Myofibrillar myopathy with abnormal foci of desmin positivity. II. Immunocytochemical analysis reveals accumulation of multiple other proteins

Journal of Neuropathology and Experimental Neurology

Volumn 55, Issue 5, 1996, Pages 563-577

  De Bleecker, Jan L ^a   Engel, Andrew G ^a   Ertl, Birgit B ^a  

^a MAYO CLINIC   (United States)

Author keywords

Amyloid; Desmin; Dystrophin; Gelsolin; Immunocytochemistry; Myopathy; NCAM

Indexed keywords

AMYLOID; AMYLOID PRECURSOR PROTEIN; DESMIN; DYSTROPHIN; GELSOLIN; NERVE CELL ADHESION MOLECULE;

ARTICLE; CELLULAR DISTRIBUTION; CLINICAL ARTICLE; HUMAN; HUMAN TISSUE; IMMUNOCYTOCHEMISTRY; MUSCLE FIBRIL; MYOPATHY; PRIORITY JOURNAL; PROTEIN LOCALIZATION;

EID: 0029925575     PISSN: 00223069     EISSN: None     Source Type: Journal    
DOI: 10.1097/00005072-199605000-00009     Document Type: Article

References (118)

1. Nakano S, Engel AG, Waclawik AJ, Emslie-Smith AM, Busis NA. Myofibrillar myopathy with abnormal foci of desmin positivity. I. Light and electron microscopy analysis of 10 cases. J Neuropathol Exp Neurol 1996;55:549-62
2. Goebel HH, Bornemann A. Desmin pathology in neuromuscular diseases. Virch Arch B Cell Pathol 1993;64:127-35
3. Vasjar J, Becker LE, Freedom RM, Murphy EG. Familial desminopathy: Myopathy with accumulation of desmin-type intermediate filaments. J Neurol Neurosurg Psychiatry 1993;56:644-48
4. Tellerman-Toppet N, Bauherz G, Noël S. Auriculo-ventricular block and distal myopathy with rimmed vacuoles and desmin storage. Clin Neuropathol 1991;10:61-64
5. Fardeau M, Godet-Guillain J, Tome F, et al. Une nouvelle affection musculaire familiale, définie par l'accumulation intrasarcoplasmique d'un matériel granulofilamentaire dense en microscopie électronique. Rev Neurol 1978;134:411-25
6. Chaponnier C, Janmey PA, Yin HL. The actin filament-severing domain of plasma gelsolin. J Cell Biol 1986;103:1473-81
7. McLauglin PJ, Gooch JT, Mannherz H-G, Weeds AG. Structure of gelsolin segment 1-actin complex and the mechanism of filament serving. Nature 1993;364:685-92
8. Vandekerckhove J, Vancompernolle K. Structural relationships of actin-binding proteins. Curr Opin Cell Biol 1992;4:36-42
9. Moore SE, Walsh FS. Specific regulation of N-CAM/D2-CAM cell adhesion molecule during skeletal muscle development. EMBO J 1985;4:623-30
10. Cashman NR, Covault J, Wollman RL, Sanes JR. Neural cell adhesion molecule in normal, denervated, and myopathic human muscle. Ann Neurol 1987;21:481-89
11. Edmonson DG, Olson EN. Helix-loop-helix proteins as regulators of muscle-specific transcription. J Biol Chem 1993;268:755-58
12. Lee W-H, Bookstein R, Hong F, Young L-J, Shew J-Y, Lee EY-HP. Human retinoblastoma susceptibility gene: Cloning, identification, and sequence. Science 1987;235:1394-99
13. Pons F, Leger JO, Chevallay M, Tomé FM, Fardeau M, Leger JJ. Immunocytochemical analysis of myosin heavy chains in human fetal skeletal muscle. J Neurol Sci 1986;76:151-63
14. Schiaffino S, Gorza L, Dones I, Cornelio F, Sartore S. Fetal myosin immunoreactivity in human dystrophic muscle. Muscle Nerve 1986;9:51-58
15. Piette J, Bessereau J-L, Huet M, Changeux JP. Two adjacent MyoD1-binding sites regulate expression of the acetylcholine receptor alpha-subunit gene. Nature 1990;345:353-55
