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Volumn 28, Issue 2, 2004, Pages 113-125

Isolation and characterisation of pentraxin-like serum proteins from the common carp Cyprinus carpio

Author keywords

Affinity chromatography; Antibody; C reactive protein (CRP); Common carp; Pentraxin; Sequence

Indexed keywords

C REACTIVE PROTEIN; CALCIUM; FISH PROTEIN; PENTRAXIN; PHOSPHORUS DERIVATIVE; POLYCLONAL ANTIBODY;

EID: 0041326280     PISSN: 0145305X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0145-305X(03)00123-X     Document Type: Article
Times cited : (33)

References (53)
  • 2
    • 0034861477 scopus 로고    scopus 로고
    • The acute phase response and innate immunity of fish
    • Bayne C.J., Gerwick L. The acute phase response and innate immunity of fish. Dev Comp Immunol. 25:2001;725-743.
    • (2001) Dev Comp Immunol , vol.25 , pp. 725-743
    • Bayne, C.J.1    Gerwick, L.2
  • 3
    • 0015010578 scopus 로고
    • Specificity of CRP for choline phosphate residues of pneumococcal C-polysaccharide
    • Volanakis J.E., Kaplan M.H. Specificity of CRP for choline phosphate residues of pneumococcal C-polysaccharide. Proc Soc Exp Biol Med. 136:1971;612-614.
    • (1971) Proc Soc Exp Biol Med , vol.136 , pp. 612-614
    • Volanakis, J.E.1    Kaplan, M.H.2
  • 4
    • 0020332414 scopus 로고
    • Complement activation by C-reactive protein
    • Volanakis J.E. Complement activation by C-reactive protein. Ann NY Acad Sci. 389:1982;235-250.
    • (1982) Ann NY Acad Sci , vol.389 , pp. 235-250
    • Volanakis, J.E.1
  • 7
    • 0022857216 scopus 로고
    • Isolation and characterization of Limulus C-reactive protein genes
    • Nguyen N.Y., Suzuki A., Cheng S.-M., Zon G., Liu T.-Y. Isolation and characterization of Limulus C-reactive protein genes. J Biol Chem. 261:1986;10450-10455.
    • (1986) J Biol Chem , vol.261 , pp. 10450-10455
    • Nguyen, N.Y.1    Suzuki, A.2    Cheng, S.-M.3    Zon, G.4    Liu, T.-Y.5
  • 8
    • 0033199575 scopus 로고    scopus 로고
    • Functional and structural diversity of CRP present in horseshoe crab haemolymph
    • Iwaki D., Osaki T., Mizunoe Y., Wai S.N., Iwanaga S., Kawabata S. Functional and structural diversity of CRP present in horseshoe crab haemolymph. Eur J Biochem. 264:1999;314-326.
    • (1999) Eur J Biochem , vol.264 , pp. 314-326
    • Iwaki, D.1    Osaki, T.2    Mizunoe, Y.3    Wai, S.N.4    Iwanaga, S.5    Kawabata, S.6
  • 9
    • 0033618423 scopus 로고    scopus 로고
    • CRP and SAP-like pentraxins are both present in Limulus haemolymph: Crystal structure of Limulus SAP
    • Shrive A.K., Metcalfe A., Cartwright J., Greenhough T.J. CRP and SAP-like pentraxins are both present in Limulus haemolymph: crystal structure of Limulus SAP. J Mol Biol. 290:1999;997-1008.
    • (1999) J Mol Biol , vol.290 , pp. 997-1008
    • Shrive, A.K.1    Metcalfe, A.2    Cartwright, J.3    Greenhough, T.J.4
  • 10
    • 0036308252 scopus 로고    scopus 로고
    • Complete cDNA sequence of an SAP-like pentraxin from Limulus polyphemus: Implications for pentraxin evolution
    • Tharia H.A., Shrive A.K., Arme C., Mills J.D., Williams G.T., Greenhough T.J. Complete cDNA sequence of an SAP-like pentraxin from Limulus polyphemus: implications for pentraxin evolution. J Mol Biol. 216:2002;583-597.
    • (2002) J Mol Biol , vol.216 , pp. 583-597
    • Tharia, H.A.1    Shrive, A.K.2    Arme, C.3    Mills, J.D.4    Williams, G.T.5    Greenhough, T.J.6
  • 11
    • 0034869253 scopus 로고    scopus 로고
    • Human C-reactive protein: Expression, structure, and function
    • Volanakis J.E. Human C-reactive protein: expression, structure, and function. Mol Immunol. 38:2001;189-197.
