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Volumn 28, Issue 12, 1998, Pages 959-967

Two major proteins from locust plasma are involved in coagulation and are specifically precipitated by laminarin, a β-1,3-glucan

Author keywords

1,3 glucan; Coagulation; Insect immunity; Locusta migratoria; Prophenoloxidase

Indexed keywords

BETA 1,3 GLUCAN; BETA-1,3-GLUCAN; GLUCAN; GLYCOSIDASE; INSECT PROTEIN; LAMINARAN; POLYSACCHARIDE; PROTEIN;

EID: 0032407614     PISSN: 09651748     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0965-1748(98)00084-8     Document Type: Article
Times cited : (28)

References (29)
  • 1
    • 0014149056 scopus 로고
    • Activation of pre-phenoloxidase in hemolymph of the silkworm, Bombyx mori
    • Ashida M., Ohnishi E. Activation of pre-phenoloxidase in hemolymph of the silkworm, Bombyx mori. Archiv. Biochem. Biophys. 122:1967;411-416.
    • (1967) Archiv. Biochem. Biophys. , vol.122 , pp. 411-416
    • Ashida, M.1    Ohnishi, E.2
  • 2
    • 0025950120 scopus 로고
    • The ß-1,3-glucan-binding protein from the crayfish Pacifastacus leniusculus, when reacted with a ß-1,3-glucan, induces spreading and degranulation of crayfish granular cells
    • Barracco A.M., Duvic B., Söderhäll K. The ß-1,3-glucan-binding protein from the crayfish Pacifastacus leniusculus, when reacted with a ß-1,3-glucan, induces spreading and degranulation of crayfish granular cells. Cell Tiss. Res. 266:1991;491-497.
    • (1991) Cell Tiss. Res. , vol.266 , pp. 491-497
    • Barracco, A.M.1    Duvic, B.2    Söderhäll, K.3
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M. A rapid and sensitive method for the quantification 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.1
  • 5
    • 0018425410 scopus 로고
    • Hemolymph coagulation in L. migratoria: Evidence for a functional equivalent of fibrinogen
    • Brehélin M. Hemolymph coagulation in L. migratoria: evidence for a functional equivalent of fibrinogen. Comp. Biochem. Physiol. 62B:1979;329-334.
    • (1979) Comp. Biochem. Physiol. , vol.62 , pp. 329-334
    • Brehélin, M.1
  • 6
    • 0026053073 scopus 로고
    • Purification of a protease inhibitor which controls prophenoloxidase activation in hemolymph of Locusta migratoria (Insecta)
    • Brehélin M., Boigegrain R.A., Drif L., Coletti-Previero M.A. Purification of a protease inhibitor which controls prophenoloxidase activation in hemolymph of Locusta migratoria (Insecta). Biochem. Biophys. Res. Commun. 179:1991;841-846.
    • (1991) Biochem. Biophys. Res. Commun. , vol.179 , pp. 841-846
    • Brehélin, M.1    Boigegrain, R.A.2    Drif, L.3    Coletti-Previero, M.A.4
  • 7
    • 45349109674 scopus 로고
    • Insect haemolymph: Cooperation between humoral and cellular factors in Locusta migratoria
    • Brehélin M., Drif L., Baud L., Boemare N. Insect haemolymph: cooperation between humoral and cellular factors in Locusta migratoria. Insect Biochem. 19:1989;301-307.
    • (1989) Insect Biochem. , vol.19 , pp. 301-307
    • Brehélin, M.1    Drif, L.2    Baud, L.3    Boemare, N.4
  • 9
    • 0001390691 scopus 로고
    • Lipid transport: Biochemistry of hemolymph lipophorin
    • In: Kerkurt, G.A., Gilbert, L.I. (Eds.), Pergamon Press, Oxford
    • Chino, H., 1985. Lipid transport: biochemistry of hemolymph lipophorin. In: Kerkurt, G.A., Gilbert, L.I. (Eds.), Insect Physiology, Biochemistry and Pharmacology. Pergamon Press, Oxford, pp. 115-135.
    • (1985) Insect Physiology, Biochemistry and Pharmacology , pp. 115-135
    • Chino, H.1
  • 10
    • 0019616108 scopus 로고
    • Diacylglycerol-carrying lipoprotein of hemolymph of the locust and some insects
    • Chino H., Kitazawa K. Diacylglycerol-carrying lipoprotein of hemolymph of the locust and some insects. J. Lipid Res. 22:1981;1042-1052.
    • (1981) J. Lipid Res. , vol.22 , pp. 1042-1052
    • Chino, H.1    Kitazawa, K.2
  • 11
    • 0000527403 scopus 로고
