From Mallory to Mallory-Denk bodies: What, how and why?

Experimental Cell Research

Volumn 313, Issue 10, 2007, Pages 2033-2049

  Zatloukal, Kurt ^d   French, Samuel W ^e   Stumptner, Cornelia ^d   Strnad, Pavel ^a,b   Harada, Masaru ^c   Toivola, Diana M ^a,b   Cadrin, Monique ^f   Omary, M Bishr ^a,b  

^a VA PALO ALTO HEALTH CARE SYSTEM   (United States)

^b Stanford California and Cofounder   (United States)

^c KURUME UNIVERSITY SCHOOL OF MEDICINE   (Japan)

^d MEDICAL UNIVERSITY OF GRAZ   (Austria)

^e HARBOR UCLA MEDICAL CENTER   (United States)

^f UNIVERSITÉ DU QUÉBEC À TROIS RIVIÈRES   (Canada)

Author keywords

ASH; Chaperones; Hepatocellular carcinoma; Idiopathic copper toxicosis; Inclusion bodies; Intermediate filaments; Keratins; Liver disease; Liver injury; NAFLD; NASH; p62; Primary biliary cirrhosis; Ubiquitin; Wilson disease

Indexed keywords

CYTOKERATIN 18; CYTOKERATIN 8; GRISEOFULVIN; PROTEIN P62; UBIQUITIN;

CYTOPLASM; DISEASE ASSOCIATION; HUMAN; LIVER DISEASE; MALLORY BODY; MOLECULAR MODEL; NONALCOHOLIC FATTY LIVER; NONHUMAN; PATHOGENESIS; PRIORITY JOURNAL; REVIEW;

ANIMALIA; MUS;

EID: 34249697629     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.yexcr.2007.04.024     Document Type: Review

References (151)

