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Volumn 65, Issue 2, 2016, Pages 147-155

Pharmacokinetics of 1-methyl-L-tryptophan after single and repeated subcutaneous application in a porcine model

Author keywords

3 dioxygenase; Indoleamine 2; Methyltryptophan; Pharmacokinetics; Pig; Tryptophan

Indexed keywords

INDOXIMOD; N METHYLTRYPTOPHAN; 1-METHYLTRYPTOPHAN; ENZYME INHIBITOR; INDOLEAMINE 2,3 DIOXYGENASE; TRYPTOPHAN;

EID: 84969581242     PISSN: 13411357     EISSN: None     Source Type: Journal    
DOI: 10.1538/expanim.15-0096     Document Type: Article
Times cited : (11)

References (37)
  • 1
    • 77953927410 scopus 로고    scopus 로고
    • Advances in porcine genomics and proteomics - a toolbox for developing the pig as a model organism for molecular biomedical research
    • Bendixen, E., Danielsen, M., Larsen, K., and Bendixen, C. 2010. Advances in porcine genomics and proteomics - a toolbox for developing the pig as a model organism for molecular biomedical research. Brief. Funct. Genomics 9: 208-219
    • (2010) Brief. Funct. Genomics , vol.9 , pp. 208-219
    • Bendixen, E.1    Danielsen, M.2    Larsen, K.3    Bendixen, C.4
  • 2
    • 0026347919 scopus 로고
    • 1-Methyl-DL-tryptophan, beta-(3-benzofuranyl)-DL-alanine (the oxygen analog of tryptophan), and beta-[3-benzo(b)thienyl]-DL-alanine (the sulfur analog of tryptophan) are competitive inhibitors for indoleamine 2,3-dioxygenase
    • Cady, S.G. and Sono, M. 1991. 1-Methyl-DL-tryptophan, beta-(3-benzofuranyl)-DL-alanine (the oxygen analog of tryptophan), and beta-[3-benzo(b)thienyl]-DL-alanine (the sulfur analog of tryptophan) are competitive inhibitors for indoleamine 2,3-dioxygenase. Arch. Biochem. Biophys. 291: 326-333
    • (1991) Arch. Biochem. Biophys , vol.291 , pp. 326-333
    • Cady, S.G.1    Sono, M.2
  • 3
    • 66049126424 scopus 로고    scopus 로고
    • Indoleamine 2,3 dioxygenase-mediated tryptophan catabolism regulates accumulation of Th1/Th17 cells in the joint in collagen-induced arthritis
    • Criado, G., Simelyte, E., Inglis, J.J., Essex, D., and Williams, R.O. 2009. Indoleamine 2,3 dioxygenase-mediated tryptophan catabolism regulates accumulation of Th1/Th17 cells in the joint in collagen-induced arthritis. Arthritis Rheum. 60: 1342-1351
    • (2009) Arthritis Rheum , vol.60 , pp. 1342-1351
    • Criado, G.1    Simelyte, E.2    Inglis, J.J.3    Essex, D.4    Williams, R.O.5
  • 7
    • 0345424863 scopus 로고    scopus 로고
    • Bioanalytical Method Validation: Analytical methods validation
    • Food and Drug Administration (FDA). 2013. Guidance for Industry. Bioanalytical Method Validation: Analytical methods validation.
    • (2013) Guidance for Industry
  • 8
    • 38649099395 scopus 로고    scopus 로고
    • Immunosuppression routed via the kynurenine pathway: A biochemical and pathophysiologic approach
    • Gonzalez, A., Varo, N., Alegre, E., Diaz, A., and Melero, I. 2008. Immunosuppression routed via the kynurenine pathway: a biochemical and pathophysiologic approach. Adv. Clin. Chem. 45: 155-197
    • (2008) Adv. Clin. Chem , vol.45 , pp. 155-197
    • Gonzalez, A.1    Varo, N.2    Alegre, E.3    Diaz, A.4    Melero, I.5
  • 9
    • 84969511779 scopus 로고    scopus 로고
    • date of access: 16.09.2015
    • Health USNIo. https://www.clinicaltrials.gov/ct2/results?term=1-methyl-D-Tryptophan&Search=Search date of access: 16.09.2015.
  • 10
