Sequence of events in the assembly of Mallory body components in mouse liver: Clues to the pathogenesis and significance of Mallory body formation

Journal of Hepatology

Volumn 34, Issue 5, 2001, Pages 665-675

  Stumptner, Cornelia ^a   Fuchsbichler, Andrea ^a   Lehner, Manfred ^a   Zatloukal, Kurt ^a   Denk, Helmut ^a  

^a UNIVERSITY OF GRAZ   (Austria)

Author keywords

Alcoholic hepatitis; Cytokeratin; Griseofulvin; Heat shock protein; Intermediate filaments; Mallory body

Indexed keywords

1,4 DIHYDRO 2,4,6 TRIMETHYL 3,5 PYRIDINEDICARBOXYLIC ACID DIETHYL ESTER; COLCHICINE; GRISEOFULVIN; HEAT SHOCK PROTEIN; KERATIN; LUMICOLCHICINE; MESSENGER RNA;

ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; CYTOSKELETON; GENE EXPRESSION; LIVER CELL; MALE; MALLORY BODY; MOUSE; NONHUMAN; PATHOGENESIS; PRIORITY JOURNAL; SYNTHESIS;

ANIMALS; ANTIGENS, SURFACE; COLCHICINE; DICARBETHOXYDIHYDROCOLLIDINE; GRISEOFULVIN; IMMUNOHISTOCHEMISTRY; INCLUSION BODIES; KERATIN-8; KERATINS; LIVER; LUMICOLCHICINES; MALE; MICE; PHOSPHORYLATION; RNA, MESSENGER; TIME FACTORS; UBIQUITIN;

EID: 0034998784     PISSN: 01688278     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0168-8278(00)00099-4     Document Type: Article

References (64)