1. Denk H., Stumptner C., and Zatloukal K. Mallory bodies revisited. J. Hepatol. 32 (2000) 689-702
2. French S.W. Present understanding of the development of Mallory's body. Arch. Pathol. Lab. Med. 107 (1983) 445-450
3. Jensen K., and Gluud C. The Mallory body: morphological, clinical and experimental studies (Part 1 of a literature survey). Hepatology 20 (1994) 1061-1077
4. Jensen K., and Gluud C. The Mallory body: theories on development and pathological significance (Part 2 of a literature survey). Hepatology 20 (1994) 1330-1342
5. Mallory F. Cirrhosis of the liver. Five different types of lesions from which it may arise. Bul. Johns Hopkins Hosp. 22 (1911) 69-75
6. Mallory F. The Principles of Pathologic Histology (1914), W.B. Saunders Company, Philadelphia
7. Denk H., Gschnait F., and Wolff K. Hepatocellar 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
8. Denk H., and Eckerstorfer R. Colchicine-induced Mallory body formation in the mouse. Lab. Invest. 36 (1977) 563-565
9. Hurst E.W., and Paget G.E. Protoporphyrin, cirrhosis and hepatoma in the livers of mice given griseofulvin. Br. J. Dermatol. 75 (1963) 105-112
10. Denk H., Franke W.W., Eckerstorfer R., Schmid E., and Kerjaschki D. Formation and involution of Mallory bodies ("alcoholic hyalin") in murine and human liver revealed by immunofluorescence microscopy with antibodies to prekeratin. Proc. Natl. Acad. Sci. U. S. A. 76 (1979) 4112-4116
11. Franke W.W., Denk H., Schmid E., Osborn M., and 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
12. Denk H., Krepler R., Lackinger E., Artlieb U., and Franke W.W. Immunological and biochemical characterization of the keratin-related component of Mallory bodies: a pathological pattern of hepatocytic cytokeratins. Liver 2 (1982) 165-175
13. Zatloukal K., Denk H., Spurej G., Lackinger E., Preisegger K.H., and Franke W.W. High molecular weight component of Mallory bodies detected by a monoclonal antibody. Lab. Invest. 62 (1990) 427-434
14. Zatloukal K., Fesus L., Denk H., Tarcsa E., Spurej G., and Bock G. High amount of epsilon-(gamma-glutamyl)lysine cross-links in Mallory bodies. Lab. Invest. 66 (1992) 774-777
15. Zatloukal K., Stumptner C., Fuchsbichler A., Heid H., Schnoelzer M., Kenner L., Kleinert R., Prinz M., Aguzzi A., and Denk H. p62 is a common component of cytoplasmic inclusions in protein aggregation diseases. Am. J. Pathol. 160 (2002) 255-263
16. Zatloukal K., Stumptner C., Lehner M., Denk H., Baribault H., Eshkind L.G., and Franke W.W. 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
17. Denk H., Stumptner C., Fuchsbichler A., Muller T., Farr G., Muller W., Terracciano L., and Zatloukal K. Are the Mallory bodies and intracellular hyaline bodies in neoplastic and non-neoplastic hepatocytes related?. J. Pathol. 208 (2006) 653-661
18. Coulombe P.A., and Omary M.B. 'Hard' and 'soft' principles defining the structure, function and regulation of keratin intermediate filaments. Curr. Opin. Cell Biol. 14 (2002) 110-122
19. Omary M.B., Coulombe P.A., and McLean W.H. Intermediate filament proteins and their associated diseases. N. Engl. J. Med. 351 (2004) 2087-2100
20. Goebel H.H. Congenital myopathies at their molecular dawning. Muscle Nerve 27 (2003) 527-548
21. Hagemann T.L., Connor J.X., and Messing A. Alexander disease-associated glial fibrillary acidic protein mutations in mice induce Rosenthal fiber formation and a white matter stress response. J. Neurosci. 26 (2006) 11162-11173
22. Mayer R.J., Lowe J., Lennox G., Doherty F., and Landon M. Intermediate filaments and ubiquitin: a new thread in the understanding of chronic neurodegenerative diseases. Prog. Clin. Biol. Res. 317 (1989) 809-818
23. Cairns N.J., Lee V.M., and Trojanowski J.Q. The cytoskeleton in neurodegenerative diseases. J. Pathol. 204 (2004) 438-449
24. Wiggers K.D., French S.W., French B.A., and Carr B.N. The ultrastructure of Mallory body filaments. Lab. Invest. 29 (1973) 652-658
25. Denk H., Franke W.W., Kerjaschki D., and Eckerstorfer R. Mallory bodies in experimental animals and man. Int. Rev. Exp. Pathol. 20 (1979) 77-121
