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Volumn 25, Issue 2, 2006, Pages 337-348

Plasma sampling and freezing procedures influence vitellogenin measurements by enzyme-linked immunoassay in the fathead minnow (Pimephales promelas)

Author keywords

Aprotinin; Enzyme linked immunoassay; Fathead minnow; Freezing; Vitellogenin

Indexed keywords

BIOASSAY; BIODEGRADATION; ENZYME KINETICS; FREEZING; IMMUNOLOGY; LIQUID CHROMATOGRAPHY;

EID: 31144475123     PISSN: 07307268     EISSN: None     Source Type: Journal    
DOI: 10.1897/05-368R.1     Document Type: Article
Times cited : (18)

References (42)
  • 1
    • 0032576482 scopus 로고    scopus 로고
    • Xenoendocrine disrupters - Environmental impacts
    • Sumpter JP. 1998. Xenoendocrine disrupters-Environmental impacts. Toxicol Lett (Amst) 102-103:337-342.
    • (1998) Toxicol Lett (Amst) , vol.102-103 , pp. 337-342
    • Sumpter, J.P.1
  • 2
    • 0031844641 scopus 로고    scopus 로고
    • Endocrine disruption in wildlife: A critical review of the evidence
    • Tyler CR, Jobling M, Sumpter JP. 1998. Endocrine disruption in wildlife: A critical review of the evidence. Crit Rev Toxicol 28:319-361.
    • (1998) Crit Rev Toxicol , vol.28 , pp. 319-361
    • Tyler, C.R.1    Jobling, M.2    Sumpter, J.P.3
  • 3
    • 0012555432 scopus 로고    scopus 로고
    • London, UK, October 28-29. Report 9906. Paris, France
    • Organization for Economic Cooperation and Development. 1999. Final report from the OECD expert consultation meeting, London, UK, October 28-29, 1998. Report 9906. Paris, France.
    • (1998) Final Report from the OECD Expert Consultation Meeting
  • 5
    • 77956833641 scopus 로고
    • Vitellogenesis and oocyte assembly
    • Hoar WS, Randall DJ, eds. Academic, New York, NY, USA
    • Mommsen TP, Walsh PJ. 1988. Vitellogenesis and oocyte assembly. In Hoar WS, Randall DJ, eds, Fish Physiology. Academic, New York, NY, USA, pp 347-406.
    • (1988) Fish Physiology , pp. 347-406
    • Mommsen, T.P.1    Walsh, P.J.2
  • 6
    • 0028840615 scopus 로고
    • Vitellogenesis as a biomarker for estrogenic contamination of the aquatic environment
    • Sumpter JP, Jobling S. 1995. Vitellogenesis as a biomarker for estrogenic contamination of the aquatic environment. Environ Health Perspect 103 (Suppl 7):173-178.
    • (1995) Environ Health Perspect , vol.103 , Issue.SUPPL. 7 , pp. 173-178
    • Sumpter, J.P.1    Jobling, S.2
  • 7
    • 0024063518 scopus 로고
    • Evolution and expression of vitellogenin genes
    • Wahli W. 1988. Evolution and expression of vitellogenin genes. Trends Genet 4:227-232.
    • (1988) Trends Genet , vol.4 , pp. 227-232
    • Wahli, W.1
  • 8
    • 0029006293 scopus 로고
    • Characterization of vitellogenin from white sturgeon, Acipenser transmontanus
    • Bidwell CA, Carlson DM. 1995. Characterization of vitellogenin from white sturgeon, Acipenser transmontanus. J Mol Evol 41:104-112.
    • (1995) J Mol Evol , vol.41 , pp. 104-112
    • Bidwell, C.A.1    Carlson, D.M.2
  • 9
    • 0029138877 scopus 로고
    • A highly conserved N-terminal sequence for teleost vitellogenin with potential value to the biochemistry, molecular biology, and pathology of Vitellogenesis
    • Folmar LC, Denslow ND, Wallace RA, LaFleur G, Gross TS, Bonomelli S, Sullivan CV. 1995. A highly conserved N-terminal sequence for teleost vitellogenin with potential value to the biochemistry, molecular biology, and pathology of Vitellogenesis. J Fish Biol 46:255-263.
