Congenital jaundice in rats with a mutation in a multidrug resistance-associated protein gene

Science

Volumn 271, Issue 5252, 1996, Pages 1126-1128

  Paulusma, Coen C ^a   Bosma, Piter J ^a   Zaman, Guido J R ^b   Bakker, Conny T M ^a   Otter, Marlies ^a   Scheffer, George L ^c   Scheper, Rik J ^c   Borst, Piet ^b   Oude Elferink, Ronald P J ^a  

^a ACADEMIC MEDICAL CENTER   (Netherlands)

^b NETHERLANDS CANCER INSTITUTE   (Netherlands)

^c VU UNIVERSITY MEDICAL CENTER   (Netherlands)

Author keywords

[No Author keywords available]

Indexed keywords

BILIRUBIN; COMPLEMENTARY DNA; MESSENGER RNA;

ANIMAL MODEL; ARTICLE; CELL MEMBRANE; DELETION MUTANT; DUBIN JOHNSON SYNDROME; GENE MUTATION; HYPERBILIRUBINEMIA; JAUNDICE; LIVER CELL; MULTIDRUG RESISTANCE; NONHUMAN; PRIORITY JOURNAL; RAT;

EID: 0029981430     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.271.5252.1126     Document Type: Article

References (39)

1. R. P. J. Oude Elferink et al., Am J. Physiol. 258, G699 (1990), T. Kitamura et al., Proc. Natl. Acad. Sci U.S A 87, 3557 (1990); R. P J. Oude Elferink et al , Biochim. Biophys. Acta. 1241, 215 (1995).
2. R. P. J. Oude Elferink et al., Am J. Physiol. 258, G699 (1990), T. Kitamura et al., Proc. Natl. Acad. Sci U.S A 87, 3557 (1990); R. P J. Oude Elferink et al , Biochim. Biophys. Acta. 1241, 215 (1995).
3. R. P. J. Oude Elferink et al., Am J. Physiol. 258, G699 (1990), T. Kitamura et al., Proc. Natl. Acad. Sci U.S A 87, 3557 (1990); R. P J. Oude Elferink et al , Biochim. Biophys. Acta. 1241, 215 (1995).
4. P. L. M. Jansen, W H. M Peters, W. H Lamers, Hepatology 5, 573 (1985)
5. P. L. M. Jansen, W H. M Peters, D. K. F Meijer, Gastroenterology 93, 1094 (1987); T Nishida, Z Gatmaitan, J. Roy-Chowdhury, I. M Arias, J Clin Invest 90, 2130 (1992).
6. P. L. M. Jansen, W H. M Peters, D. K. F Meijer, Gastroenterology 93, 1094 (1987); T Nishida, Z Gatmaitan, J. Roy-Chowdhury, I. M Arias, J Clin Invest 90, 2130 (1992).
7. M Huber, A. Guhlmann, P. L. M. Jansen, D. Keppler, Hepatology 7, 224 (1987); T. Ishikawa, M. Müller, C. Klunemann, C Schaub, D Keppler, J. Biol Chem. 265, 19279 (1990); R. P J. Oude Elferink, J. de Haan, K Lambert, A F Hofmann, P. L. M Jansen, Hepatology 7, 1109 (1987); F. Kuipers et al., J. Lipid Res 30, 1835 (1989).
8. M Huber, A. Guhlmann, P. L. M. Jansen, D. Keppler, Hepatology 7, 224 (1987); T. Ishikawa, M. Müller, C. Klunemann, C Schaub, D Keppler, J. Biol Chem. 265, 19279 (1990); R. P J. Oude Elferink, J. de Haan, K Lambert, A F Hofmann, P. L. M Jansen, Hepatology 7, 1109 (1987); F. Kuipers et al., J. Lipid Res 30, 1835 (1989).
9. M Huber, A. Guhlmann, P. L. M. Jansen, D. Keppler, Hepatology 7, 224 (1987); T. Ishikawa, M. Müller, C. Klunemann, C Schaub, D Keppler, J. Biol Chem. 265, 19279 (1990); R. P J. Oude Elferink, J. de Haan, K Lambert, A F Hofmann, P. L. M Jansen, Hepatology 7, 1109 (1987); F. Kuipers et al., J. Lipid Res 30, 1835 (1989).
10. M Huber, A. Guhlmann, P. L. M. Jansen, D. Keppler, Hepatology 7, 224 (1987); T. Ishikawa, M. Müller, C. Klunemann, C Schaub, D Keppler, J. Biol Chem. 265, 19279 (1990); R. P J. Oude Elferink, J. de Haan, K Lambert, A F Hofmann, P. L. M Jansen, Hepatology 7, 1109 (1987); F. Kuipers et al., J. Lipid Res 30, 1835 (1989).
11. S. P. C. Cole et al , Science 258, 1650 (1992)
12. G. Jedlitschky, I. Leier, U. Buchholz, M Center, D. Keppler, Cancer Res 54, 4833 (1994); M. Müller et al., Proc. Natl Acad. Sci. U.S A. 91, 13033 (1994).
13. G. Jedlitschky, I. Leier, U. Buchholz, M Center, D. Keppler, Cancer Res 54, 4833 (1994); M. Müller et al., Proc. Natl Acad. Sci. U.S A. 91, 13033 (1994).
14. G J. R Zaman et al , Cancer Res 53, 1747 (1993)
15. R Evers et al., J. Clin. Invest., in press.
16. M H de Vries et al., Naunyn-Schmiedeberg's Arch. Phamacol 340, 588 (1989)
