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Volumn 263, Issue 3, 2012, Pages 352-359

Intravenous application of an anticalin dramatically lowers plasma digoxin levels and reduces its toxic effects in rats

Author keywords

Anticalin; Antidotal therapy; Digoxin toxicity; Rats

Indexed keywords

ANTICALIN DIGA16; ANTIDOTE; DIGOXIN; SODIUM CHLORIDE; UNCLASSIFIED DRUG;

EID: 84865434852     PISSN: 0041008X     EISSN: 10960333     Source Type: Journal    
DOI: 10.1016/j.taap.2012.07.009     Document Type: Article
Times cited : (23)

References (53)
  • 3
  • 4
    • 0030763546 scopus 로고    scopus 로고
    • Multicenter study of Abbott AxSYM Digoxin II assay and comparison with 6 methods for susceptibility to digoxin-like immunoreactive factors
    • Azzazy H.M., Duh S.H., Maturen A., Schaller E., Shaw L., Grimaldi R., Shock G., Christenson R.H. Multicenter study of Abbott AxSYM Digoxin II assay and comparison with 6 methods for susceptibility to digoxin-like immunoreactive factors. Clin. Chem. 1997, 43:1635-1640.
    • (1997) Clin. Chem. , vol.43 , pp. 1635-1640
    • Azzazy, H.M.1    Duh, S.H.2    Maturen, A.3    Schaller, E.4    Shaw, L.5    Grimaldi, R.6    Shock, G.7    Christenson, R.H.8
  • 6
    • 0026772320 scopus 로고
    • Influence of assay methods on serum concentrations of digoxin during FAB fragment treatment
    • Banner W., Bach P., Burk B., Freestone S., Gooch W.M. Influence of assay methods on serum concentrations of digoxin during FAB fragment treatment. J. Toxicol. Clin. Toxicol. 1992, 30:259-267.
    • (1992) J. Toxicol. Clin. Toxicol. , vol.30 , pp. 259-267
    • Banner, W.1    Bach, P.2    Burk, B.3    Freestone, S.4    Gooch, W.M.5
  • 8
    • 17544362782 scopus 로고    scopus 로고
    • Digoxin-specific antibody fragments: how much and when?
    • Bateman D.N. Digoxin-specific antibody fragments: how much and when?. Toxicol. Rev. 2004, 23:135-143.
    • (2004) Toxicol. Rev. , vol.23 , pp. 135-143
    • Bateman, D.N.1
  • 9
    • 0001127258 scopus 로고
    • An analysis of the time-relations of electrocardiograms
    • Bazett H.C. An analysis of the time-relations of electrocardiograms. Heart 1920, 7:353-370.
    • (1920) Heart , vol.7 , pp. 353-370
    • Bazett, H.C.1
  • 10
    • 0033515005 scopus 로고    scopus 로고
    • Small antibody-like proteins with prescribed ligand specificities derived from the lipocalin fold
    • Beste G., Schmidt F.S., Stibora T., Skerra A. Small antibody-like proteins with prescribed ligand specificities derived from the lipocalin fold. Proc. Natl. Acad. Sci. U. S. A. 1999, 96:1898-1903.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 1898-1903
    • Beste, G.1    Schmidt, F.S.2    Stibora, T.3    Skerra, A.4
  • 11
    • 84865433618 scopus 로고    scopus 로고
    • Half-life extension of therapeutic proteins via genetic fusion to recombinant PEG mimetics
    • Wiley-VCH, Weinheim, R. Kontermann (Ed.)
    • Binder U., Skerra A. Half-life extension of therapeutic proteins via genetic fusion to recombinant PEG mimetics. Therapeutic Proteins - Strategies to Modulate Their Plasma Half-lives 2012, 63-80. Wiley-VCH, Weinheim. R. Kontermann (Ed.).
    • (2012) Therapeutic Proteins - Strategies to Modulate Their Plasma Half-lives , pp. 63-80
    • Binder, U.1    Skerra, A.2
  • 12
  • 14
    • 0025286532 scopus 로고
    • Crystallographic refinement of human serum retinol binding protein at 2Å resolution
    • Cowan S.W., Newcomer M.E., Jones T.A. Crystallographic refinement of human serum retinol binding protein at 2Å resolution. Proteins 1990, 8:44-61.
    • (1990) Proteins , vol.8 , pp. 44-61
    • Cowan, S.W.1    Newcomer, M.E.2    Jones, T.A.3
  • 15
    • 34247092061 scopus 로고    scopus 로고
    • Therapeutic drug monitoring of digoxin: impact of endogenous and exogenous digoxin-like immunoreactive substances
    • Dasgupta A. Therapeutic drug monitoring of digoxin: impact of endogenous and exogenous digoxin-like immunoreactive substances. Toxicol. Rev. 2006, 25:273-281.