1. Denk H., Franke W.W., Kerjaschki D., Eckerstorfer R. Mallory bodies in experimental animals and man. Int Rev Exp Pathol. 20:1979;77-121.
2. Denk H., Stumptner C., Zatloukal K. Mallory bodies revisited. J Hepatol. 32:2000;689-702.
3. Denk H., Gschnait F., Wolff K. Hepatocellular hyalin (Mallory bodies) in long term griseofulvin-treated mice. A new experimental model for the study of hyalin formation. Lab Invest. 32:1975;773-776.
4. Yokoo H., Harwood T.R., Racker D., Arak S. Experimental production of Mallory bodies in mice by diet containing 3,5-diethoxycarbonyl-1,4-dihydrocollidine. Gastroenterology. 83:1982;109-113.
5. Yokoo H., Minick O.T., Batti F., Kent G. Morphologic variants of alcoholic hyalin. Am J Pathol. 69:1972;25-32.
6. Franke W.W., Denk H., Schmid E., Osborn M., Weber K. Ultrastructural, biochemical, and immunologic characterization of Mallory bodies in livers of griseofulvin-treated mice. Fimbriated rods of filaments containing prekeratin-like polypeptides. Lab Invest. 40:1979;207-220.
7. Zatloukal K., Böck G., Rainer I., Denk H., Weber K. High molecular weight components are main constituents of Mallory bodies isolated with a fluorescence activated cell sorter. Lab Invest. 64:1991;200-206.
8. Hazan R., Denk H., Franke W.W., Lackinger E., Schiller D.L. Change of cytokeratin organization during development of Mallory bodies as revealed by a monoclonal antibody. Lab Invest. 54:1986;543-553.
9. Denk H., Franke W.W., Dragosics B., Zeiler I. Pathology of cytoskeleton of liver cells: demonstration of Mallory bodies (alcoholic hyalin) in murine and human hepatocytes by immunofluorescence microscopy using antibodies to cytokeratin polypeptides from hepatocytes. Hepatology. 1:1981;9-20.
10. Zatloukal K., Denk H., Spurej G., Lackinger E., Preisegger K.H., Franke W.W. High molecular weight component of Mallory bodies detected by a monoclonal antibody. Lab Invest. 62:1990;427-434.
11. Preisegger K.H., Zatloukal K., Spurej G., Riegelnegg D., Denk H. Common epitopes of human and murine Mallory bodies and Lewy bodies as revealed by a neurofilament antibody. Lab Invest. 66:1992;193-199.
12. Cadrin M., Marceau N., French S.W. Cytokeratin of apparent high molecular weight in livers from griseofulvin-fed mice. J Hepatol. 14:1992;226-231.
13. Cadrin M., Hovington H., Marceau N., McFarlane-Anderson N. Early perturbations in keratin and actin gene expression and fibrillar organisation in griseofulvin-fed mouse liver. J. Hepatol. 33:2000;199-207.
14. Denk H., Bernklau G., Krepler R. Effect of griseofulvin treatment and neoplastic transformation on transglutaminase activity in mouse liver. Liver. 4:1984;208-213.
15. Zatloukal K., Denk H., Lackinger E., Rainer I. Hepatocellular cytokeratins as substrates of transglutaminases. Lab Invest. 61:1989;603-608.
16. Zatloukal K., Fesus L., Denk H., Tarcsa E., Spurej G., Böck G. High amount of ε-(γ-glutamyl)lysine cross-links in Mallory bodies. Lab Invest. 66:1992;774-777.
17. Kachi K., Wong P.T.T., French S.W. Molecular structural changes in Mallory body proteins in human and mouse livers: An infrared spectroscopy study. Exp Mol Pathol. 59:1993;197-210.
18. Salmhofer H., Rainer I., Zatloukal K., Denk H. Posttranslational events involved in griseofulvin-induced keratin cytoskeleton alterations. Hepatology. 20:1994;731-740.
19. Stumptner C., Omary M.B., Fickert P., Denk H., Zatloukal K. Hepatocyte cytokeratins are hyperphosphorylated at multiple sites in human alcoholic hepatitis and in a Mallory body mouse model. Am J Pathol. 156:2000;77-90.
20. Jensen K., Gluud Ch. The Mallory body: theories on development and pathological significance (Part 2 of a literature survey). Hepatology. 20:1994;1330-1342.
21. Jensen K., Gluud Ch. The Mallory body: morphological, clinical and experimental studies (Part 1 of a literature survey). Hepatology. 20:1994;1061-1077.
