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Volumn 50, Issue 3, 2007, Pages 480-488

Influence of conformation and intramolecular hydrogen bonding on the acyl glucuronidation and biliary excretion of acetylenic bis-dipyrrinones related to bilirubin

Author keywords

[No Author keywords available]

Indexed keywords

ACETYLENE DERIVATIVE; ALKYL GROUP; BILIRUBIN; BILIRUBIN DERIVATIVE; BILIVERDIN; CARBOXYL GROUP; DICARBOXYLIC ACID DERIVATIVE; GLUCURONOSYLTRANSFERASE; MULTIDRUG RESISTANCE PROTEIN 2; PYRROLE DERIVATIVE; TETRAPYRROLE DERIVATIVE;

EID: 33846901538     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm0609521     Document Type: Article
Times cited : (25)

References (30)
  • 1
    • 0027141121 scopus 로고
    • Solvent-dependent conformation and hydrogen-bonding capacity of cyclosporin A: Evidence from partition coefficients and molecular dynamics simulations
    • el Tayar, N.; Mark, A. E.; Vallat, P.; Brunne, R. M.; Testa, B.; van Gunsteren, W. F. Solvent-dependent conformation and hydrogen-bonding capacity of cyclosporin A: evidence from partition coefficients and molecular dynamics simulations. J. Med. Chem. 1993, 36, 3757-3764.
    • (1993) J. Med. Chem , vol.36 , pp. 3757-3764
    • el Tayar, N.1    Mark, A.E.2    Vallat, P.3    Brunne, R.M.4    Testa, B.5    van Gunsteren, W.F.6
  • 2
    • 0030629822 scopus 로고    scopus 로고
    • Bilirubin metabolism and kernicterus
    • Gourley, G. R. Bilirubin metabolism and kernicterus. Adv. Pediatr. 1997, 44, 173-229.
    • (1997) Adv. Pediatr , vol.44 , pp. 173-229
    • Gourley, G.R.1
  • 3
    • 30144437158 scopus 로고    scopus 로고
    • UDP-glucuronosyltransferases: Gene structures of UGT1 and UGT2 families
    • Owens, I. S.; Basu, N. K.; Banerjee, R. UDP-glucuronosyltransferases: gene structures of UGT1 and UGT2 families. Methods Enzymol. 2005, 400, 1-22.
    • (2005) Methods Enzymol , vol.400 , pp. 1-22
    • Owens, I.S.1    Basu, N.K.2    Banerjee, R.3
  • 4
    • 0032698874 scopus 로고    scopus 로고
    • ABC transporters are both enzymes and membrane transporters. In the nomenclature introduced by Holland and Blight the term allocrite refers to compounds whose passage across membranes is facilitated by an ABC tranporter: Holland, I. B.; Blight, M. A. ABC-ATPases, adaptable energy generators fuelling transmembrane movement of a variety of molecules in organisms from bacteria to humans. J. Mol. Biol. 1999, 293, 381-399.
    • ABC transporters are both enzymes and membrane transporters. In the nomenclature introduced by Holland and Blight the term "allocrite" refers to compounds whose passage across membranes is facilitated by an ABC tranporter: Holland, I. B.; Blight, M. A. ABC-ATPases, adaptable energy generators fuelling transmembrane movement of a variety of molecules in organisms from bacteria to humans. J. Mol. Biol. 1999, 293, 381-399.
  • 5
    • 0344665555 scopus 로고    scopus 로고
    • Dietrich, C. G.; Geier, A.; Oude, Elferink, R. J. P. ABC of oral bioavailability: transporters as gatekeepers in the gut. Gut 2003, 52, 1788-1795.