16. Bessereau J-L, Mendelzon D, LePoupon C, Fiszman M, Changeux J-P, Piette J. Muscle-specific expression of the acetylcholine receptor alpha-subunit gene requires both positive and negative interactions between myogenic factors, SP1, and GBF factors. EMBO J 1993;12:443-49
17. Selkoe DJ. The molecular pathology of Alzhetmer's disease. Neuron 1991;6:487-98
18. Yankner BA, Mesulam M-M. β-Amyloid and the pathogenesis of Alzheimer's disease. N Engl J Med 1991;325:1849-57
19. Eikelenboom P, Hack CE, Kamphorst W, Rozemuller JM. Distribution pattern and functional state of complement proteins and α1-antichymotrypsin in cerebral β/A4 deposits in Alzheimer's disease. Res Immunol 1992;143:617-20
20. Abraham CR. The role of acute-phase protein α1-antichymotrypsin in brain dysfunction and injury. Res Immunol 1992;143:631-36
21. McGeer PL, McGeer EG. Complement proteins and complement inhibitors in Alzheimer's disease. Res Immunol 1992;143:621-24
22. Rogers J, Schultz J, Brachova L, et al. Complement activation and β-amyloid-mediated neurotoxicity in Alzheimer's disease. Res Immunol 1992;143:624-30
23. Benson MD. Amyloidosis. In: Scriver CR, Beaudet AL, Sly WS, et al, eds. The metabolic and molecular bases of inherited disease. 7th Ed. New York. McGraw-Hill, 1995:4159-91
24. Jacobson DR, Buxbaum JN. Genetic aspects of amyloidosis. Adv Hum Genet 1991;20:69-123
25. Stone MJ. Amyloidosis: A final common pathway for protein deposition in tissues. Blood 1990;75:531-45
26. Kalaria RN. Serum amyloid P component and related molecules associated with the acute-phase response in Alzheimer's disease. Res Immunol 1992;143:637-41
27. Kitamoto T, Ogomori K, Tateishi J, Prusiner SB. Formic acid pretreatment enhances immunostaining of cerebral and systemic amyloids. Lab Invest 1987;57:230-36
28. De Bleecker JL, Engel AG, Winkelmann JC Localization of dystrophin and β-spectrin in vacuolar myopathies. Am J Pathol 1993;143:1200-1208
29. Engel AG, Arahata K. Monoclonal antibody analysis of mononuclear cells in myopathies. II: Phenotypes of autoinvasive cells in polymyositis and inclusion body myositis. Ann Neurol 1984; 16: 209-15
30. Puchtler H, Sweat F. Congo red as a stain for fluorescence microscopy of amyloid. J Histochem Cytochem 1965;13:693-94
31. Askanas V, Engel WK, Alvarez RB. Enhanced detection of Congo-red positive amyloid deposits in muscle fibers of inclusion body myositis and brain of Alzheimer's disease using fluorescence technique. Neurology 1993;43:1265-67
32. Wulf EA, Deboben A, Bautz FA, Faulstich H, Wieland T. Fluorescent phallotoxin, a tool for the visualization of cellular actin. J Histochem Cytochem 1965;13:693-94
33. Rozemuller JM, Abbink JJ, Kamp AM, Stam FC, Hack CE, Eikelenboom P. Distribution pattern and functional state of α1-antichymotrypsin in plaques and vascular amyloid in Alzheimer's disease. An immunohistochemical study with monoclonal antibodies against native and inactivated α1-antichymotrypsin. Acta Neuropathol 1991;82:200-207
34. Manetto V, Abdul-Karim FW, Perry G, Tabaton M, AutilioGambetti L, Gambetti P. Selective presence of ubiquitin in intracellular inclusions. Am J Pathol 1989:134:505-13
35. Perry G, Friedman R, Shaw G, Chau V. Ubiquitin is detected in neurofibrillary tangles and senile plaque neuntes of Alzheimer disease brains. Proc Natl Acad Sci USA 1987;84:3033-36