    • Lipophorin inhibits the adhesion of cockroach (Periplaneta americana) haemocytes in vitro
    • Coodin S., Caveney S. Lipophorin inhibits the adhesion of cockroach (Periplaneta americana) haemocytes in vitro. J. Insect Physiol. 38:1992;853-862.
    • (1992) J. Insect Physiol. , vol.38 , pp. 853-862
    • Coodin, S.1    Caveney, S.2
  • 12
    • 84990467464 scopus 로고
    • Molecular characteristics of lipophorin, the juvenile hormone binding protein in hemolymph of the Colorado potato beetle, Leptinotarsa decemlineata
    • De Kort C.A.D., Koopmanschap A.B. Molecular characteristics of lipophorin, the juvenile hormone binding protein in hemolymph of the Colorado potato beetle, Leptinotarsa decemlineata. Archiv. Insect Biochem. Physiol. 5:1987;255-259.
    • (1987) Archiv. Insect Biochem. Physiol. , vol.5 , pp. 255-259
    • De Kort, C.A.D.1    Koopmanschap, A.B.2
  • 13
    • 0025351924 scopus 로고
    • Purification and characterization of a ß-1,3-glucan binding protein from the plasma of the crayfish Pacifastacus leniusculus
    • Duvic B., Söderhäll K. Purification and characterization of a ß-1,3-glucan binding protein from the plasma of the crayfish Pacifastacus leniusculus. J. Biol. Chem. 265:1990;9327-9332.
    • (1990) J. Biol. Chem. , vol.265 , pp. 9327-9332
    • Duvic, B.1    Söderhäll, K.2
  • 14
    • 0026780529 scopus 로고
    • Purification and partial characterization of a ß-1,3-glucan-binding-protein membrane receptor from blood cells of the crayfish Pacifastacus leniusculus
    • Duvic B., Söderhäll K. Purification and partial characterization of a ß-1,3-glucan-binding-protein membrane receptor from blood cells of the crayfish Pacifastacus leniusculus. Eur. J. Biochem. 207:1992;223-228.
    • (1992) Eur. J. Biochem. , vol.207 , pp. 223-228
    • Duvic, B.1    Söderhäll, K.2
  • 15
    • 0000931098 scopus 로고
    • ß-1,3-glucan binding proteins from plasma of the crayfish Astacus astacus and Procambarus clarkii
    • Duvic B., Söderhäll K. ß-1,3-glucan binding proteins from plasma of the crayfish Astacus astacus and Procambarus clarkii. J. Crustacean Biol. 13:1993;403-408.
    • (1993) J. Crustacean Biol. , vol.13 , pp. 403-408
    • Duvic, B.1    Söderhäll, K.2
  • 16
    • 0014064044 scopus 로고
    • Automated equipment for sequence determinations
    • Edman P., Begg G. Automated equipment for sequence determinations. Eur. J. Biochem. 1:1967;80-91.
    • (1967) Eur. J. Biochem. , vol.1 , pp. 80-91
    • Edman, P.1    Begg, G.2
  • 17
    • 0020674063 scopus 로고
    • Lipophorin as the plasma coagulogen in Locusta migratoria
    • Gellissen G. Lipophorin as the plasma coagulogen in Locusta migratoria. Naturwissenschaften. 70:1983;45-46.
    • (1983) Naturwissenschaften , vol.70 , pp. 45-46
    • Gellissen, G.1
  • 18
    • 0002646346 scopus 로고
    • Purification and properties of a diglyceride-binding lipoprotein (LPI) of the hemolymph of adult male Locusta migratoria
    • Gellissen G., Emmerich H. Purification and properties of a diglyceride-binding lipoprotein (LPI) of the hemolymph of adult male Locusta migratoria. J. Comp. Physiol. 136B:1980;1-9.
    • (1980) J. Comp. Physiol. , vol.136 , pp. 1-9
    • Gellissen, G.1    Emmerich, H.2
  • 19
    • 0028839529 scopus 로고
    • Identification of the major lipoproteins in crayfish hemolymph as proteins involved in immune recognition and clotting
    • Hall M., van Heusden M.C., Söderhäll K. Identification of the major lipoproteins in crayfish hemolymph as proteins involved in immune recognition and clotting. Biochem. Biophys. Res. Commun. 216:1995;939-946.
    • (1995) Biochem. Biophys. Res. Commun. , vol.216 , pp. 939-946
    • Hall, M.1    Van Heusden, M.C.2    Söderhäll, K.3
  • 20
    • 0026495346 scopus 로고
    • Treatment of low density lipoprotein with lipoprotein lipase: Diacylglycerol content has no effect on dissociation of apolipophorin III from low-density lipophorin