26. Virtanen I., Lehto V.P., Kurki P., Miettinen A., Linder E., and Stenman S. Intermediate filaments in hyaline material in alcoholic liver disease (Mallory bodies) and in cultured hepatoma cells. Virchows Arch. B: Cell Pathol. 29 (1979) 363-367
27. Cadrin M., Kawahara H., Ohta M., Katsuma Y., Marceau N., and French S.W. Mallory bodies in hepatomas and hyperplastic nodules: in vitro and in vivo studies. Prog. Clin. Biol. Res. 331 (1990) 231-248
28. Pei R.J., Danbara N., Tsujita-Kyutoku M., Yuri T., and Tsubura A. Immunohistochemical profiles of Mallory body by a panel of anti-cytokeratin antibodies. Med. Electron Microsc. 37 (2004) 114-118
29. Schirmacher P., Dienes H.P., and Moll R. De novo expression of nonhepatocellular cytokeratins in Mallory body formation. Virchows Arch. 432 (1998) 143-152
30. Omary M.B., Ku N.O., Tao G.Z., Toivola D.M., and Liao J. "Heads and tails" of intermediate filament phosphorylation: multiple sites and functional insights. Trends Biochem. Sci. 31 (2006) 383-394
31. Salmhofer H., Rainer I., Zatloukal K., and Denk H. Posttranslational events involved in griseofulvin-induced keratin cytoskeleton alterations. Hepatology 20 (1994) 731-740
32. Cadrin M., Anderson N.M., Aasheim L.H., Kawahara H., Franks D.J., and French S.W. Modifications in cytokeratin and actin in cultured liver cells derived from griseofulvin-fed mice. Lab. Invest. 72 (1995) 453-460
33. Fausther M., Villeneuve L., and Cadrin M. Heat shock protein 70 expression, keratin phosphorylation and Mallory body formation in hepatocytes from griseofulvin-intoxicated mice. Comp. Hepatol. 3 (2004) 5
34. Stumptner C., Omary M.B., Fickert P., Denk H., and 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
35. Zatloukal K., Bock G., Rainer I., Denk H., and 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
36. Cadrin M., Marceau N., and French S.W. Cytokeratin of apparent high molecular weight in livers from griseofulvin-fed mice. J. Hepatol. 14 (1992) 226-231
37. Strnad P., Harada M., Siegel M., Terkeltaub R.A., Graham R.M., Khosla C., and Omary M.B. Transglutaminase-2 regulates Mallory body inclusion formation and injury associated liver hypertrophy. Gastroenterology 132 (2007) 1515-1526
38. Omar R., Pappolla M., and Saran B. Immunocytochemical detection of the 70-kd heat shock protein in alcoholic liver disease. Arch. Pathol. Lab. Med. 114 (1990) 589-592
39. Riley N.E., Li J., McPhaul L.W., Bardag-Gorce F., Lue Y.H., and French S.W. Heat shock proteins are present in mallory bodies (cytokeratin aggresomes) in human liver biopsy specimens. Exp. Mol. Pathol. 74 (2003) 168-172
40. Janig E., Stumptner C., Fuchsbichler A., Denk H., and Zatloukal K. Interaction of stress proteins with misfolded keratins. Eur. J. Cell Biol. 84 (2005) 329-339
41. Seibenhener M.L., Babu J.R., Geetha T., Wong H.C., Krishna N.R., and Wooten M.W. Sequestosome 1/p62 is a polyubiquitin chain binding protein involved in ubiquitin proteasome degradation. Mol. Cell. Biol. 24 (2004) 8055-8068
42. Bjorkoy G., Lamark T., Brech A., Outzen H., Perander M., Overvatn A., Stenmark H., and Johansen T. p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death. J. Cell Biol. 171 (2005) 603-614
43. Nan L., Wu Y., Bardag-Gorce F., Li J., French B.A., Fu A.N., Francis T., Vu J., and French S.W. p62 is involved in the mechanism of Mallory body formation. Exp. Mol. Pathol. 77 (2004) 168-175
44. Dil Kuazi A., Kito K., Abe Y., Shin R.W., Kamitani T., and Ueda N. NEDD8 protein is involved in ubiquitinated inclusion bodies. J. Pathol. 199 (2003) 259-266
45. Nan L., Wu Y., Bardag-Gorce F., Li J., French B.A., Wilson L.T., Khanh Nguyen S., and French S.W. RNA interference of VCP/p97 increases Mallory body formation. Exp. Mol. Pathol. 78 (2005) 1-9
46. Denk H., and Franke W.W. Rearrangement of the hepatocyte cytoskeleton after toxic damage: involution, dispersal and peripheral accumulation of Mallory body material after drug withdrawal. Eur. J. Cell Biol. 23 (1981) 241-249