22. Denk H., Eckerstorfer R., Gschnait F., Konrad K., Wolff K. Experimental induction of hepatocellular hyalin (Mallory bodies) in mice by griseofulvin treatment. I. Light microscopic observations. Lab Invest. 35:1976;377-382.
23. Denk H., Eckerstorfer R. Colchicine-induced Mallory body formation in the mouse. Lab Invest. 36:1977;563-565.
24. Klassen L.W., Tuma D., Sorrell M.F. Immune mechanisms of alcohol-induced liver disease. Hepatology. 22:1995;355-357.
25. Yuan Q.X., Marceau N., French B.A., Fu P., French S.W. Mallory body induction in drug-primed mouse liver. Hepatology. 24:1996;603-612.
26. Yuan Q.X., Marceau N., French B.A., Fu P., French S.W. Heat shock in vivo induces Mallory body formation in drug primed mouse liver. Exp Mol Pathol. 63:1995;63-76.
27. Yuan Q.X., Nagao Y., Gaal K., Hu B., French S.W. Mechanism of Mallory body formation induced by okadaic acid in drug-primed mice. Exp Mol Pathol. 65:1998;87-103.
28. Yuan Q., French B.A., French S.W. Tautomycin induces extensive Mallory body formation in drug primed mouse livers. Hepatology. 28:1998;256A.
29. Zhang-Gouillon Z.Q., Yuan Q.X., Hu B., Marceau B., French B.A., Gaal K., et al. Mallory body formation by ethanol feeding in drug-primed mice. Hepatology. 27:1998;116-122.
30. Nagao Y., Yuan Q.X., Wan Y.J.Y., French B., French S.W. Pathogenesis of Mallory body formation: studies using the drug-primed mouse model. Hepatol Res. 13:1998;42-54.
31. Wilson L., Friedkin M. The biochemical events of mitosis. I. Synthesis and properties of colchicine labeled with tritium in its acetyl moiety. Biochemistry. 5:1966;2463-2468.
32. Zatloukal K., Spurej G., Lackinger E., Rainer I., Denk H. Fate of Mallory body-containing hepatocytes: disappearance of Mallory bodies and restoration of the hepatocytic intermediate filament cytoskeleton after drug withdrawal in the griseofulvin treated mouse. Hepatology. 11:1990;652-661.
33. Krieg P., Amtmann E., Sauer G. The simultaneous extraction of high-molecular-weight DNA and of RNA from solid tumors. Anal Biochem. 134:1983;288-294.
34. Eferl R, Lehner M, Kenner L, Kapfer I, Gürtl B, Zatloukal K. Evaluation of different standard types for quantitative reverse transcription polymerase chain reaction: possible pitfalls and strategies for avoidance. Elsevier Trends Journals, Technical Tips Online 1997; (http://tto.trends.com) TO 1214.
35. Zatloukal K., Stumptner C., Lehner M., Denk H., Baribault H., Eshkind L.G., et al. Cytokeratin 8 protects from hepatotoxicity, and its ratio to cytokeratin 18 determines the ability of hepatocytes to form Mallory bodies. Am J Pathol. 156:2000;1263-1274.
36. Hames B.D., Higgins S.J. Nucleic acid hybridization. A practical approach. 1988;IRL Press, Oxford, Washington, DC.
37. Hutter H., Zatloukal K., Winter G., Stumptner C., Denk H. Disturbance of keratin homeostasis in griseofulvin-intoxicated mouse liver. Lab Invest. 69:1993;576-582.
38. Kachi K., Cadrin M., French S.W. Synthesis of Mallory body, intermediate filament, and microfilament proteins in liver cell primary cultures. Lab Invest. 68:1993;71-81.
39. Magin T.M., Schröder R., Leitgeb S., Wanninger F., Zatloukal K., Grund C., et al. Lessons from keratin 18 knockout mice: formation of novel keratin filaments, secondary loss of keratin 7 and accumulation of liver-specific keratin 8-positive aggregates. J Cell Biol. 140:1998;1441-1451.
40. Klemenz R., Fröhli E., Steiger R.H., Schäfer R., Avyama A. αB-crystallin is a small heat shock protein. Proc Natl Acad Sci USA. 88:1991;3652-3656.
41. Lowe J., McDermott H., Pike I., Spendlove I., Landon M., Mayer R.J. αB-crystallin expression in non-lenticular tissues and selective presence in ubiquitinated inclusion bodies in human disease. J Pathol. 166:1992;61-68.
42. Kaufman R.J. Molecular chaperones and the heat shock response. Biochem Biophys Acta. 1423:1998;R13-R27.
43. Rassow J., Von Ahsen O., Bömer U., Pfanner N. Molecular chaperones: towards a characterization of the heat-shock protein 70 family. Trends Cell Biol. 7:1997;129-133.
