dihydroxyindole, 5,6-dihydroxyindole-2-carboxylic acid, and their O-methyl derivatives. Anal. Biochem. 170, 335-340
    • (1988) Anal. Biochem. , vol.170 , pp. 335-340
    • Wakamatsu, K.1    Ito, S.2
  • 29
    • 0029981365 scopus 로고    scopus 로고
    • The o-diphenol oxidase activity of arthropod hemocyanin
    • Zlateva, T., Di Muro, P., Salvato, B., and Beltramini, M. (1996). The o-diphenol oxidase activity of arthropod hemocyanin. FEBS Lett. 384, 251-254.
    • (1996) FEBS Lett. , vol.384 , pp. 251-254
    • Zlateva, T.1    Di Muro, P.2    Salvato, B.3    Beltramini, M.4


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