    • 85052029591 scopus 로고    scopus 로고
    • date of access: 16.09.2015
    • Health USNIo. https://www.clinicaltrials.gov/ct2/show/results/NCT01042535?term=1-methyl-D-Tryptophan&rank=1§=Xb70156 date of access: 16.09.2015.
  • 11
    • 33846689594 scopus 로고    scopus 로고
    • Inhibition of indoleamine 2,3-dioxygen-ase in dendritic cells by stereoisomers of 1-methyl-trypto-phan correlates with antitumor responses
    • Hou, D.Y., Muller, A.J., Sharma, M.D., DuHadaway, J., Ba-nerjee, T., Johnson, M., Mellor, A.L., Prendergast, G.C., and Munn, D.H. 2007. Inhibition of indoleamine 2,3-dioxygen-ase in dendritic cells by stereoisomers of 1-methyl-trypto-phan correlates with antitumor responses. Cancer Res. 67: 792-801
    • (2007) Cancer Res , vol.67 , pp. 792-801
    • Hou, D.Y.1    Muller, A.J.2    Sharma, M.D.3    Duhadaway, J.4    Ba-Nerjee, T.5    Johnson, M.6    Mellor, A.L.7    Prendergast, G.C.8    Munn, D.H.9
  • 13
    • 0037227770 scopus 로고    scopus 로고
    • Carbendazim: Disposition, cellular permeability, metabolite identification, and pharmacokinetic comparison with its nanoparticle
    • Jia, L., Wong, H., Wang, Y., Garza, M., and Weitman, S.D. 2003. Carbendazim: disposition, cellular permeability, metabolite identification, and pharmacokinetic comparison with its nanoparticle. J. Pharm. Sci. 92: 161-172
    • (2003) J. Pharm. Sci , vol.92 , pp. 161-172
    • Jia, L.1    Wong, H.2    Wang, Y.3    Garza, M.4    Weitman, S.D.5
  • 16
    • 52449118755 scopus 로고    scopus 로고
    • Interaction of tryptophan derivatives with SLC6A14 (ATB0,+) reveals the potential of the transporter as a drug target for cancer chemotherapy
    • Karunakaran, S., Umapathy, N.S., Thangaraju, M., Hat-anaka, T., Itagaki, S., Munn, D.H., Prasad, P.D., and Ga-napathy, V. 2008. Interaction of tryptophan derivatives with SLC6A14 (ATB0,+) reveals the potential of the transporter as a drug target for cancer chemotherapy. Biochem. J. 414: 343-355
    • (2008) Biochem. J , vol.414 , pp. 343-355
    • Karunakaran, S.1    Umapathy, N.S.2    Thangaraju, M.3    Hat-Anaka, T.4    Itagaki, S.5    Munn, D.H.6    Prasad, P.D.7    Ga-Napathy, V.8
  • 17
    • 77955648350 scopus 로고    scopus 로고
    • Psychological stress-induced, IDO1-dependent tryptophan catabolism: Implications on immunosuppression in mice and humans
    • Kiank, C., Zeden, J.P., Drude, S., Domanska, G., Fusch, G., Otten, W., and Schuett, C. 2010. Psychological stress-induced, IDO1-dependent tryptophan catabolism: implications on immunosuppression in mice and humans. PLoS ONE 5: e11825
    • (2010) Plos ONE , vol.5
    • Kiank, C.1    Zeden, J.P.2    Drude, S.3    Domanska, G.4    Fusch, G.5    Otten, W.6    Schuett, C.7
  • 18
    • 84889483786 scopus 로고    scopus 로고
    • In vitro evaluation of metabolic drug-drug interactions: Concepts and practice
    • Li, A.PWiley, Hoboken
    • Li, A.P. 2007. In vitro evaluation of metabolic drug-drug interactions: concepts and practice. pp. 1-30. In: Drug-drug interaction in pharmaceutical development (Li, A.P. ed.), Wiley, Hoboken.
    • (2007) Drug-Drug Interaction in Pharmaceutical Development , pp. 1-30
    • Li, A.P.1
  • 20
    • 74849101015 scopus 로고    scopus 로고
    • Indoleamine 2,3-dioxygenase, an emerging target for anti-cancer therapy
    • Liu, X., Newton, R.C., Friedman, S.M., and Scherle, P.A. 2009. Indoleamine 2,3-dioxygenase, an emerging target for anti-cancer therapy. Curr. Cancer Drug Targets 9: 938-952