36. Lowe J, Blanchard A, Morrell K, et al. Ubiquitin is a common factor in intermediate filament inclusion bodies of diverse types in man, including those of Parkinson's disease, Pick's disease, and Alzheimer's disease, as well as Rosenthal fibers in cerebellar astrocytomas, cytoplasmic bodies in muscle, and Mallory bodies in alcoholic liver disease. J Pathol 1988;155:9-15
37. Hershko A. Ubiquitin-mediated protein degradation J Biol Chem 1988;263:15237-40
38. Orlowski M. The multicatalytic proteinase complex, a major extralysosomal proteolyic system. Biochemistry 1990;29:10289-97
39. Sabatelli M, Bertini E, Ricci E, et al. Peripheral neuropathy with giant axons and cardiomyopathy associated with desmin type intermediate filaments in skeletal muscle. J Neurol Sci 1992;109:1 110
40. Caron A, Chapon F, Berthelin C, Viader F, Lechavelier B. Inclusions in familial cytoplasmic body myopathy are stained with dystrophin. Neuromuscul Disord 1993;3:541-46
41. Bertini E, Bosman C, Ricci E, et al. Neuromyopathy and restrictive cardiomyopathy with accumulation intermediate filaments: A clinical, morphological and biochemical study. Acta Neuropathol 1991;81:632-40
42. Weeds A, Maciver S. F-actin capping proteins. Curr Opin Cell Biol 1993;5:63-69
43. Edström L, Thornell L-E, Albo J, Landin S, Samuelson M. Myopathy with respiratory failure and typical myofibrillar lesions. J Neurol Sci 1990;96:211-28
44. Askanas V, Bilak M, Leclerc A, Tomé F. Prion protein is strongly immunolocalized at the postsynaptic domain of human normal neuromuscular junctions. Neurosci Lett 1993;159:111-14
45. Prelle A, Moggio M, Comi GP, Gallanti A, Checcarelli N. Congenital myopathy associated with abnormal accumulation of desmin and dystrophin. Neuromuscul Disord 1992;169-75
46. Selkoe DJ, Podlisny MB, Joachim CL, et al. Beta-amyloid precursor protein of Alzheimer disease occurs as 110- to 135-kilodalton membrane-associated proteins in neural and nonneural tissues. Proc Natl Acad Sci USA 1988;85:7341-45
47. Pelissier JF, Pouget J, Chapin C, Figarella D. Myopathy associated wih desmin type intermediate filaments. An immunoelectron microscopic study. J Neurol Sci 1989;89:49-61
48. Goebel HH. Desmin-related neuromuscular disorders. Muscle Nerve 1995;18;1306-20
49. Ertl B, De Bleecker JL, Engel AG. Patterns of abnormal protein expression in target formations and unstructured cores. (Abstract) Muscle nerve 1994;Supplement 1:S91
50. Sarnat H. Myotubular myopathy: Arrest of morphogenesis of myofibers associated with persistence of fetal vimentin and desmin. Can J Neurol Sci 1990;17:109-23
51. Misra AK, Menon NK, Mishra SK. Abnormal distribution of desmin and vimentin in myofibers in adult onset myotubular myopathy. Muscle Nerve 1992;15:1246-52
52. Sarnat HB. Vinentin and desmin in maturing skeletal muscle and developmental myopathies. Neurology 1992;42:1616-24
53. Sarnat HB. New insights into the pathogenesis of congenital myopathies. J Child Neurol 1994;9:193-201
54. Rapaport L, Contard F, Samuel JL, et al. Storage of phosphorylated desmin in a familial myopathy. FEBS Lett 1989;231:421-25
55. Geisler N, Weber K. Phosphorylation of desmin in vitro inhibits formation of intermediate filaments; identification of three kinase Λ sites in the aminoterminal head domain. EMBO J 1988;7:15-20