    • (2006) Toxicol. Rev. , vol.25 , pp. 273-281
    • Dasgupta, A.1
  • 16
    • 35649024789 scopus 로고    scopus 로고
    • Structural insight into the dual ligand specificity and mode of high density lipoprotein association of apolipoprotein D
    • Eichinger A., Nasreen A., Kim H.J., Skerra A. Structural insight into the dual ligand specificity and mode of high density lipoprotein association of apolipoprotein D. J. Biol. Chem. 2007, 282:31068-31075.
    • (2007) J. Biol. Chem. , vol.282 , pp. 31068-31075
    • Eichinger, A.1    Nasreen, A.2    Kim, H.J.3    Skerra, A.4
  • 18
    • 38949158378 scopus 로고    scopus 로고
    • Seromucosal transport of intravenously administered carbamazepine is not enhanced by oral doses of activated charcoal in rats
    • Eyer F., Jung N., Neuberger H., Witte A., Poethko T., Henke J., Zilker T. Seromucosal transport of intravenously administered carbamazepine is not enhanced by oral doses of activated charcoal in rats. Basic Clin. Pharmacol. Toxicol. 2008, 102:337-346.
    • (2008) Basic Clin. Pharmacol. Toxicol. , vol.102 , pp. 337-346
    • Eyer, F.1    Jung, N.2    Neuberger, H.3    Witte, A.4    Poethko, T.5    Henke, J.6    Zilker, T.7
  • 19
    • 78049501965 scopus 로고    scopus 로고
    • Free and total digoxin in serum during treatment of acute digoxin poisoning with Fab fragments: case study
    • Eyer F., Steimer W., Muller C., Zilker T. Free and total digoxin in serum during treatment of acute digoxin poisoning with Fab fragments: case study. Am. J. Crit. Care 2010, 19:387-391.
    • (2010) Am. J. Crit. Care , vol.19 , pp. 387-391
    • Eyer, F.1    Steimer, W.2    Muller, C.3    Zilker, T.4
  • 20
    • 10644288676 scopus 로고    scopus 로고
    • Fab antibody fragments: some applications in clinical toxicology
    • Flanagan R.J., Jones A.L. Fab antibody fragments: some applications in clinical toxicology. Drug Saf. 2004, 27:1115-1133.
    • (2004) Drug Saf. , vol.27 , pp. 1115-1133
    • Flanagan, R.J.1    Jones, A.L.2
  • 21
    • 0036865552 scopus 로고    scopus 로고
    • The neutrophil lipocalin NGAL is a bacteriostatic agent that interferes with siderophore-mediated iron acquisition
    • Goetz D.H., Holmes M.A., Borregaard N., Bluhm M.E., Raymond K.N., Strong R.K. The neutrophil lipocalin NGAL is a bacteriostatic agent that interferes with siderophore-mediated iron acquisition. Mol. Cell 2002, 10:1033-1043.
    • (2002) Mol. Cell , vol.10 , pp. 1033-1043
    • Goetz, D.H.1    Holmes, M.A.2    Borregaard, N.3    Bluhm, M.E.4    Raymond, K.N.5    Strong, R.K.6
  • 22
    • 77953658260 scopus 로고    scopus 로고
    • The immunogenicity of humanized and fully human antibodies: residual immunogenicity resides in the CDR regions
    • Harding F.A., Stickler M.M., Razo J., DuBridge R.B. The immunogenicity of humanized and fully human antibodies: residual immunogenicity resides in the CDR regions. MAbs 2010, 2:256-265.
    • (2010) MAbs , vol.2 , pp. 256-265
    • Harding, F.A.1    Stickler, M.M.2    Razo, J.3    DuBridge, R.B.4
  • 23
  • 24
    • 0017685973 scopus 로고
    • Physiologically based pharmacokinetic model for digoxin distribution and elimination in the rat
    • Harrison L.I., Gibaldi M. Physiologically based pharmacokinetic model for digoxin distribution and elimination in the rat. J. Pharm. Sci. 1977, 66:1138-1142.
    • (1977) J. Pharm. Sci. , vol.66 , pp. 1138-1142
    • Harrison, L.I.1    Gibaldi, M.2
  • 26
    • 0023571833 scopus 로고
    • Determination of free digoxin concentrations in serum for monitoring Fab treatment of digoxin overdose
    • Hursting M.J., Raisys V.A., Opheim K.E., Bell J.L., Trobaugh G.B., Smith T.W. Determination of free digoxin concentrations in serum for monitoring Fab treatment of digoxin overdose. Clin. Chem. 1987, 33:1652-1655.
    • (1987) Clin. Chem. , vol.33 , pp. 1652-1655
    • Hursting, M.J.1    Raisys, V.A.2    Opheim, K.E.3    Bell, J.L.4    Trobaugh, G.B.5    Smith, T.W.6