    • Hiraoka T., Katagiri C. Treatment of low density lipoprotein with lipoprotein lipase: diacylglycerol content has no effect on dissociation of apolipophorin III from low-density lipophorin. J. Biochem. 112:1992;689-693.
    • (1992) J. Biochem. , vol.112 , pp. 689-693
    • Hiraoka, T.1    Katagiri, C.2
  • 22
    • 0029687285 scopus 로고    scopus 로고
    • The prophenoloxidase activating system and associated proteins in invertebrates
    • In: Rinkevich, B., Müller, W.E.G. (Eds.), Springer, Berlin
    • Johansson, M.W., Söderhäll, K., 1996. The prophenoloxidase activating system and associated proteins in invertebrates. In: Rinkevich, B., Müller, W.E.G. (Eds.), Invertebrate Immunology. Springer, Berlin, pp. 46-66.
    • (1996) Invertebrate Immunology , pp. 46-66
    • Johansson, M.W.1    Söderhäll, K.2
  • 23
    • 0028010474 scopus 로고
    • Clearance of lipopolysaccharide in hemolymph of the silkworm bombyx mori: Its role in the termination of cecropin mRNA induction
    • Kato Y., Motoi Y., Taniai K., Kadonookuda K., Hiramatsu M., Yamakawa M. Clearance of lipopolysaccharide in hemolymph of the silkworm bombyx mori: its role in the termination of cecropin mRNA induction. Insect. Biochem. Molec. Biol. 24:1994;539-545.
    • (1994) Insect. Biochem. Molec. Biol. , vol.24 , pp. 539-545
    • Kato, Y.1    Motoi, Y.2    Taniai, K.3    Kadonookuda, K.4    Hiramatsu, M.5    Yamakawa, M.6
  • 24
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 277:1970;680-685.
    • (1970) Nature , vol.277 , pp. 680-685
    • Laemmli, U.K.1
  • 25
    • 0029692452 scopus 로고    scopus 로고
    • Clotting and immune defense in Limulidae
    • In: Rinkevich, B., Müller, W.E.G. (Eds.), Springer, Berlin
    • Muta, T., Iwanaga, S., 1996. Clotting and immune defense in Limulidae. In: Rinkevich, B., Müller, W.E.G. (Eds.), Invertebrate Immunology. Springer, Berlin, pp. 154-189.
    • (1996) Invertebrate Immunology , pp. 154-189
    • Muta, T.1    Iwanaga, S.2
  • 26
    • 0024297132 scopus 로고
    • Purification of a ß-1,3-glucan recognition protein in the prophenoloxidase activating system from hemolymph of the silkworm, Bombyx mori
    • Ochiai M., Ashida M. Purification of a ß-1,3-glucan recognition protein in the prophenoloxidase activating system from hemolymph of the silkworm, Bombyx mori. J. Biol. Chem. 263:1988;12056-12062.
    • (1988) J. Biol. Chem. , vol.263 , pp. 12056-12062
    • Ochiai, M.1    Ashida, M.2
  • 27
    • 0002821345 scopus 로고
    • Lipopolysaccharide-induced activation of prophenoloxidase activating system in crayfish haemocyte lysate
    • Söderhäll K., Häll L. Lipopolysaccharide-induced activation of prophenoloxidase activating system in crayfish haemocyte lysate. Biochim. Biophys. Acta. 797:1984;99-104.
    • (1984) Biochim. Biophys. Acta , vol.797 , pp. 99-104
    • Söderhäll, K.1    Häll, L.2
  • 28
    • 33746992088 scopus 로고
    • The properties and purification of a Blaberus craniifer plasma protein which enhances the activation of haemocyte prophenoloxidase by a beta-1,3-glucan
    • Söderhäll K., Rögener W., Söderhäll I., Newton R., Ratcliffe N.A. The properties and purification of a Blaberus craniifer plasma protein which enhances the activation of haemocyte prophenoloxidase by a beta-1,3-glucan. Insect Biochem. 18:1988;323-330.
    • (1988) Insect Biochem. , vol.18 , pp. 323-330
    • Söderhäll, K.1    Rögener, W.2    Söderhäll, I.3    Newton, R.4    Ratcliffe, N.A.5
  • 29
    • 0028347392 scopus 로고
    • Opsonic activity of cell adhesion proteins and ß-1,3-Glucan binding proteins from two crustaceans
    • Thörnqvist P.O., Johansson M.W., Söderhäll K. Opsonic activity of cell adhesion proteins and ß-1,3-Glucan binding proteins from two crustaceans. Dev. Comp. Immunol. 18:1994;3-12.
    • (1994) Dev. Comp. Immunol. , vol.18 , pp. 3-12
    • Thörnqvist, P.O.1    Johansson, M.W.2    Söderhäll, K.3


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