47. Okanoue T., Ohta M., Ou O., Kachi K., Kagawa K., Yuki T., Okuno T., Takino T., and French S.W. Relationship of Mallory bodies to intermediate filaments in hepatocytes. A scanning electron microscopy study. Lab. Invest. 53 (1985) 534-540
48. Zatloukal K., Spurej G., Rainer I., Lackinger E., and 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
49. Cadrin M., French S.W., and Wong P.T. Alteration in molecular structure of cytoskeleton proteins in griseofulvin-treated mouse liver: a pressure tuning infrared spectroscopy study. Exp. Mol. Pathol. 55 (1991) 170-179
50. Muller T., Langner C., Fuchsbichler A., Heinz-Erian P., Ellemunter H., Schlenck B., Bavdekar A.R., Pradhan A.M., Pandit A., Muller-Hocker J., Melter M., Kobayashi K., Nagasaka H., Kikuta H., Muller W., Tanner M.S., Sternlieb I., Zatloukal K., and Denk H. Immunohistochemical analysis of Mallory bodies in Wilsonian and non-Wilsonian hepatic copper toxicosis. Hepatology 39 (2004) 963-969
51. Yokoo H., Harwood T.R., Racker D., and Arak S. Experimental production of Mallory bodies in mice by diet containing 3,5-diethoxycarbonyl-1,4-dihydrocollidine. Gastroenterology 83 (1982) 109-113
52. French S.W., Ihrig T.J., and Norum M.L. A method of isolation of Mallory bodies in a purified fraction. Lab. Invest. 26 (1972) 240-244
53. C. Stumptner, A. Fuchsbichler, K. Zatloukal, and H. Denk, In vitro production of mallory bodies and intracellular hyaline bodies: The central role of p62, Hepatology (in press).
54. P.J. Scheuer, J.H. Lefkowitch, Eds., Liver biopsy Interpretation, Seventh Edition, 2005.
55. Ishak K.G., Goodman Z.D., and Stocker T.J. Hepatocellular carcinoma. Atlas of Tumor Pathology, Tumors of the Liver and Intrahepatic Bile Ducts (2001)
56. Lefkowitch J.H., Lobritto S.J., Brown Jr. R.S., Emond J.C., Schilsky M.L., Rosenthal L.A., George D.M., and Cairo M.S. Ground-glass, polyglucosan-like hepatocellular inclusions: a "new" diagnostic entity. Gastroenterology 131 (2006) 713-718
57. Warnock M.L., Press M., and Churg A. Further observations on cytoplasmic hyaline in the lung. Hum. Pathol. 11 (1980) 59-65
58. Yamada T., Uehara K., Kawanishi R., Mizutani T., Sunagawa K., Araya J., and Kawabata Y. Immunohistochemical detection of ubiquitin-positive intracytoplasmic eosinophilic inclusion bodies in diffuse alveolar damage. Histopathology 48 (2006) 846-854
59. Tsang W.Y., Chum N.P., Tang S.K., Tse C.C., and Chan J.K. Mallory's bodies in placental site nodule. Arch. Pathol. Lab. Med. 117 (1993) 547-550
60. Jagirdar J., Irie T., French S.W., Patil J., Schwarz R., and Paronetto F. Globular Mallory-like bodies in renal cell carcinoma: report of a case and review of cytoplasmic eosinophilic globules. Hum. Pathol. 16 (1985) 949-952
61. Pasquinelli G., Preda P., Martinelli G.N., Galassi A., Santini D., and Venza E. Filamentous inclusions in nonneoplastic and neoplastic pancreas: an ultrastructural and immunogold labeling study. Ultrastruct. Pathol. 19 (1995) 495-500
62. Rubin E., and Lieber C.S. Experimental alcoholic hepatitis: a new primate model. Science 182 (1973) 712-713
63. Meierhenry E.F., Ruebner B.H., Gershwin M.E., Hsieh L.S., and French S.W. Mallory body formation in hepatic nodules of mice ingesting dieldrin. Lab. Invest. 44 (1981) 392-396
64. Meierhenry E.F., Ruebner B.H., Gershwin M.E., Hsieh L.S., and French S.W. Dieldrin-induced mallory bodies in hepatic tumors of mice of different strains. Hepatology 3 (1983) 90-95
65. Akeda S., Fujita K., Kosaka Y., and French S.W. Mallory body formation and amyloid deposition in the liver of aged mice fed a vitamin A deficient diet for a prolonged period. Lab. Invest. 54 (1986) 228-233
66. Yuan Q.X., Marceau N., French B.A., Fu P., and French S.W. Mallory body induction in drug-primed mouse liver. Hepatology 24 (1996) 603-612
67. Stumptner C., Fuchsbichler A., Lehner M., Zatloukal K., and Denk H. Sequence of events in the assembly of Mallory body components in mouse liver: clues to the pathogenesis and significance of Mallory body formation. J. Hepatol. 34 (2001) 665-675
68. Stumptner C., Fuchsbichler A., Heid H., Zatloukal K., and Denk H. Mallory body-a disease-associated type of sequestosome. Hepatology 35 (2002) 1053-1062