    • (2009) Curr. Cancer Drug Targets , vol.9 , pp. 938-952
    • Liu, X.1    Newton, R.C.2    Friedman, S.M.3    Scherle, P.A.4
  • 21
    • 54849418903 scopus 로고    scopus 로고
    • IDO1 and IDO2 are expressed in human tumors: Levobut not dextro-1-methyl tryptophan inhibits tryptophan catabolism. Cancer Immunol
    • Lob, S., Konigsrainer, A., Zieker, D., Brucher, B.L., Ram-mensee, H.G., Opelz, G., and Terness, P. 2009. IDO1 and IDO2 are expressed in human tumors: levobut not dextro-1-methyl tryptophan inhibits tryptophan catabolism. Cancer Immunol. Immunother. 58: 153-157
    • (2009) Immunother , vol.58 , pp. 153-157
    • Lob, S.1    Konigsrainer, A.2    Zieker, D.3    Brucher, B.L.4    Ram-Mensee, H.G.5    Opelz, G.6    Terness, P.7
  • 22
    • 41349088840 scopus 로고    scopus 로고
    • Levobut not dextro-1-methyl tryptophan abrogates the IDO activity of human dendritic cells
    • Lob, S., Konigsrainer, A., Schafer, R., Rammensee, H.G., Opelz, G., and Terness, P. 2008. Levobut not dextro-1-methyl tryptophan abrogates the IDO activity of human dendritic cells. Blood 111: 2152-2154
    • (2008) Blood , vol.111 , pp. 2152-2154
    • Lob, S.1    Konigsrainer, A.2    Schafer, R.3    Rammensee, H.G.4    Opelz, G.5    Terness, P.6
  • 24
    • 83555173607 scopus 로고    scopus 로고
    • Factors influencing the use and interpretation of animal models in the development of parenteral drug delivery systems
    • Martinez, M.N. 2011. Factors influencing the use and interpretation of animal models in the development of parenteral drug delivery systems. AAPS J. 13: 632-649
    • (2011) AAPS J , vol.13 , pp. 632-649
    • Martinez, M.N.1
  • 27
    • 16244408626 scopus 로고    scopus 로고
    • Inhibition of indoleamine 2,3-dioxygenase, an immunoregulatory target of the cancer suppression gene Bin1, potentiates cancer chemotherapy
    • Muller, A.J., DuHadaway, J.B., Donover, P.S., Sutanto-Ward, E., and Prendergast, G.C. 2005. Inhibition of indoleamine 2,3-dioxygenase, an immunoregulatory target of the cancer suppression gene Bin1, potentiates cancer chemotherapy. Nat. Med. 11: 312-319
    • (2005) Nat. Med , vol.11 , pp. 312-319
    • Muller, A.J.1    Duhadaway, J.B.2    Donover, P.S.3    Sutanto-Ward, E.4    Prendergast, G.C.5
  • 29
    • 0021011171 scopus 로고
    • Chronical venous catheterization for frequent blood sampling in unrestrained pigs
    • Rodriguez, H. and Kunavongkrit, A. 1983. Chronical venous catheterization for frequent blood sampling in unrestrained pigs. Acta Vet. Scand. 24: 318-320
    • (1983) Acta Vet. Scand , vol.24 , pp. 318-320
    • Rodriguez, H.1    Kunavongkrit, A.2
  • 30
    • 84879793564 scopus 로고    scopus 로고
    • Assessment of juvenile pigs to serve as human pediatric surrogates for preclinical formulation pharmacokinetic testing
    • Roth, W.J., Kissinger, C.B., McCain, R.R., Cooper, B.R., Marchant-Forde, J.N., Vreeman, R.C., Hannou, S., and Knipp, G.T. 2013. Assessment of juvenile pigs to serve as human pediatric surrogates for preclinical formulation pharmacokinetic testing. AAPS J. 15: 763-774
    • (2013) AAPS J , vol.15 , pp. 763-774
    • Roth, W.J.1    Kissinger, C.B.2    McCain, R.R.3    Cooper, B.R.4    Marchant-Forde, J.N.5    Vreeman, R.C.6    Hannou, S.7    Knipp, G.T.8
  • 31
    • 0037080320 scopus 로고    scopus 로고