    • Dietrich, C. G.; Geier, A.; Oude, Elferink, R. J. P. ABC of oral bioavailability: transporters as gatekeepers in the gut. Gut 2003, 52, 1788-1795.
  • 6
    • 33847080622 scopus 로고    scopus 로고
    • The apical conjugate efflux pump ABCC2 (MRP2)
    • in press
    • Nies, A. T.; Keppler, D. The apical conjugate efflux pump ABCC2 (MRP2). Pfluegers Arch., in press.
    • Pfluegers Arch
    • Nies, A.T.1    Keppler, D.2
  • 7
    • 3542995726 scopus 로고    scopus 로고
    • The complexities of hepatic drug transport: Current knowledge and emerging concepts
    • Chandra, P.; Brouwer, K. L. The complexities of hepatic drug transport: current knowledge and emerging concepts. Pharm. Res. 2004, 21, 719-35.
    • (2004) Pharm. Res , vol.21 , pp. 719-735
    • Chandra, P.1    Brouwer, K.L.2
  • 9
    • 0017844381 scopus 로고
    • Structure of di-isopropylammonium bilirubinate
    • Mugnoli, A.; Manitto, P.; Monti, D. Structure of di-isopropylammonium bilirubinate. Nature 1978, 273, 568-569.
    • (1978) Nature , vol.273 , pp. 568-569
    • Mugnoli, A.1    Manitto, P.2    Monti, D.3
  • 10
    • 30444438168 scopus 로고    scopus 로고
    • Crystal structure of phycocyanobilin:ferredoxin oxidoreductase in complex with biliverdin IXα, a key enzyme in the biosynthesis of phycocyanobilin
    • Hagiwara, Y.; Sugishima, M.; Takahashi, Y.; Fukuyama, K. Crystal structure of phycocyanobilin:ferredoxin oxidoreductase in complex with biliverdin IXα, a key enzyme in the biosynthesis of phycocyanobilin. Proc. Natl. Acad. Sci. U.S.A. 2006, 103, 27-32.
    • (2006) Proc. Natl. Acad. Sci. U.S.A , vol.103 , pp. 27-32
    • Hagiwara, Y.1    Sugishima, M.2    Takahashi, Y.3    Fukuyama, K.4
  • 11
    • 0028958953 scopus 로고
    • Structure determination of the biliverdin apomyoglobin complex: Crystal structure analysis of two crystal forms at 1.4 and 1.5 Å resolution
    • Wagner, U. G.; Müller, N.; Schmitzberger, W.; Falk, H.; Kratky, C. Structure determination of the biliverdin apomyoglobin complex: Crystal structure analysis of two crystal forms at 1.4 and 1.5 Å resolution. J. Mol. Biol. 1995, 247, 326-337.
    • (1995) J. Mol. Biol , vol.247 , pp. 326-337
    • Wagner, U.G.1    Müller, N.2    Schmitzberger, W.3    Falk, H.4    Kratky, C.5
  • 14
    • 0031810176 scopus 로고    scopus 로고
    • Probing the conformation of bilirubins with monopropionic analogs: A biological, spectroscopic, and molecular modeling study
    • Kogan, M. J.; Mora, M. E.; Awruch, J.; Delfino, J. M. Probing the conformation of bilirubins with monopropionic analogs: a biological, spectroscopic, and molecular modeling study. Bioorg. Med. Chem. 1998, 6, 151-161.
    • (1998) Bioorg. Med. Chem , vol.6 , pp. 151-161
    • Kogan, M.J.1    Mora, M.E.2    Awruch, J.3    Delfino, J.M.4
  • 16
    • 33846910329 scopus 로고    scopus 로고
    • 2 linkage.
    • 2 linkage.
  • 18
    • 33845377321 scopus 로고    scopus 로고