69. Tazawa J., Irie T., and French S.W. Mallory body formation runs parallel to gamma-glutamyl transferase induction in hepatocytes of griseofulvin-fed mice. Hepatology 3 (1983) 989-1001
70. Fickert P., Trauner M., Fuchsbichler A., Stumptner C., Zatloukal K., and Denk H. Bile acid-induced Mallory body formation in drug-primed mouse liver. Am. J. Pathol. 161 (2002) 2019-2026
71. Yuan Q.X., Marceau N., French B.A., Fu P., and French S.W. Heat shock in vivo induces Mallory body formation in drug primed mouse liver. Exp. Mol. Pathol. 63 (1995) 63-76
72. French B.A., van Leeuwen F., Riley N.E., Yuan Q.X., Bardag-Gorce F., Gaal K., Lue Y.H., Marceau N., and French S.W. Aggresome formation in liver cells in response to different toxic mechanisms: role of the ubiquitin-proteasome pathway and the frameshift mutant of ubiquitin. Exp. Mol. Pathol. 71 (2001) 241-246
73. Yuan Q.X., Nagao Y., Gaal K., Hu B., and French S.W. Mechanisms of mallory body formation induced by okadaic acid in drug-primed mice. Exp. Mol. Pathol. 65 (1998) 87-103
74. Roomi M.W., Gaal K., Yuan Q.X., French B.A., Fu P., Bardag-Gorce F., and French S.W. Preneoplastic liver cell foci expansion induced by thioacetamide toxicity in drug-primed mice. Exp. Mol. Pathol. 81 (2006) 8-14
75. Zhang-Gouillon Z.Q., Yuan Q.X., Hu B., Marceau N., French B.A., Gaal K., Nagao Y., Wan Y.J., and French S.W. Mallory body formation by ethanol feeding in drug-primed mice. Hepatology 27 (1998) 116-122
76. Nakamichi I., Toivola D.M., Strnad P., Michie S.A., Oshima R.G., Baribault H., and Omary M.B. Keratin 8 overexpression promotes mouse Mallory body formation. J. Cell Biol. 171 (2005) 931-937
77. Magin T.M., Schroder R., Leitgeb S., Wanninger F., Zatloukal K., Grund C., and Melton D.W. 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
78. Harada M., Strnad P., Resurreccion E., Ku N.O., and Omary M.B. Keratin 18 overexpression but not phosphorylation or filament organization blocks mouse Mallory body formation. Hepatology 45 (2007) 88-96
79. Ku N.O., Michie S., Oshima R.G., and Omary M.B. Chronic hepatitis, hepatocyte fragility, and increased soluble phosphoglycokeratins in transgenic mice expressing a keratin 18 conserved arginine mutant. J. Cell Biol. 131 (1995) 1303-1314
80. Lorand L., and Graham R.M. Transglutaminases: crosslinking enzymes with pleiotropic functions. Nat. Rev., Mol. Cell Biol. 4 (2003) 140-156
81. Komatsu M., Waguri S., Ueno T., Iwata J., Murata S., Tanida I., Ezaki J., Mizushima N., Ohsumi Y., Uchiyama Y., Kominami E., Tanaka K., and Chiba T. Impairment of starvation-induced and constitutive autophagy in Atg7-deficient mice. J. Cell Biol. 169 (2005) 425-434
82. Kachi K., Cadrin M., and French S.W. Synthesis of Mallory body, intermediate filament, and microfilament proteins in liver cell primary cultures. An electron microscopic autoradiography assay. Lab. Invest. 68 (1993) 71-81
83. Bardag-Gorce F., Riley N.E., Nan L., Montgomery R.O., Li J., French B.A., Lue Y.H., and French S.W. The proteasome inhibitor, PS-341, causes cytokeratin aggresome formation. Exp. Mol. Pathol. 76 (2004) 9-16
84. Nan L., Dedes J., French B.A., Bardag-Gorce F., Li J., Wu Y., and French S.W. Mallory body (cytokeratin aggresomes) formation is prevented in vitro by p38 inhibitor. Exp. Mol. Pathol. 80 (2006) 228-240
85. Hirano K., Roth J., Zuber C., and Ziak M. Expression of a mutant ER-retained polytope membrane protein in cultured rat hepatocytes results in Mallory body formation. Histochem. Cell Biol. 117 (2002) 41-53
86. Nakamichi I., Hatakeyama S., and Nakayama K.I. Formation of Mallory body-like inclusions and cell death induced by deregulated expression of keratin 18. Mol. Biol. Cell 13 (2002) 3441-3451
87. Harada M., Kumemura H., Omary M.B., Kawaguchi T., Maeyama N., Hanada S., Taniguchi E., Koga H., Suganuma T., Ueno T., and Sata M. Proteasome inhibition induces inclusion bodies associated with intermediate filaments and fragmentation of the Golgi apparatus. Exp. Cell Res. 288 (2003) 60-69