44. Hartl F.U. Molecular chaperones in cellular protein folding. Nature. 381:1996;571-580.
45. Quinlan R., Van den Ijssel P. Fatal attraction: when chaperone turns harlot. Nature Medicine. 5:1999;25-26.
46. Deshaies R.J. Make it or break it: the role of ubiquitin-dependent proteolysis in cellular regulation. Trends Cell Biol. 5:1995;428-434.
47. Weissman A.M. Regulating protein degradation by ubiquitination. Immunol Today. 18:1997;189-198.
48. Lowe J., Blanchard A., Morrell K., Lennox G., Reynolds L., Billett M., et al. Ubiquitin is a common factor in intermediate filament inclusion bodies of diverse type in man including those of Parkinson's disease, Pick's disease, and Alzheimer's disease, as well as Rosenthal fibres in cerebellar astrocytomas, cytoplasmic bodies in muscle, and Mallory bodies in alcoholic liver disease. J Pathol. 155:1988;9-15.
49. Ohta M., Marceau N., Perry G., Manetto V., Gambetti P., Autilio-Gambetti L., et al. Ubiquitin is present on the cytokeratin intermediate filaments and Mallory bodies of hepatocytes. Lab Invest. 59:1988;848-856.
50. Fataccioli V., Andrand E., Gentil M., French S.W., Rouach H. Effects of chronic ethanol administration on rat liver proteasome activities: relationship with oxidative stress. Hepatology. 29:1999;14-20.
51. Nukina N., Kosik K.S., Selkoe D.J. Recognition of Alzheimer paired helical filaments by monoclonal neurofilament antibodies is due to crossreaction with tau protein. Proc Natl Acad Sci USA. 84:1987;3415-3419.
52. Lichtenberg-Kraag B., Mandelkow E.M., Biernat J., Steiner B., Schröter C., Gustke N., et al. Phosphorylation-dependent epitopes of neurofilament antibodies on tau protein and relationship with Alzheimer tau. Proc Natl Acad Sci USA. 89:1992;5384-5388.
53. Vincent I., Rosado M., Davies P. Mitotic mechanisms in Alzheimer's disease? J Cell Biol. 132:1996;413-425.
54. Kondratick C.M., Vandre D.D. Alzheimer's disease neurofibrillary tangles contain mitosis-specific phosphoepitopes. J Neurochem. 67:1996;2405-2416.
55. Westendorf J.M., Rao P.N., Gerace L. Cloning of cDNAs for M-phase phosphoproteins recognized by the MPM2 monoclonal antibody and determination of the phosphorylated epitope. Proc Natl Acad Sci USA. 91:1994;714-718.
56. De Matteis F., Gibbs A.H., Holley A.E. Occurrence and biological properties of N-methyl protoporphyrin. Am NY Acad Sci. 514:1987;30-40.
57. Bailey S.M., Cunningham C.C. Acute and chronic ethanol increases reactive oxygen species generation and decreases viability in fresh, isolated rat hepatocytes. Hepatology. 28:1998;1318-1326.
58. Tsukamoto H. Oxidative stress, antioxidants, and alcoholic liver fibrogenesis. Alcohol. 10:1993;465-467.
59. Rouach H., Fataccioli V., Gentil M., French S.W., Morimoto M., Nordmann R. Effect of chronic ethanol feeding on lipid peroxidation and protein oxidation in relation to liver pathology. Hepatology. 25:1997;351-355.
60. Albano E., Clot P., Morimoto M., Tomasi A., Ingelman-Sundberg M., French S.W. Role of cytochrome P450 2E1-dependent formation of hydroxyethyl free radical in the development of liver damage in rats intragastrally fed with ethanol. Hepatology. 23:1996;155-163.
61. Stadtman E.R., Berlett B.S. Free-radical-mediated modification of proteins. Wallace K.B. Free radical toxicology. 1997;71-87 Taylor and Francis, London, Philadephia, PA.
62. Ortiz de Montellano P.R., Beilan H.S., Kunze K.L. N-alkylprotoporphyrin IX formation in 3,5-dicarbethoxy-1,4-dihydrocollidine-treated rats. Transfer of the alkyl group from the substrate to the porphyrin. J Biol Chem. 256:1981;6708-6713.
63. Brady A.M., Lock E.A. Inhibition of ferrochelatase and accumulation of porphyrins in mouse hepatocyte culture exposed to porphyrinogenic chemicals. Arch Toxicol. 66:1992;175-181.
64. Cadrin M., McFarlane Anderson N., Aasheim L.H., Kawahara H., Franks D.J., French S.W. Modifications in cytokeratin and actin in cultured liver cells derived from griseofulvin-fed mice. Lab Invest. 72:1995;453-460.