    • Houk, K. N.; Scott, L. T.; Rondan, N. G.; Spellmeyer, D. C.; Reinhardt, G.; Hyun, J. L.; Decicco, G. J.; Weiss, R.; Chen, M. H. M.; Bass, L. S.; Clardy, J.; Jørgensen, F. S.; Eaton, T. A.; Sarkozi, V.; Petit, C. M.; Ng, L.; Jordan, K. D. Pericyclynes: exploded cycloalkanes with unusual orbital interactions and conformational properties. Mm2 and Sto-3G calculations, X-ray crystal-structures, photoelectron-spectra, and electron transmission spectra. J. Am. Chem. Soc. 1985, 107, 6556-6562.
    • (c) Houk, K. N.; Scott, L. T.; Rondan, N. G.; Spellmeyer, D. C.; Reinhardt, G.; Hyun, J. L.; Decicco, G. J.; Weiss, R.; Chen, M. H. M.; Bass, L. S.; Clardy, J.; Jørgensen, F. S.; Eaton, T. A.; Sarkozi, V.; Petit, C. M.; Ng, L.; Jordan, K. D. Pericyclynes: exploded cycloalkanes with unusual orbital interactions and conformational properties. Mm2 and Sto-3G calculations, X-ray crystal-structures, photoelectron-spectra, and electron transmission spectra. J. Am. Chem. Soc. 1985, 107, 6556-6562.
  • 19
    • 0242660830 scopus 로고    scopus 로고
    • Tu, B.; Ghosh, B.; Lightner, D. A. A new class of linear tetrapyrroles: acetylenic 10,10a-didehydro-10a-homobilirubins. J. Org. Chem. 2003, 68, 8950-8963.
    • Tu, B.; Ghosh, B.; Lightner, D. A. A new class of linear tetrapyrroles: acetylenic 10,10a-didehydro-10a-homobilirubins. J. Org. Chem. 2003, 68, 8950-8963.
  • 20
    • 2442428089 scopus 로고    scopus 로고
    • Novel linear tetrapyrroles: Hydrogen bonding in diacetylenic bilirubins
    • Tu, B.; Ghosh, B.; Lightner, D. A. Novel linear tetrapyrroles: hydrogen bonding in diacetylenic bilirubins. Monatsh. Chem. 2004, 135, 519-541.
    • (2004) Monatsh. Chem , vol.135 , pp. 519-541
    • Tu, B.1    Ghosh, B.2    Lightner, D.A.3
  • 21
    • 0033552261 scopus 로고    scopus 로고
    • Synthesis of a 10-oxo-bilirubin. Effects of the oxo group on conformation, transhepatic transport and glucuronidation
    • Chen, Q.; Huggins, M. T.; Lightner, D. L.; Norona, W.; McDonagh, A. F. Synthesis of a 10-oxo-bilirubin. Effects of the oxo group on conformation, transhepatic transport and glucuronidation. J. Am. Chem. Soc. 1999, 121, 9253-9264.
    • (1999) J. Am. Chem. Soc , vol.121 , pp. 9253-9264
    • Chen, Q.1    Huggins, M.T.2    Lightner, D.L.3    Norona, W.4    McDonagh, A.F.5
  • 22
    • 0001373940 scopus 로고    scopus 로고
    • Conformational analysis of symmetric bilirubin analogues with varying length alkanoic acids. Enantioselectivity by human serum albumin
    • Trull, F. R.; Person, R. V.; Lightner, D. A. Conformational analysis of symmetric bilirubin analogues with varying length alkanoic acids. Enantioselectivity by human serum albumin. J. Chem. Soc., Perkin Trans. 2 1997, 1241-1250.
    • (1997) J. Chem. Soc., Perkin Trans. 2 , pp. 1241-1250
    • Trull, F.R.1    Person, R.V.2    Lightner, D.A.3
  • 23
    • 0027115591 scopus 로고
    • Isolation and characterisation of a new hepatic bilirubin UDP-glucuronosyltransferase: Absence from Gunn rat liver
    • Clarke, D. J.; Keen, J. N.; Burchell, B. Isolation and characterisation of a new hepatic bilirubin UDP-glucuronosyltransferase: Absence from Gunn rat liver. FEBS Lett. 1992, 299, 183-186.
    • (1992) FEBS Lett , vol.299 , pp. 183-186