  • 27
    • 0026749889 scopus 로고
    • Recognition and management of digitalis toxicity
    • disc 118G-119G
    • Kelly R.A., Smith T.W. Recognition and management of digitalis toxicity. Am. J. Cardiol. 1992, 69:108G-118G. disc 118G-119G.
    • (1992) Am. J. Cardiol. , vol.69
    • Kelly, R.A.1    Smith, T.W.2
  • 28
    • 67749142080 scopus 로고    scopus 로고
    • High-affinity recognition of lanthanide(III) chelate complexes by a reprogrammed human lipocalin 2
    • Kim H.J., Eichinger A., Skerra A. High-affinity recognition of lanthanide(III) chelate complexes by a reprogrammed human lipocalin 2. J. Am. Chem. Soc. 2009, 131:3565-3576.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 3565-3576
    • Kim, H.J.1    Eichinger, A.2    Skerra, A.3
  • 29
    • 0016129772 scopus 로고
    • Stimulation of the development of the hepatic excretory mechanism for ouabain in newborn rats with microsomal enzyme inducers
    • Klaassen C.D. Stimulation of the development of the hepatic excretory mechanism for ouabain in newborn rats with microsomal enzyme inducers. J. Pharmacol. Exp. Ther. 1974, 191:212-218.
    • (1974) J. Pharmacol. Exp. Ther. , vol.191 , pp. 212-218
    • Klaassen, C.D.1
  • 30
    • 0038799729 scopus 로고    scopus 로고
    • Structural mechanism of specific ligand recognition by a lipocalin tailored for the complexation of digoxigenin
    • Korndörfer I.P., Schlehuber S., Skerra A. Structural mechanism of specific ligand recognition by a lipocalin tailored for the complexation of digoxigenin. J. Mol. Biol. 2003, 330:385-396.
    • (2003) J. Mol. Biol. , vol.330 , pp. 385-396
    • Korndörfer, I.P.1    Schlehuber, S.2    Skerra, A.3
  • 32
    • 0021255107 scopus 로고
    • Reversal of lethal digoxin toxicity in guinea pigs using monoclonal antibodies and Fab fragments
    • Lechat P., Mudgett-Hunter M., Margolies M.N., Haber E., Smith T.W. Reversal of lethal digoxin toxicity in guinea pigs using monoclonal antibodies and Fab fragments. J. Pharmacol. Exp. Ther. 1984, 229:210-213.
    • (1984) J. Pharmacol. Exp. Ther. , vol.229 , pp. 210-213
    • Lechat, P.1    Mudgett-Hunter, M.2    Margolies, M.N.3    Haber, E.4    Smith, T.W.5
  • 33
    • 44149098469 scopus 로고    scopus 로고
    • Pharmacokinetics of recombinant human lipocalin-type prostaglandin D synthase/beta-trace in canine
    • Li W., Mase M., Inui T., Shimoda M., Isomura K., Oda H., Yamada K., Urade Y. Pharmacokinetics of recombinant human lipocalin-type prostaglandin D synthase/beta-trace in canine. Neurosci. Res. 2008, 61:289-293.
    • (2008) Neurosci. Res. , vol.61 , pp. 289-293
    • Li, W.1    Mase, M.2    Inui, T.3    Shimoda, M.4    Isomura, K.5    Oda, H.6    Yamada, K.7    Urade, Y.8
  • 35
    • 84865435888 scopus 로고    scopus 로고
    • First in human phase I study of PRS-050 (Angiocal), a VEGF-A targeting anticalin, in patients with advanced solid tumors: results of a dose escalation study
    • Mross K., Fischer R., Richly H., Scharr D., Buechert M., Stern A., Hoth D., Gille H., Audoly L.P., Scheulen M.E. First in human phase I study of PRS-050 (Angiocal), a VEGF-A targeting anticalin, in patients with advanced solid tumors: results of a dose escalation study. Mol. Cancer Ther. 2011, 10:A212.
    • (2011) Mol. Cancer Ther. , vol.10
    • Mross, K.1    Fischer, R.2    Richly, H.3    Scharr, D.4    Buechert, M.5    Stern, A.6    Hoth, D.7    Gille, H.8    Audoly, L.P.9    Scheulen, M.E.10
  • 39
    • 0026345997 scopus 로고
    • Colchicine intoxication: clinical pharmacology, risk factors, features, and management
    • Putterman C., Ben-Chetrit E., Caraco Y., Levy M. Colchicine intoxication: clinical pharmacology, risk factors, features, and management. Semin. Arthritis Rheum. 1991, 21:143-155.
    • (1991) Semin. Arthritis Rheum. , vol.21 , pp. 143-155
    • Putterman, C.1    Ben-Chetrit, E.2    Caraco, Y.3    Levy, M.4
  • 41