    • Determination of drug-plasma protein binding kinetics and equilibria by chromatographic profiling: Exemplification of the method using L-tryptophan and albumin
    • Talbert, A.M., Tranter, G.E., Holmes, E., and Francis, P.L. 2002. Determination of drug-plasma protein binding kinetics and equilibria by chromatographic profiling: exemplification of the method using L-tryptophan and albumin. Anal. Chem. 74: 446-452
    • (2002) Anal. Chem , vol.74 , pp. 446-452
    • Talbert, A.M.1    Tranter, G.E.2    Holmes, E.3    Francis, P.L.4
  • 32
    • 27544499713 scopus 로고    scopus 로고
    • Biochemical and medical aspects of the indoleamine 2,3-dioxygenase-initiated L-tryptophan metabolism
    • Takikawa, O. 2005. Biochemical and medical aspects of the indoleamine 2,3-dioxygenase-initiated L-tryptophan metabolism. Biochem. Biophys. Res. Commun. 338: 12-19
    • (2005) Biochem. Biophys. Res. Commun , vol.338 , pp. 12-19
    • Takikawa, O.1
  • 33
    • 0142137237 scopus 로고    scopus 로고
    • Evidence for a tumoral immune resistance mechanism based on tryptophan degradation by indoleamine 2,3-dioxygenase
    • Uyttenhove, C., Pilotte, L., Theate, I., Stroobant, V., Colau, D., Parmentier, N., Boon, T., and Van den Eynde, B.J. 2003. Evidence for a tumoral immune resistance mechanism based on tryptophan degradation by indoleamine 2,3-dioxygenase. Nat. Med. 9: 1269-1274
    • (2003) Nat. Med , vol.9 , pp. 1269-1274
    • Uyttenhove, C.1    Pilotte, L.2    Theate, I.3    Stroobant, V.4    Colau, D.5    Parmentier, N.6    Boon, T.7    Van Den Eynde, B.J.8
  • 35
    • 77953802515 scopus 로고    scopus 로고
    • A combination of the metabolic enzyme inhibitor APO866 and the immune adjuvant L-1-methyl tryptophan induces additive antitumor activity
    • Yang, H.J., Yen, M.C., Lin, C.C., Lin, C.M., Chen, Y.L., Weng, T.Y., Huang, T.T., Wu, C.L., and Lai, M.D. 2010. A combination of the metabolic enzyme inhibitor APO866 and the immune adjuvant L-1-methyl tryptophan induces additive antitumor activity. Exp. Biol. Med. (Maywood) 235: 869-876
    • (2010) Exp. Biol. Med. (Maywood) , vol.235 , pp. 869-876
    • Yang, H.J.1    Yen, M.C.2    Lin, C.C.3    Lin, C.M.4    Chen, Y.L.5    Weng, T.Y.6    Huang, T.T.7    Wu, C.L.8    Lai, M.D.9
  • 36
    • 0030897401 scopus 로고    scopus 로고
    • Effect of mobile phase composition on the binding kinetics of chiral solutes on a protein-based high-performance liquid chromatography column: Interactions of D-and L-tryptophan with immobilized human serum albumin
    • Yang, J. and Hage, D.S. 1997. Effect of mobile phase composition on the binding kinetics of chiral solutes on a protein-based high-performance liquid chromatography column: interactions of D-and L-tryptophan with immobilized human serum albumin. J. Chromatogr. A 766: 15-25
    • (1997) J. Chromatogr. A , vol.766 , pp. 15-25
    • Yang, J.1    Hage, D.S.2
  • 37
    • 0028299106 scopus 로고
    • Release and absorption rates of intramuscularly and subcutaneously injected pharmaceuticals
    • Zuidema, J., Kadir, F., Titulaer, H.A.C., and Oussoren, C. 1994. Release and absorption rates of intramuscularly and subcutaneously injected pharmaceuticals. Int. J. Pharm. 105: 189-207
    • (1994) Int. J. Pharm , vol.105 , pp. 189-207
    • Zuidema, J.1    Kadir, F.2    Titulaer, H.A.C.3    Oussoren, C.4


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