88. Hanada S., Harada M., Kumemura H., Omary M.B., Kawaguchi T., Taniguchi E., Koga H., Yoshida T., Maeyama M., Baba S., Ueno T., and Sata M. Keratin-containing inclusions affect cell morphology and distribution of cytosolic cellular components. Exp. Cell Res. 304 (2005) 471-482
89. Marceau N., Gilbert S., and Loranger A. Uncovering the roles of intermediate filaments in apoptosis. Methods Cell Biol. 78 (2004) 95-129
90. Wu Y., Nan L., Bardag-Gorce F., Li J., French B.A., Wilson L.T., Dedes J., and French S.W. The role of laminin-integrin signaling in triggering MB formation. An in vivo and in vitro study. Exp. Mol. Pathol. 79 (2005) 1-8
91. Goldberg A.L. Protein degradation and protection against misfolded or damaged proteins. Nature 426 (2003) 895-899
92. Macario A.J., and Conway de Macario E. Sick chaperones, cellular stress, and disease. N. Engl. J. Med. 353 (2005) 1489-1501
93. Carbone D.L., Doorn J.A., Kiebler Z., Ickes B.R., and Petersen D.R. Modification of heat shock protein 90 by 4-hydroxynonenal in a rat model of chronic alcoholic liver disease. J. Pharmacol. Exp. Ther. 315 (2005) 8-15
94. McClellan A.J., Tam S., Kaganovich D., and Frydman J. Protein quality control: chaperones culling corrupt conformations. Nat. Cell Biol. 7 (2005) 736-741
95. Vadlamudi R.K., Joung I., Strominger J.L., and Shin J. p62, a phosphotyrosine-independent ligand of the SH2 domain of p56lck, belongs to a new class of ubiquitin-binding proteins. J. Biol. Chem. 271 (1996) 20235-20237
96. Donaldson K.M., Li W., Ching K.A., Batalov S., Tsai C.C., and Joazeiro C.A. Ubiquitin-mediated sequestration of normal cellular proteins into polyglutamine aggregates. Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 8892-8897
97. Sanz L., Sanchez P., Lallena M.J., Diaz-Meco M.T., and Moscat J. The interaction of p62 with RIP links the atypical PKCs to NF-kappaB activation. EMBO J. 18 (1999) 3044-3053
98. Sanz L., Diaz-Meco M.T., Nakano H., and Moscat J. The atypical PKC-interacting protein p62 channels NF-kappaB activation by the IL-1-TRAF6 pathway. EMBO J. 19 (2000) 1576-1586
99. Zhong B., Zhou Q., Toivola D.M., Tao G.Z., Resurreccion E.Z., and Omary M.B. Organ-specific stress induces mouse pancreatic keratin overexpression in association with NF-kappaB activation. J. Cell Sci. 117 (2004) 1709-1719
100. Nan L., Wu Y., Bardag-Gorce F., Li J., French B.A., Wilson L.T., and French S.W. The p105/50 NF-kappaB pathway is essential for Mallory body formation. Exp. Mol. Pathol. 78 (2005) 198-206
101. Hazan R., Denk H., Franke W.W., Lackinger E., and Schiller D.L. Change of cytokeratin organization during development of Mallory bodies as revealed by a monoclonal antibody. Lab. Invest. 54 (1986) 543-553
102. Zatloukal K., Denk H., Spurej G., and Hutter H. Modulation of protein composition of nuclear lamina. Reduction of lamins B1 and B2 in livers of griseofulvin-treated mice. Lab. Invest. 66 (1992) 589-597
103. Merlini G., and Bellotti V. Molecular mechanisms of amyloidosis. N. Engl. J. Med. 349 (2003) 583-596
104. Ross C.A., and Poirier M.A. Protein aggregation and neurodegenerative disease. Nat. Med. 10 Suppl (2004) S10-S17
105. Ku N.O., Azhar S., and Omary M.B. Keratin 8 phosphorylation by p38 kinase regulates cellular keratin filament reorganization: modulation by a keratin 1-like disease causing mutation. J. Biol. Chem. 277 (2002) 10775-10782
106. Ku N.O., and Omary M.B. A disease- and phosphorylation-related nonmechanical function for keratin 8. J. Cell Biol. 174 (2006) 115-125
107. Ku N.O., and Omary M.B. Keratins turn over by ubiquitination in a phosphorylation-modulated fashion. J. Cell Biol. 149 (2000) 547-552
108. Zatloukal K., Denk H., Lackinger E., and Rainer I. Hepatocellular cytokeratins as substrates of transglutaminases. Lab. Invest. 61 (1989) 603-608
109. Nilsson M.R., Driscoll M., and Raleigh D.P. Low levels of asparagine deamidation can have a dramatic effect on aggregation of amyloidogenic peptides: implications for the study of amyloid formation. Protein Sci. 11 (2002) 342-349
110. Mandrusiak L.M., Beitel L.K., Wang X., Scanlon T.C., Chevalier-Larsen E., Merry D.E., and Trifiro M.A. Transglutaminase potentiates ligand-dependent proteasome dysfunction induced by polyglutamine-expanded androgen receptor. Hum. Mol. Genet. 12 (2003) 1497-1506