    • (1995) J Fish Biol , vol.46 , pp. 255-263
    • Folmar, L.C.1    Denslow, N.D.2    Wallace, R.A.3    Lafleur, G.4    Gross, T.S.5    Bonomelli, S.6    Sullivan, C.V.7
  • 12
    • 0031820953 scopus 로고    scopus 로고
    • Adverse reproductive effects in male fathead minnows (Pimephales promelas) exposed to environmentally relevant concentrations of the natural estrogens, estradiol, and estrone
    • Panter GH, Thompson RS, Sumpter JP 1998. Adverse reproductive effects in male fathead minnows (Pimephales promelas) exposed to environmentally relevant concentrations of the natural estrogens, estradiol, and estrone. Aquat Toxicol 42:243-253.
    • (1998) Aquat Toxicol , vol.42 , pp. 243-253
    • Panter, G.H.1    Thompson, R.S.2    Sumpter, J.P.3
  • 13
    • 0032935602 scopus 로고    scopus 로고
    • An in vivo testing system for endocrine disrupters in fish early life stages using induction of vitellogenin
    • Tyler CR, van Aerie R, Hutchinson TH, Maddix S, Trip H. 1999. An in vivo testing system for endocrine disrupters in fish early life stages using induction of vitellogenin. Environ Toxicol Chem 18:337-347.
    • (1999) Environ Toxicol Chem , vol.18 , pp. 337-347
    • Tyler, C.R.1    Van Aerie, R.2    Hutchinson, T.H.3    Maddix, S.4    Trip, H.5
  • 14
    • 0036910293 scopus 로고    scopus 로고
    • Window of sensitivity for the estrogenic effects of ethinylestradiol in early life-stages of fathead minnow, Pimephales promelas
    • Van Aerie R, Pounds N, Hutchinson TH, Maddix S, Tyler CR. 2002. Window of sensitivity for the estrogenic effects of ethinylestradiol in early life-stages of fathead minnow, Pimephales promelas. Ecotoxicology 11:423-434.
    • (2002) Ecotoxicology , vol.11 , pp. 423-434
    • Van Aerie, R.1    Pounds, N.2    Hutchinson, T.H.3    Maddix, S.4    Tyler, C.R.5
  • 15
    • 0034662010 scopus 로고    scopus 로고
    • Development of a reproductive performance test for endocrine disrupting chemicals using pair-breeding fathead minnows (Pimephales promelas)
    • Harries JE, Runnals T Hill E, Harris CA, Maddix S, Sumpter JP, Tyler CR. 2000. Development of a reproductive performance test for endocrine disrupting chemicals using pair-breeding fathead minnows (Pimephales promelas). Environ Sci Technol 34:3003-3011.
    • (2000) Environ Sci Technol , vol.34 , pp. 3003-3011
    • Harries, J.E.1    Runnals, T.2    Hill, E.3    Harris, C.A.4    Maddix, S.5    Sumpter, J.P.6    Tyler, C.R.7
  • 16
    • 0037317977 scopus 로고    scopus 로고
    • Comparison of ELISAs for detecting vitellogenin in the fathead minnow (Pimephales promelas)
    • Mylchreest E, Snajdr S, Korte JJ, Ankley G. 2003. Comparison of ELISAs for detecting vitellogenin in the fathead minnow (Pimephales promelas). Comp Biochem Phvsiol C 134:251-257.
    • (2003) Comp Biochem Phvsiol C , vol.134 , pp. 251-257
    • Mylchreest, E.1    Snajdr, S.2    Korte, J.J.3    Ankley, G.4
  • 17
    • 8144226621 scopus 로고    scopus 로고
    • Comparative evaluation of ELISAs for detecting vitellogenin in the fathead minnow (Pimephales promelas) - A response to Tyler et al
    • Korte JJ, Mylchreest E, Ankley GT 2004. Comparative evaluation of ELISAs for detecting vitellogenin in the fathead minnow (Pimephales promelas)-A response to Tyler et al. Comp Biochem Physiol C 138:533-536.
    • (2004) Comp Biochem Physiol C , vol.138 , pp. 533-536
    • Korte, J.J.1    Mylchreest, E.2    Ankley, G.T.3
  • 18
    • 8144225869 scopus 로고    scopus 로고
    • ELlSAs for detecting vitellogenin in the fathead minnow (Pimephales promelas) - A critical analysis. Response to Mylchreest et al
    • Tyler CR, van Aerie R, Santos EM. 2004. ELlSAs for detecting vitellogenin in the fathead minnow (Pimephales promelas)-A critical analysis. Response to Mylchreest et al. Comp Biochem Physiol C 138:531-532.