    • 34547735974 scopus 로고    scopus 로고
    • Fusion of a recombinant antibody fragment with a homo-amino-acid polymer: effects on biophysical properties and prolonged plasma half-life
    • Schlapschy M., Theobald I., Mack H., Schottelius M., Wester H.J., Skerra A. Fusion of a recombinant antibody fragment with a homo-amino-acid polymer: effects on biophysical properties and prolonged plasma half-life. Protein Eng. Des. Sel. 2007, 20:273-284.
    • (2007) Protein Eng. Des. Sel. , vol.20 , pp. 273-284
    • Schlapschy, M.1    Theobald, I.2    Mack, H.3    Schottelius, M.4    Wester, H.J.5    Skerra, A.6
  • 42
    • 0034646561 scopus 로고    scopus 로고
    • A novel type of receptor protein, based on the lipocalin scaffold, with specificity for digoxigenin
    • Schlehuber S., Beste G., Skerra A. A novel type of receptor protein, based on the lipocalin scaffold, with specificity for digoxigenin. J. Mol. Biol. 2000, 297:1105-1120.
    • (2000) J. Mol. Biol. , vol.297 , pp. 1105-1120
    • Schlehuber, S.1    Beste, G.2    Skerra, A.3
  • 43
    • 12844276589 scopus 로고    scopus 로고
    • Lipocalins in drug discovery: from natural ligand-binding proteins to "anticalins"
    • Schlehuber S., Skerra A. Lipocalins in drug discovery: from natural ligand-binding proteins to "anticalins". Drug Discov. Today 2005, 10:23-33.
    • (2005) Drug Discov. Today , vol.10 , pp. 23-33
    • Schlehuber, S.1    Skerra, A.2
  • 44
    • 34250766201 scopus 로고    scopus 로고
    • The Strep-tag system for one-step purification and high-affinity detection or capturing of proteins
    • Schmidt T.G., Skerra A. The Strep-tag system for one-step purification and high-affinity detection or capturing of proteins. Nat. Protoc. 2007, 2:1528-1535.
    • (2007) Nat. Protoc. , vol.2 , pp. 1528-1535
    • Schmidt, T.G.1    Skerra, A.2
  • 46
    • 0034684235 scopus 로고    scopus 로고
    • Lipocalins as a scaffold
    • Skerra A. Lipocalins as a scaffold. Biochim. Biophys. Acta 2000, 1482:337-350.
    • (2000) Biochim. Biophys. Acta , vol.1482 , pp. 337-350
    • Skerra, A.1
  • 47
    • 0344033650 scopus 로고    scopus 로고
    • Imitating the humoral immune response
    • Skerra A. Imitating the humoral immune response. Curr. Opin. Chem. Biol. 2003, 7:683-693.
    • (2003) Curr. Opin. Chem. Biol. , vol.7 , pp. 683-693
    • Skerra, A.1
  • 48
    • 0017756477 scopus 로고
    • Antibody-hapten reaction kinetics: a comparison of hapten interactions with IgG and Fab preparations
    • Skubitz K.M., O'Hara D.S., Smith T.W. Antibody-hapten reaction kinetics: a comparison of hapten interactions with IgG and Fab preparations. J. Immunol. 1977, 118:1971-1976.
    • (1977) J. Immunol. , vol.118 , pp. 1971-1976
    • Skubitz, K.M.1    O'Hara, D.S.2    Smith, T.W.3
  • 49
    • 0018769879 scopus 로고
    • Immunogenicity and kinetics of distribution and elimination of sheep digoxin-specific IgG and Fab fragments in the rabbit and baboon
    • Smith T.W., Lloyd B.L., Spicer N., Haber E. Immunogenicity and kinetics of distribution and elimination of sheep digoxin-specific IgG and Fab fragments in the rabbit and baboon. Clin. Exp. Immunol. 1979, 36:384-396.
    • (1979) Clin. Exp. Immunol. , vol.36 , pp. 384-396
    • Smith, T.W.1    Lloyd, B.L.2    Spicer, N.3    Haber, E.4
  • 51
    • 0024318983 scopus 로고
    • An update on digoxin
    • Stone J.A., Soldin S.J. An update on digoxin. Clin. Chem. 1989, 35:1326-1331.
    • (1989) Clin. Chem. , vol.35 , pp. 1326-1331
    • Stone, J.A.1    Soldin, S.J.2
  • 53
    • 0020626895 scopus 로고
    • Comparison of digoxin-induced cardiac toxicity in resistant and sensitive species
    • Weinhouse E., Kaplanski J., Posner J. Comparison of digoxin-induced cardiac toxicity in resistant and sensitive species. J. Pharm. Pharmacol. 1983, 35:580-583.
    • (1983) J. Pharm. Pharmacol. , vol.35 , pp. 580-583
    • Weinhouse, E.1    Kaplanski, J.2    Posner, J.3


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