    • (2001) Mol Immunol , vol.38 , pp. 189-197
    • Volanakis, J.E.1
  • 12
    • 0018425762 scopus 로고
    • Serum amyloid P-component is an acute-phase reactant in the mouse
    • Pepys M.B., Baltz M., Gomer K., Davies A.J.S., Doenhoff M. Serum amyloid P-component is an acute-phase reactant in the mouse. Nature. 278:1979;259-261.
    • (1979) Nature , vol.278 , pp. 259-261
    • Pepys, M.B.1    Baltz, M.2    Gomer, K.3    Davies, A.J.S.4    Doenhoff, M.5
  • 13
    • 0027364848 scopus 로고
    • Serum amyloid P (female protein) of the Syrian hamster. Gene structure and expression
    • Rudnick C.M., Dowton S.B. Serum amyloid P (female protein) of the Syrian hamster. Gene structure and expression. J Biol Chem. 268:1993;21760-21769.
    • (1993) J Biol Chem , vol.268 , pp. 21760-21769
    • Rudnick, C.M.1    Dowton, S.B.2
  • 14
    • 0031556386 scopus 로고    scopus 로고
    • Harbor seal C-reactive protein: Purification, characterisation of specific monoclonal antibodies and development of an immuno-assay to measure serum C-reactive protein concentrations
    • Funke C., King D.P., Brotheridge R.M., Adelung D., Stott J.L. Harbor seal C-reactive protein: purification, characterisation of specific monoclonal antibodies and development of an immuno-assay to measure serum C-reactive protein concentrations. Vet Immun Immunopath. 59:1997;151-162.
    • (1997) Vet Immun Immunopath , vol.59 , pp. 151-162
    • Funke, C.1    King, D.P.2    Brotheridge, R.M.3    Adelung, D.4    Stott, J.L.5
  • 16
    • 0021111710 scopus 로고
    • Isolation and characterisation of two major serum pentraxins from the dogfish Mustelus canis
    • Robey F.A., Tanaka T., Liu T.-Y. Isolation and characterisation of two major serum pentraxins from the dogfish Mustelus canis. J Biol Chem. 258:1983;2889-2894.
    • (1983) J Biol Chem , vol.258 , pp. 2889-2894
    • Robey, F.A.1    Tanaka, T.2    Liu, T.-Y.3
  • 17
    • 0031812288 scopus 로고    scopus 로고
    • Plasma proteins of rainbow trout (Oncorhynchus mykiss) isolated by binding to lipopolysaccharide from Aeromonas salmonicida
    • Hoover G.J., El-Mowafi A., Simko E., Kocal T.E., Ferguson H.W., Hayes M.A. Plasma proteins of rainbow trout (Oncorhynchus mykiss) isolated by binding to lipopolysaccharide from Aeromonas salmonicida. Comp Biochem Physiol. B120:1998;559-569.
    • (1998) Comp Biochem Physiol , vol.120 , pp. 559-569
    • Hoover, G.J.1    El-Mowafi, A.2    Simko, E.3    Kocal, T.E.4    Ferguson, H.W.5    Hayes, M.A.6
  • 18
    • 0031740244 scopus 로고    scopus 로고
    • Effect of environmental pollutants on the CRP of a freshwater major carp Catla catla
    • Paul I., Mandal C., Mandal C. Effect of environmental pollutants on the CRP of a freshwater major carp Catla catla. Dev Comp Immunol. 22:1998;519-532.
    • (1998) Dev Comp Immunol , vol.22 , pp. 519-532
    • Paul, I.1    Mandal, C.2    Mandal, C.3
  • 19
    • 0000738347 scopus 로고
    • Changes in serum concentrations of channel catfish phosphorylcholine-reactive protein in response to inflammatory agents, low-temperature shock and infection by the fungus Saprolegnia sp
    • Szalai A.J., Bly J.E., Clem L.W. Changes in serum concentrations of channel catfish phosphorylcholine-reactive protein in response to inflammatory agents, low-temperature shock and infection by the fungus Saprolegnia sp. Fish Shellfish Immunol. 4:1994;323-336.