    • (2004) Comp Biochem Physiol C , vol.138 , pp. 531-532
    • Tyler, C.R.1    Van Aerie, R.2    Santos, E.M.3
  • 20
    • 0034601707 scopus 로고    scopus 로고
    • A zebrafish vitellogenin gene (vg3) encodes a novel vitellogenin without a phosvitin domain and may represent a primitive vertebrate vitellogenin gene
    • Wang H, Yan T, Tan JTT, Gong Z. 2000. A zebrafish vitellogenin gene (vg3) encodes a novel vitellogenin without a phosvitin domain and may represent a primitive vertebrate vitellogenin gene. Gene 256:303-310.
    • (2000) Gene , vol.256 , pp. 303-310
    • Wang, H.1    Yan, T.2    Tan, J.T.T.3    Gong, Z.4
  • 22
    • 0032972894 scopus 로고    scopus 로고
    • Fathead minnow (Pimephales promelas) vitellogenin: Purification, characterization, and quantitative immunoassay for the detection of estrogenic compounds
    • Parks LG, Cheek AO, Denslow ND, Heppell SA, McLachlan JA, LeBlanc GA, Sullivan CV. 1999. Fathead minnow (Pimephales promelas) vitellogenin: Purification, characterization, and quantitative immunoassay for the detection of estrogenic compounds. Comp Biochem Physiol C 123:113-125.
    • (1999) Comp Biochem Physiol C , vol.123 , pp. 113-125
    • Parks, L.G.1    Cheek, A.O.2    Denslow, N.D.3    Heppell, S.A.4    McLachlan, J.A.5    LeBlanc, G.A.6    Sullivan, C.V.7
  • 23
    • 0030728066 scopus 로고    scopus 로고
    • Degradation of vitellogenins by 170 kDa trypsin-like protease in the plasma of the tilapia, Oreochromis niloticus
    • Inaba K, Buerano CC, Natividad FF, Morisawa M. 1997. Degradation of vitellogenins by 170 kDa trypsin-like protease in the plasma of the tilapia, Oreochromis niloticus. Comp Biochem Physiol B 118:85-90.
    • (1997) Comp Biochem Physiol B , vol.118 , pp. 85-90
    • Inaba, K.1    Buerano, C.C.2    Natividad, F.F.3    Morisawa, M.4
  • 24
    • 0034743640 scopus 로고    scopus 로고
    • Effects of estradiol-17β treatment on in vitro and in vivo synthesis of two distinct vitellogenins in tilapia
    • Takemura A, Kim BH. 2001. Effects of estradiol-17β treatment on in vitro and in vivo synthesis of two distinct vitellogenins in tilapia. Comp Biochem Physiol A 129:641-651.
    • (2001) Comp Biochem Physiol A , vol.129 , pp. 641-651
    • Takemura, A.1    Kim, B.H.2
  • 25
    • 31244431656 scopus 로고    scopus 로고
    • Quantitative measurement of fathead minnow vitellogenin by liquid chromatography combined with tandem mass spectrometry using a signature peptide of vitellogenin
    • Zhang F, Bartels MJ, Brodeur JC, Woodburn KB. 2004. Quantitative measurement of fathead minnow vitellogenin by liquid chromatography combined with tandem mass spectrometry using a signature peptide of vitellogenin. Environ Toxicol Chem 23:1408-1415.
    • (2004) Environ Toxicol Chem , vol.23 , pp. 1408-1415
    • Zhang, F.1    Bartels, M.J.2    Brodeur, J.C.3    Woodburn, K.B.4
  • 26
    • 0027130917 scopus 로고
    • Isolation, immunochemical detection, and observations of the instability of vitellogenin from four teleosts
    • Silversand C, Hyllner SJ, Haux C. 1993. Isolation, immunochemical detection, and observations of the instability of vitellogenin from four teleosts. J Exp Zool 267:587-597.
    • (1993) J Exp Zool , vol.267 , pp. 587-597
    • Silversand, C.1    Hyllner, S.J.2    Haux, C.3
  • 27
    • 1642462880 scopus 로고    scopus 로고
    • Differential scanning calorimetry investigation of formation of poly(ethylene glycol) hydrate with controlled freeze-thawing of aqueous protein solution
    • Hillgren A, Alden M. 2004. Differential scanning calorimetry investigation of formation of poly(ethylene glycol) hydrate with controlled freeze-thawing of aqueous protein solution. Journal of Applied Polymer Science 91:1626-1634.