111. Ravikumar B., Duden R., and Rubinsztein D.C. Aggregate-prone proteins with polyglutamine and polyalanine expansions are degraded by autophagy. Hum. Mol. Genet. 11 (2002) 1107-1117
112. Bardag-Gorce F., van Leeuwen F.W., Nguyen V., French B.A., Li J., Riley N., McPhaul L.W., Lue Y.H., and French S.W. The role of the ubiquitin-proteasome pathway in the formation of mallory bodies. Exp. Mol. Pathol. 73 (2002) 75-83
113. Bardag-Gorce F., French B.A., Lue Y.H., Nguyen V., Wan Y.J., and French S.W. Mallory bodies formed in proteasome-depleted hepatocytes: an immunohistochemical study. Exp. Mol. Pathol. 70 (2001) 7-18
114. Venkatraman P., Wetzel R., Tanaka M., Nukina N., and Goldberg A.L. Eukaryotic proteasomes cannot digest polyglutamine sequences and release them during degradation of polyglutamine-containing proteins. Mol. Cell 14 (2004) 95-104
115. Pickart C.M., and Cohen R.E. Proteasomes and their kin: proteases in the machine age. Nat. Rev., Mol. Cell Biol. 5 (2004) 177-187
116. Hayashi T., and Goto S. Age-related changes in the 20S and 26S proteasome activities in the liver of male F344 rats. Mech. Ageing Dev. 102 (1998) 55-66
117. Fataccioli V., Andraud E., Gentil M., French S.W., and Rouach H. Effects of chronic ethanol administration on rat liver proteasome activities: relationship with oxidative stress. Hepatology 29 (1999) 14-20
118. van Leeuwen F.W., de Kleijn D.P., van den Hurk H.H., Neubauer A., Sonnemans M.A., Sluijs J.A., Koycu S., Ramdjielal R.D., Salehi A., Martens G.J., Grosveld F.G., Peter J., Burbach H., and Hol E.M. Frameshift mutants of beta amyloid precursor protein and ubiquitin-B in Alzheimer's and Down patients. Science 279 (1998) 242-247
119. Lindsten K., de Vrij F.M., Verhoef L.G., Fischer D.F., van Leeuwen F.W., Hol E.M., Masucci M.G., and Dantuma N.P. Mutant ubiquitin found in neurodegenerative disorders is a ubiquitin fusion degradation substrate that blocks proteasomal degradation. J. Cell Biol. 157 (2002) 417-427
120. McPhaul L.W., Wang J., Hol E.M., Sonnemans M.A., Riley N., Nguyen V., Yuan Q.X., Lue Y.H., Van Leeuwen F.W., and French S.W. Molecular misreading of the ubiquitin B gene and hepatic mallory body formation. Gastroenterology 122 (2002) 1878-1885
121. Ishak K.G., Zimmerman H.J., and Ray M.B. Alcoholic liver disease: pathologic, pathogenetic and clinical aspects. Alcohol Clin. Exp. Res. 15 (1991) 45-66
122. French S.W., Nash J., Shitabata P., Kachi K., Hara C., Chedid A., and Mendenhall C.L. Pathology of alcoholic liver disease. VA Cooperative Study Group 119. Semin. Liver Dis. 13 (1993) 154-169
123. French S.W., Kawahara H., Cadrin M., and Kachi K. Cytoskeleton. In: LeBouten A.V. (Ed). Molecular and Cell Biology of the Liver (1993), CRC Press, Boca Raton
124. Hall P. Pathological spectrum of alcoholic liver disease. In: Hall P. (Ed). Alcoholic Liver Disease: Pathology and Pathogenesis (1995), Edward Arnold, London
125. Burt A.D., Mutton A., and Day C.P. Diagnosis and interpretation of steatosis and steatohepatitis. Semin. Diagn. Pathol. 15 (1998) 246-258
126. Brunt E.M., Janney C.G., Di Bisceglie A.M., Neuschwander-Tetri B.A., and Bacon B.R. Nonalcoholic steatohepatitis: a proposal for grading and staging the histological lesions. Am. J. Gastroenterol. 94 (1999) 2467-2474
127. Brunt E.M. Nonalcoholic steatohepatitis. Semin. Liver Dis. 24 (2004) 3-20
128. Hubscher S.G. Histological assessment of non-alcoholic fatty liver disease. Histopathology 49 (2006) 450-465
129. Brunt E.M. Non-alcoholic fatty liver disease. In: Burt A.D., Portmann B.C., and Farrell L.D. (Eds). Mc Sween's Pathology of the Liver (2007), Churchill Livingstone Elsevier
130. Hall P. Alcoholic liver disease. In: Burt A.D., Portmann B.C., and Farrell L.D. (Eds). Mc Sween's Pathology of the Liver (2007), Churchill Livingstone Elsevier
131. Ray M.B. Distribution patterns of cytokeratin antigen determinants in alcoholic and nonalcoholic liver diseases. Hum. Pathol. 18 (1987) 61-66