    • (1994) Fish Shellfish Immunol , vol.4 , pp. 323-336
    • Szalai, A.J.1    Bly, J.E.2    Clem, L.W.3
  • 20
    • 0035894557 scopus 로고    scopus 로고
    • Acute phase response of C-reactive protein of Labeo rohita to aquatic pollutants is accompanied by the appearance of distinct molecular forms
    • Sinha S., Mandal C., Allen A.K., Mandal C. Acute phase response of C-reactive protein of Labeo rohita to aquatic pollutants is accompanied by the appearance of distinct molecular forms. Arch Biochem Biophys. 396:2001;139-150.
    • (2001) Arch Biochem Biophys , vol.396 , pp. 139-150
    • Sinha, S.1    Mandal, C.2    Allen, A.K.3    Mandal, C.4
  • 21
    • 0019506750 scopus 로고
    • The effect of inflammatory agents on CRP and SAP levels in plaice serum
    • White A., Fletcher T.C., Pepys M.B., Baldo B.A. The effect of inflammatory agents on CRP and SAP levels in plaice serum. Comp Biochem Physiol. C69:1981;325-329.
    • (1981) Comp Biochem Physiol , vol.69 , pp. 325-329
    • White, A.1    Fletcher, T.C.2    Pepys, M.B.3    Baldo, B.A.4
  • 22
    • 0026907317 scopus 로고
    • Elevation of C-reactive protein in serum of Channa punctatus as an indicator of water pollution
    • Ghosh S., Bhattacharya S. Elevation of C-reactive protein in serum of Channa punctatus as an indicator of water pollution. Indian J Exp Biol. 30:1992;736-737.
    • (1992) Indian J Exp Biol , vol.30 , pp. 736-737
    • Ghosh, S.1    Bhattacharya, S.2
  • 24
    • 0024340115 scopus 로고
    • Activation of trout macrophages and production of CRP after immunisation with Vibrio anguillarum
    • Kodama H., Yamada F., Murai T., Nakanishi Y., Mikami T., Izawa H. Activation of trout macrophages and production of CRP after immunisation with Vibrio anguillarum. Dev Comp Immunol. 13:1989;123-132.
    • (1989) Dev Comp Immunol , vol.13 , pp. 123-132
    • Kodama, H.1    Yamada, F.2    Murai, T.3    Nakanishi, Y.4    Mikami, T.5    Izawa, H.6
  • 25
    • 0020678795 scopus 로고
    • Induction in rainbow trout of an acute phase (C-reactive) protein by chemicals of environmental concern
    • Winkelhake J.L., Vodicnik M.J., Taylor J.L. Induction in rainbow trout of an acute phase (C-reactive) protein by chemicals of environmental concern. Comp Biochem Physiol. C74:1983;55-58.
    • (1983) Comp Biochem Physiol , vol.74 , pp. 55-58
    • Winkelhake, J.L.1    Vodicnik, M.J.2    Taylor, J.L.3
  • 27
    • 0033025199 scopus 로고    scopus 로고
    • Changes in serum concentration of an SAP-like pentraxin in Atlantic salmon Salmo salar during infection and inflammation
    • Lund V., Olafsen J.A. Changes in serum concentration of an SAP-like pentraxin in Atlantic salmon Salmo salar during infection and inflammation. Dev Comp Immunol. 23:1999;61-70.
    • (1999) Dev Comp Immunol , vol.23 , pp. 61-70
    • Lund, V.1    Olafsen, J.A.2
  • 28
    • 0035315263 scopus 로고    scopus 로고
    • Molecular cloning of carp (Cyprinus carpio) C-type lectin and pentraxin by use of suppression subtractive hybridisation
    • Fujiki K., Bayne C.J., Shin D.-H., Nakao M., Yang T. Molecular cloning of carp (Cyprinus carpio) C-type lectin and pentraxin by use of suppression subtractive hybridisation. Fish Shellfish Immunol. 11:2001;275-279.
    • (2001) Fish Shellfish Immunol , vol.11 , pp. 275-279
    • Fujiki, K.1    Bayne, C.J.2    Shin, D.-H.3    Nakao, M.4    Yang, T.5
  • 30
    • 0033868512 scopus 로고    scopus 로고
    • Metal accumulation and metallothionein in two populations of brown trout, Salmo trutta, exposed to different natural water environments during a run-off episode
    • Olsvik P.A., Gundersen P., Andersen A., Zachariassen K.E. Metal accumulation and metallothionein in two populations of brown trout, Salmo trutta, exposed to different natural water environments during a run-off episode. Aquat Toxicol. 50:2000;301-316.