    • (2004) Journal of Applied Polymer Science , vol.91 , pp. 1626-1634
    • Hillgren, A.1    Alden, M.2
  • 28
    • 0032782071 scopus 로고    scopus 로고
    • Instability, stabilization, and formulation of liquid protein pharmaceuticals
    • Wang W. 1999. Instability, stabilization, and formulation of liquid protein pharmaceuticals. Int J Pharm 185:129-188.
    • (1999) Int J Pharm , vol.185 , pp. 129-188
    • Wang, W.1
  • 29
    • 0030770631 scopus 로고    scopus 로고
    • Rational design of stable lyophilized protein formulations: Some practical advice
    • Carpenter JF, Pikal MJ, Chang BS, Randolph TW. 1997. Rational design of stable lyophilized protein formulations: Some practical advice. Pharm Res 14:969-975.
    • (1997) Pharm Res , vol.14 , pp. 969-975
    • Carpenter, J.F.1    Pikal, M.J.2    Chang, B.S.3    Randolph, T.W.4
  • 30
    • 9244244147 scopus 로고    scopus 로고
    • Quantitation of 17α-ethinylestradiol in aquatic samples using liquid-liquid phase extraction, dansyl derivatization, and liquid chromatography/positive electrospray tandem mass spectrometry
    • Zhang F, Bartels MJ, Brodeur JC, Woodburn KB. 2004. Quantitation of 17α-ethinylestradiol in aquatic samples using liquid-liquid phase extraction, dansyl derivatization, and liquid chromatography/positive electrospray tandem mass spectrometry. Rapid Commun Mass Spectrom 18:2739-2742.
    • (2004) Rapid Commun Mass Spectrom , vol.18 , pp. 2739-2742
    • Zhang, F.1    Bartels, M.J.2    Brodeur, J.C.3    Woodburn, K.B.4
  • 31
    • 84908219488 scopus 로고
    • Statistical methods for assessing agreement between two methods of clinical measurement
    • Bland JM, Altman DG. 1986. Statistical methods for assessing agreement between two methods of clinical measurement. Lancet i:307-310.
    • (1986) Lancet , vol.1 , pp. 307-310
    • Bland, J.M.1    Altman, D.G.2
  • 32
    • 0344088420 scopus 로고    scopus 로고
    • Development of enzyme-linked immunosorbent assays for two forms of vitellogenin in Japanese common goby (Acanthogobius flavimanus)
    • Ohkubo N, Mochida K, Adachi S, Hara A, Hotta K, Nakamura Y, Matsubara T. 2003. Development of enzyme-linked immunosorbent assays for two forms of vitellogenin in Japanese common goby (Acanthogobius flavimanus). Gen Comp Endocrinol 131:353-364.
    • (2003) Gen Comp Endocrinol , vol.131 , pp. 353-364
    • Ohkubo, N.1    Mochida, K.2    Adachi, S.3    Hara, A.4    Hotta, K.5    Nakamura, Y.6    Matsubara, T.7
  • 33
    • 0026519984 scopus 로고
    • Monoclonal antibody-based immunoassay of vitellogenin in the blood of male channel catfish (Ictalurus punctatus)
    • Goodwin AE, Grizzle JM, Bradley JT, Estridge BH. 1992. Monoclonal antibody-based immunoassay of vitellogenin in the blood of male channel catfish (Ictalurus punctatus). Comp Biochem Physiol B 101:441-446.
    • (1992) Comp Biochem Physiol B , vol.101 , pp. 441-446
    • Goodwin, A.E.1    Grizzle, J.M.2    Bradley, J.T.3    Estridge, B.H.4
  • 34
    • 0037333806 scopus 로고    scopus 로고
    • Vitellogenin isolation, purification, and antigenic cross-reactivity in three teleost species
    • Watts M, Pankhurst NW, Pryce A, Sun B. 2003. Vitellogenin isolation, purification, and antigenic cross-reactivity in three teleost species. Comp Biochem Physiol B 134:467-476.