17. A 213-bp PCR product was obtained from rat lung cDNA after first-round amplification with degenerate primers corresponding to amino acids 678 to 648 (forward) and 770 to 776 (reverse) and subsequent second-round amplification with nested primers corresponding to amino acids 694 to 700 (forward) and 760 to 766 (reverse) of the hMRP1 sequence (5).
18. 4 (pH 7, 0), 2 mM EDTA, and 7% SDS (hybridization solution) for 20 hours. Filters were washed four times in 2× saline sodium citrate (SSC), 1% SDS for 30 min at 65°C and autoradiographed Nucleotide sequences were determined by the dideoxynucleotide chain method [F. Sanger, S Nicklen, A. R. Coulson, Proc. Natl. Acad. Sci. U.S.A. 74, 463 (1977)] The cmoat cDNA sequence has been deposited with Gen Bank (accession number L49379).
19. W. R. Pearson and D. J. Lipman, Proc. Natl. Acad. Sci. U.S.A 85, 2444 (1988)
20. C F. Higgins, Annu. Rev. Cell Biol. 8, 67 (1992).
21. M. S. Szczypka, J A. Wemmie, W. S. Moye-Rowley, D. J. Thiele, J Biol Chem. 269, 22853 (1994).
22. J. R. Riordan et al., Science 245, 1066 (1989).
23. A fusion gene, consisting of the gene for the Escherichia coli maltose-binding protein and the 3′ part of the cmoat cDNA corresponding to amino acids 1340 to 1541, was constructed in pMal-c [C V. Maina et al., Gene 74, 365 (1977)]. The fusion protein was produced in E. coli strain JM101 and purified by amylose resin affinity chromatography. Mice were injected three times during 6 weeks with 200 μg of the purified protein. The first injection was in the presence of Freund's complete adjuvant, and the subsequent boosts in Freund's incomplete adjuvant. Two weeks after the final boost with a glutathioneS-transferase-cMOAT fusion protein, splenocytes were isolated and fused with myeloma cells. Hybridomas were screened by enzyme-linked immunosorbent assay with the glutathione-S-transferase-cMOAT fusion protein and subsequently tested for positivity in protein immunoblots
24. - rat digestion produced two bands of 206 and 66 bp, whereas in the Wistar rats three bands of 83, 122, and 67 bp were observed
25. R. Mayer et al , J. Cell Biol. 131, 137 (1995).
26. J. M Crawford and J. L Gollan, in Disease of the Liver, L. Schiff and E. R. Schiff, Eds. (Lippincott, Philadelphia, ed. 7, 1993), vol. 1, pp. 42-84
27. G. J R. Zaman et al., Proc. Natl. Acad. Sci. U.S.A 91, 8822 (1994)
28. S. P. C. Cole et al., Cancer Res. 54, 5902 (1994)
29. G. J. R. Zaman et al , Proc. Natl. Acad. Sci. U.S.A. 92, 7690 (1995).
30. M. Otter, J. Kuiper, D. Rijken, A. J van Zonneveld, Biochem. Mol Biol. Int 37, 563 (1995).
31. J. Sambrook, E. F. Fritsch, T Maniatis, Molecular Cloning: A Laboratory Manual (Cold Spring Harbor Laboratory, Cold Spring Harbor, NY, 1989).
32. Single-letter abbreviations for the amino acid residuas are as follows: A, Ala; C, Cys; D, Asp; E, Glu; F, Phe; G, Gly; H, His; I, lle; K, Lys; L, Leu; M, Met; N, Asn; P, Pro; Q, Gln; R, Arg; S, Ser; T, Thr; V, Val; W, Trp; and Y, Tyr.
33. J. Devereux et al., Nucleic Acid Res. 12, 387 (1984)
34. P. Klein, M. Kanehisa, C. Delisi, Biochim. Biophys. Acta 815, 468 (1985)
35. 32P-labeled 1.2-kb Pst I fragment of the rat glyceraldehyde-3-phosphate dehydrogenase cDNA [Ph. Forth et al , Nucleic Acid Res. 13, 1431 (1985)] was used to estimate variations in RNA loading.
36. 32P-labeled 1.2-kb Pst I fragment of the rat glyceraldehyde-3-phosphate dehydrogenase cDNA [Ph. Forth et al , Nucleic Acid Res. 13, 1431 (1985)] was used to estimate variations in RNA loading.
37. 2 III-5 hybridoma culture medium diluted eight-fold with PBS/M/T) for 2 hours Immunoreactivity was visualized with peroxidase-conjugated rabbit antibody to mouse immunoglobulin G (anti-mouse IgG) and subsequent staining with 3,3′-diaminobenzidine and 4-chloro-1-naphthol substrate. P-glycoproteins were detected with mAb C219 and peroxidase-conjugated rabbit anti-mouse IgG. Immune complexes were visualized by enhanced chemiluminescence.
38. J J. M. Smit et al., Lab Invest. 71, 638 (1994).
39. - rat colony.