    • (2000) Aquat Toxicol , vol.50 , pp. 301-316
    • Olsvik, P.A.1    Gundersen, P.2    Andersen, A.3    Zachariassen, K.E.4
  • 32
    • 0021106542 scopus 로고
    • Purification of IgG monoclonal antibody by caprylic acid precipitation
    • Russ C., Callegaro I., Lanza B., Ferrone S. Purification of IgG monoclonal antibody by caprylic acid precipitation. J Immunol Meth. 65:1983;269-271.
    • (1983) J Immunol Meth , vol.65 , pp. 269-271
    • Russ, C.1    Callegaro, I.2    Lanza, B.3    Ferrone, S.4
  • 33
    • 0001155019 scopus 로고
    • Characterisation of the major plasma apoliproteins of the HDL in carp (Cyprinus carpio)
    • Amthauer R., Villanueva M.I.N., Concha M., Krauskope M. Characterisation of the major plasma apoliproteins of the HDL in carp (Cyprinus carpio). Comp Biochem Physiol. B92:1989;787-793.
    • (1989) Comp Biochem Physiol , vol.92 , pp. 787-793
    • Amthauer, R.1    Villanueva, M.I.N.2    Concha, M.3    Krauskope, M.4
  • 35
    • 0023791268 scopus 로고
    • Interaction of cibacron blue and anilinonaphthalenesulfonate with lipoproteins provides a new means for simple isolation of these plasma proteins
    • Amthauer R., Concha M., Villanueva J., Krauskopf M. Interaction of cibacron blue and anilinonaphthalenesulfonate with lipoproteins provides a new means for simple isolation of these plasma proteins. Biochem Biophys Res Comm. 154:1988;752-757.
    • (1988) Biochem Biophys Res Comm , vol.154 , pp. 752-757
    • Amthauer, R.1    Concha, M.2    Villanueva, J.3    Krauskopf, M.4
  • 37
    • 0026666939 scopus 로고
    • Pentraxin family of proteins interact specifically with phosphorylcholine and or phosphorylethanolamine
    • Schwalbe R.A., Dahlback B., Coe J.E., Nelsestuen G.L. Pentraxin family of proteins interact specifically with phosphorylcholine and or phosphorylethanolamine. Biochemistry. 31:1992;4907-4915.
    • (1992) Biochemistry , vol.31 , pp. 4907-4915
    • Schwalbe, R.A.1    Dahlback, B.2    Coe, J.E.3    Nelsestuen, G.L.4
  • 38
    • 0025285866 scopus 로고
    • Preliminary crystallographic analysis of C-reactive protein from Limulus polyphemus
    • Myles D.A.A., Bailey S., Rule S.A., Jones G.R., Greenhough T.J. Preliminary crystallographic analysis of C-reactive protein from Limulus polyphemus. J Mol Biol. 213:1990;223-225.
    • (1990) J Mol Biol , vol.213 , pp. 223-225
    • Myles, D.A.A.1    Bailey, S.2    Rule, S.A.3    Jones, G.R.4    Greenhough, T.J.5
  • 41
    • 0029316274 scopus 로고
    • Characterisation of rainbow trout C-polysaccharide binding proteins
    • Murata M., Kodama H., Onuma M. Characterisation of rainbow trout C-polysaccharide binding proteins. J Vet Med Sci. 57:1995;419-425.
    • (1995) J Vet Med Sci , vol.57 , pp. 419-425
    • Murata, M.1    Kodama, H.2    Onuma, M.3
  • 42
    • 0017872572 scopus 로고
    • Analogues in other mammals and in fish of human plasma proteins C-reactive protein and amyloid P component
    • Pepys M.B., Dash A.C., Fletcher T.C., Richardson N., Munn E.A., Feinstein A. Analogues in other mammals and in fish of human plasma proteins C-reactive protein and amyloid P component. Nature. 273:1978;168-170.
    • (1978) Nature , vol.273 , pp. 168-170
    • Pepys, M.B.1    Dash, A.C.2    Fletcher, T.C.3    Richardson, N.4    Munn, E.A.5    Feinstein, A.6
  • 43
    • 0028774537 scopus 로고
    • Comparative analysis of pentraxins: Implications for protomer assembly and ligand binding
    • Srinivasan N., White H.E., Emsley J., Wood S.P., Pepys M.B., Blundell T.L. Comparative analysis of pentraxins: implications for protomer assembly and ligand binding. Structure. 2:1994;1017-1027.