    • (2003) Comp Biochem Physiol B , vol.134 , pp. 467-476
    • Watts, M.1    Pankhurst, N.W.2    Pryce, A.3    Sun, B.4
  • 35
    • 0029360380 scopus 로고
    • Vitellogenins of Oreochromis niloticus: Identification, isolation, and biochemical and immunochemical characterization
    • Buerano CC, Inaba K, Natividad FF, Morisawa M. 1995. Vitellogenins of Oreochromis niloticus: Identification, isolation, and biochemical and immunochemical characterization. J Exp Zool 273:59-69.
    • (1995) J Exp Zool , vol.273 , pp. 59-69
    • Buerano, C.C.1    Inaba, K.2    Natividad, F.F.3    Morisawa, M.4
  • 36
    • 0030266263 scopus 로고    scopus 로고
    • Plasma vitellogenin of grouper (Epinephelus malabaricus): Isolation and properties
    • Utarabhand P, Bunlipatanon P. 1996. Plasma vitellogenin of grouper (Epinephelus malabaricus): Isolation and properties. Comp Biochem Physiol C 115C:101-110.
    • (1996) Comp Biochem Physiol C , vol.115 C , pp. 101-110
    • Utarabhand, P.1    Bunlipatanon, P.2
  • 37
    • 0033199056 scopus 로고    scopus 로고
    • Two forms of vitellogenin yielding two distinct lipovitellins, play different roles during oocyte maturation and early development of barfin flounder, Verasper moseri, a marine teleost that spawns pelagic eggs
    • Matsubara T, Ohkubo N, Andoh T, Sullivan CV, Hara A. 1999. Two forms of vitellogenin yielding two distinct lipovitellins, play different roles during oocyte maturation and early development of barfin flounder, Verasper moseri, a marine teleost that spawns pelagic eggs. Dev Biol 213:18-32.
    • (1999) Dev Biol , vol.213 , pp. 18-32
    • Matsubara, T.1    Ohkubo, N.2    Andoh, T.3    Sullivan, C.V.4    Hara, A.5
  • 38
    • 0035870296 scopus 로고    scopus 로고
    • Lipovitellins derived from two forms of vitellogenin are differentially processed during oocyte maturation in haddock (Melanogrammus aeglefinus)
    • Reith M, Munholland J, Kelly J, Finn RN, Fyhn HJ. 2001. Lipovitellins derived from two forms of vitellogenin are differentially processed during oocyte maturation in haddock (Melanogrammus aeglefinus). J Exp Zool 291:58-67.
    • (2001) J Exp Zool , vol.291 , pp. 58-67
    • Reith, M.1    Munholland, J.2    Kelly, J.3    Finn, R.N.4    Fyhn, H.J.5
  • 39
    • 0036891380 scopus 로고    scopus 로고
    • Purification and identification of a second form of vitellogenin from ascites of medaka (Oryzias latipes) treated with estrogen
    • Shimizu M, Fujiwara Y, Fukada H, Hara A. 2002. Purification and identification of a second form of vitellogenin from ascites of medaka (Oryzias latipes) treated with estrogen. J Exp Zool 293:726-735.
    • (2002) J Exp Zool , vol.293 , pp. 726-735
    • Shimizu, M.1    Fujiwara, Y.2    Fukada, H.3    Hara, A.4
  • 40
    • 0035992455 scopus 로고    scopus 로고
    • Development and validation of an enzyme-linked immunosorbent assay to measure vitellogenin in the zebrafish (Danio rerio)
    • Brion F, Nilsen BM, Eidem JK, Goksoyr A, Porcher, JM. 2002. Development and validation of an enzyme-linked immunosorbent assay to measure vitellogenin in the zebrafish (Danio rerio). Environ Toxicol Chem 28:1699-1708.
    • (2002) Environ Toxicol Chem , vol.28 , pp. 1699-1708
    • Brion, F.1    Nilsen, B.M.2    Eidem, J.K.3    Goksoyr, A.4    Porcher, J.M.5
  • 42
    • 8844277553 scopus 로고    scopus 로고
    • Deduced primary structures of three types of vitellogenin in mosquitofish (Gambusia affinis), a viviparous fish
    • Sawaguchi S, Koya Y, Matsubara T. 2003. Deduced primary structures of three types of vitellogenin in mosquitofish (Gambusia affinis), a viviparous fish. Fish Physiol Biochem 28:363-364.
    • (2003) Fish Physiol Biochem , vol.28 , pp. 363-364
    • Sawaguchi, S.1    Koya, Y.2    Matsubara, T.3


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