    • Clarke, D.J.1    Keen, J.N.2    Burchell, B.3
  • 24
    • 0025744087 scopus 로고
    • Genetic defect of bilirubin UDP-glucuronosyltransferase in the hyperbilirubinemic Gunn rat
    • Sato, H.; Aono, S.; Kashiwamata, S.; Koiwai, O. Genetic defect of bilirubin UDP-glucuronosyltransferase in the hyperbilirubinemic Gunn rat. Biochem. Biophys. Res. Commun. 1991, 177, 1161-1164.
    • (1991) Biochem. Biophys. Res. Commun , vol.177 , pp. 1161-1164
    • Sato, H.1    Aono, S.2    Kashiwamata, S.3    Koiwai, O.4
  • 25
    • 0021804301 scopus 로고
    • Hereditary chronic conjugated hyperbilirubinemia in mutant rats caused by defective hepatic anion transport
    • Jansen, P. L.; Peters, W. H.; Lamers, W. H. Hereditary chronic conjugated hyperbilirubinemia in mutant rats caused by defective hepatic anion transport. Hepatology 1985, 5, 573-579.
    • (1985) Hepatology , vol.5 , pp. 573-579
    • Jansen, P.L.1    Peters, W.H.2    Lamers, W.H.3
  • 26
    • 0030814774 scopus 로고    scopus 로고
    • The canalicular multispecific organic anion transporter and conjugated hyperbilirubinemia in rat and man
    • Paulusma, C. C.; Oude Elferink, R. P. J. The canalicular multispecific organic anion transporter and conjugated hyperbilirubinemia in rat and man. J. Mol. Med. 1997, 75, 420-428.
    • (1997) J. Mol. Med , vol.75 , pp. 420-428
    • Paulusma, C.C.1    Oude Elferink, R.P.J.2
  • 27
    • 0028280962 scopus 로고
    • Bilirubin conformational analysis and circular dichroism
    • Person, R. V.; Peterson, B. R.; Lightner, D. A. Bilirubin conformational analysis and circular dichroism. J. Am. Chem. Soc. 1994, 116, 42-59.
    • (1994) J. Am. Chem. Soc , vol.116 , pp. 42-59
    • Person, R.V.1    Peterson, B.R.2    Lightner, D.A.3
  • 28
    • 0001614291 scopus 로고
    • Phototherapy for neonatal jaundice. Configurational isomers of bilirubin
    • McDonagh, A. F.; Palma, L. A.; Trull, F. R.; Lightner, D. A. Phototherapy for neonatal jaundice. Configurational isomers of bilirubin. J. Am. Chem. Soc. 1982, 104, 6865-6867.
    • (1982) J. Am. Chem. Soc , vol.104 , pp. 6865-6867
    • McDonagh, A.F.1    Palma, L.A.2    Trull, F.R.3    Lightner, D.A.4
  • 29
    • 0344532816 scopus 로고
    • Molecular mechanisms of phototherapy for neonatal jaundice
    • Lightner, D. A.; McDonagh, A. F. Molecular mechanisms of phototherapy for neonatal jaundice. Acc. Chem. Res. 1984, 17, 417-424.
    • (1984) Acc. Chem. Res , vol.17 , pp. 417-424
    • Lightner, D.A.1    McDonagh, A.F.2
  • 30
    • 26844553565 scopus 로고    scopus 로고
    • Synthesis and hepatic transport of strongly fluorescent cholephilic dipyrrinones
    • Woydziak, Z. R.; Boiadjiev, S. E.; Norona, W. S.; McDonagh, A. F.; Lightner, D. A. Synthesis and hepatic transport of strongly fluorescent cholephilic dipyrrinones. J. Org. Chem. 2005, 70, 8417-8423.
    • (2005) J. Org. Chem , vol.70 , pp. 8417-8423
    • Woydziak, Z.R.1    Boiadjiev, S.E.2    Norona, W.S.3    McDonagh, A.F.4    Lightner, D.A.5


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