    • (1994) Structure , vol.2 , pp. 1017-1027
    • Srinivasan, N.1    White, H.E.2    Emsley, J.3    Wood, S.P.4    Pepys, M.B.5    Blundell, T.L.6
  • 44
    • 0026686334 scopus 로고
    • Isolation of an acute phase phosphorylcholine-reactive pentraxin from channel catfish (Ictalarus punctatus)
    • Szalai A.J., Norcum M.T., Bly J.E., Clem L.W. Isolation of an acute phase phosphorylcholine-reactive pentraxin from channel catfish (Ictalarus punctatus). Comp Biochem Physiol. B102:1992;535-543.
    • (1992) Comp Biochem Physiol , vol.102 , pp. 535-543
    • Szalai, A.J.1    Norcum, M.T.2    Bly, J.E.3    Clem, L.W.4
  • 45
    • 0027015891 scopus 로고
    • Purification of C-reactive protein from Channa punctatus (Bloch)
    • Mitra S., Bhattacharya S. Purification of C-reactive protein from Channa punctatus (Bloch). Indian J Biochem Biophys. 29:1992;508-511.
    • (1992) Indian J Biochem Biophys , vol.29 , pp. 508-511
    • Mitra, S.1    Bhattacharya, S.2
  • 46
    • 0017388013 scopus 로고
    • C-reactive protein-like precipitin and lysozyme in the lumpsucker Cyclopterus lumpus during the breeding season
    • Fletcher T.C., White A., Baldo B.A. C-reactive protein-like precipitin and lysozyme in the lumpsucker Cyclopterus lumpus during the breeding season. Comp Biochem Physiol. B57:1977;353-357.
    • (1977) Comp Biochem Physiol , vol.57 , pp. 353-357
    • Fletcher, T.C.1    White, A.2    Baldo, B.A.3
  • 47
  • 48
    • 0031903161 scopus 로고    scopus 로고
    • Atypical phosphorylcholine-reactive protein from Atlantic Salmon Salmo salar L
    • Lund V., Olafsen J.A. Atypical phosphorylcholine-reactive protein from Atlantic Salmon Salmo salar L. Comp Biochem Physiol. B119:1998;471-477.
    • (1998) Comp Biochem Physiol , vol.119 , pp. 471-477
    • Lund, V.1    Olafsen, J.A.2
  • 49
    • 0025294165 scopus 로고
    • Isolation and characterization of rainbow trout C-reactive protein
    • Murai T., Kodama H., Naiki M., Mikami T., Izawa H. Isolation and characterization of rainbow trout C-reactive protein. Dev Comp Immunol. 14:1990;49-58.
    • (1990) Dev Comp Immunol , vol.14 , pp. 49-58
    • Murai, T.1    Kodama, H.2    Naiki, M.3    Mikami, T.4    Izawa, H.5
  • 50
    • 0033325655 scopus 로고    scopus 로고
    • Lectin like properties and differential sugar binding characteristics of C-reactive proteins purified from sera of normal and pollutant induced Labeo rohita
    • Mandal C., Sinha S., Mandal C. Lectin like properties and differential sugar binding characteristics of C-reactive proteins purified from sera of normal and pollutant induced Labeo rohita. Glycoconj J. 16:1999;741-750.
    • (1999) Glycoconj J , vol.16 , pp. 741-750
    • Mandal, C.1    Sinha, S.2    Mandal, C.3
  • 52
    • 0032051803 scopus 로고    scopus 로고
    • A comparative study of pentraxin-like proteins in different fish species
    • Lund V., Olafsen J.A. A comparative study of pentraxin-like proteins in different fish species. Dev Comp Immunol. 22:1998;185-194.
    • (1998) Dev Comp Immunol , vol.22 , pp. 185-194
    • Lund, V.1    Olafsen, J.A.2
  • 53
    • 0028491066 scopus 로고
    • Isolation and characterization of rainbow trout (Oncorhynchus mykiss) serum amyloid P component (SAP)
    • Murata M., Onuma M., Kodama H. Isolation and characterization of rainbow trout (Oncorhynchus mykiss) serum amyloid P component (SAP). J Vet Med Sci. 56:1994;661-665.
    • (1994) J Vet Med Sci , vol.56 , pp. 661-665
    • Murata, M.1    Onuma, M.2    Kodama, H.3


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