132. Wanless I.R., and Lentz J.S. Fatty liver hepatitis (steatohepatitis) and obesity: an autopsy study with analysis of risk factors. Hepatology 12 (1990) 1106-1110
133. Pinto H.C., Baptista A., Camilo M.E., Valente A., Saragoca A., and de Moura M.C. Nonalcoholic steatohepatitis. Clinicopathological comparison with alcoholic hepatitis in ambulatory and hospitalized patients. Dig. Dis. Sci. 41 (1996) 172-179
134. Matteoni C.A., Younossi Z.M., Gramlich T., Boparai N., Liu Y.C., and McCullough A.J. Nonalcoholic fatty liver disease: a spectrum of clinical and pathological severity. Gastroenterology 116 (1999) 1413-1419
135. Mendler M.H., Kanel G., and Govindarajan S. Proposal for a histological scoring and grading system for non-alcoholic fatty liver disease. Liver Int. 25 (2005) 294-304
136. Gramlich T., Kleiner D.E., McCullough A.J., Matteoni C.A., Boparai N., and Younossi Z.M. Pathologic features associated with fibrosis in nonalcoholic fatty liver disease. Hum. Pathol. 35 (2004) 196-199
137. Orrego H., Blake J.E., Blendis L.M., and Medline A. Prognosis of alcoholic cirrhosis in the presence and absence of alcoholic hepatitis. Gastroenterology 92 (1987) 208-214
138. Kleiner D.E., Brunt E.M., Van Natta M., Behling C., Contos M.J., Cummings O.W., Ferrell L.D., Liu Y.C., Torbenson M.S., Unalp-Arida A., Yeh M., McCullough A.J., and Sanyal A.J. Design and validation of a histological scoring system for nonalcoholic fatty liver disease. Hepatology 41 (2005) 1313-1321
139. Lee W.C., Yoshihara M., and Littleton J.T. Cytoplasmic aggregates trap polyglutamine-containing proteins and block axonal transport in a Drosophila model of Huntington's disease. Proc. Natl. Acad. Sci. U. S. A. 101 (2004) 3224-3229
140. Stenoien D.L., Cummings C.J., Adams H.P., Mancini M.G., Patel K., DeMartino G.N., Marcelli M., Weigel N.L., and Mancini M.A. Polyglutamine-expanded androgen receptors form aggregates that sequester heat shock proteins, proteasome components and SRC-1, and are suppressed by the HDJ-2 chaperone. Hum. Mol. Genet. 8 (1999) 731-741
141. Suhr S.T., Senut M.C., Whitelegge J.P., Faull K.F., Cuizon D.B., and Gage F.H. Identities of sequestered proteins in aggregates from cells with induced polyglutamine expression. J. Cell Biol. 153 (2001) 283-294
142. Bence N.F., Sampat R.M., and Kopito R.R. Impairment of the ubiquitin-proteasome system by protein aggregation. Science 292 (2001) 1552-1555
143. Peters M., Liebman H.A., Tong M.J., and Tinberg H.M. Alcoholic hepatitis: granulocyte chemotactic factor from Mallory body-stimulated human peripheral blood mononuclear cells. Clin. Immunol. Immunopathol. 28 (1983) 418-430
144. Woltsche M., Zatloukal K., and Denk H. Enzyme-histochemical studies of griseofulvin-intoxicated mouse livers. Liver 11 (1991) 231-240
145. Zatloukal K., Stumptner C., Fuchsbichler A., Janig E., and Denk H. Intermediate filament protein inclusions. Methods Cell Biol. 78 (2004) 205-228
146. Toivola D.M., Ku N.O., Resurreccion E.Z., Nelson D.R., Wright T.L., and Omary M.B. Keratin 8 and 18 hyperphosphorylation is a marker of progression of human liver disease. Hepatology 40 (2004) 459-466
147. Lowe J., Blanchard A., Morrell K., Lennox G., Reynolds L., Billett M., Landon M., and Mayer R.J. 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
148. Ohta M., Marceau N., Perry G., Manetto V., Gambetti P., Autilio-Gambetti L., Metuzals J., Kawahara H., Cadrin M., and French S.W. Ubiquitin is present on the cytokeratin intermediate filaments and Mallory bodies of hepatocytes. Lab. Invest. 59 (1988) 848-856
149. Stumptner C., Heid H., Fuchsbichler A., Hauser H., Mischinger H.J., Zatloukal K., and Denk H. Analysis of intracytoplasmic hyaline bodies in a hepatocellular carcinoma. Demonstration of p62 as major constituent. Am. J. Pathol. 154 (1999) 1701-1710
150. Preisegger K.H., Zatloukal K., Spurej G., Riegelnegg D., and 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
151. Riley N.E., Li J., Worrall S., Rothnagel J.A., Swagell C., van Leeuwen F.W., and French S.W. The Mallory body as an aggresome: in vitro studies. Exp. Mol. Pathol. 72 (2002) 17-23