56. Inagaki M, Gonda Y, Matsuyama M, Nishizawa K, Nishi Y, Sato C. Intermediate filament reconstitution in vitro. The role of phosphorylation on the assembly-disassembly of desmin. J Biol Chem 1988;263:5970-78
57. Kusubata M. Matsuoka Y. Tsujimura K, et al. cdc2 Kinase phosphorylation of desmin at three serine/threonine residues in the amino-terminal head domain. Biochem Biophys Res Commun 1993;190:927-34
58. Schultheiss T, Lin Z, Ishikawa H, Zamir I, Stoeckert CJ, Holtzer H. Desmin/vimentin intermediate filaments are dispensable for many aspects of myogenesis. J Cell Biol 1991;114:953-66
59. Lin Z, Eshleman J, Forry-Shaudies S, Duran S, Lessard JL, Holtzer H. Sequential disassembly of myofibrils induced by myristate acetate in cultured myotubes. J Cell Biol 1987;105:1365-76
60. Lin Z, Eshleman J, Ground C, et al. Differential response of myofibrillar and cytoskeletal proteins in cells treated with phorbol myristate esters. J Cell Biol 1989;108:1079-91
61. Castellani L, Reedy MC, Gauzzi MC, Provezano C, Alemà S, Falcone G. Maintenance of the differentiated state in skeletal muscle: Activation of v-Src disrupts sarcomeres in quail myotubes. J Cell Biol 1995;130:871-85
62. Inagaki M, Nishi Y, Nishizawa K, Matsuyama M, Sato C. Site-specific phosphorylation induces disassembly of vimentin filaments in vitro. Nature 1987;328:649-52
63. Gettemans J, De Ville Y, Vandekerckhove J, Waelkens E. Physarum actin is phosphorylated as the actin-fragmin complex at residues Thr203 and Thr202 by a specific 80 kDa kinase. EMBO J 1992;11:3185-91
64. Fabbrizio E, Bonet-Kerrache A, Leger JJ, Mornet D. Actin-dystrophin interface. Biochemistry 1993;32:10457-63
65. Matsumura K, Campbell KP. Dystrophin-glycoprotein complex: Its role in the molecular pathogenesis of muscular dystrophies. Muscle Nerve 1994;17:2-15
66. Dmytrenko GM, Pumplin DW, Bloch RJ. Dystrophin in a membrane skeletal network: Localization and comparison to other proteins. J Neurosci 1993;13:547-58
67. Helliwell TR, Green RT, Green A, Edwards RH. Hereditary distal myopathy with granulo-filamentous cytoplasmic inclusions containing desmin, dystrophin and vimentin. J Neurol Sci 1994; 124: 174-87
68. Caron A, Viader F, Lechevalier B. Chapon F. Cytoplasmic body myopathy: Familial cases with accumulation of desmin and dystrophin. An immunohistochemical, immunoelectron microscopic and biochemical study. Acta Neuropathol 1995;90:150-57
69. Bornemann A, Schmalbruch H. Desmin and vimentin in regenerating muscles. Muscle Nerve 1992;15:14-20
70. Fürst DO, Osborn M, Weber K. Myogenesis in the mouse embryo: Differential onset of myogenic proteins and the involvement of titin in myofibril assembly. J Cell Biol 1989;109:517-27
71. Moore SE, Walsh FS. Nerve dependent regulation of neural cell adhesion molecule in skeletal muscle. Neuroscience 1986;18:499-505
72. Gu W, Schneider JW, Condorelli G, Kaushai S, Mahdavi V, Nadal-Ginard B. Interaction of myogenic factors and the retinoblastoma protein mediates muscle cell commitment and differentiation. Cell 1993;72:309-24
73. Füchtbauer E-M, Westphal H. MyoD and myogenin are coexpressed in regenerating skeletal muscle of the mouse. Dev Dyn 1992;193:34-39
74. Clark RF, Goate AM. Molecular genetics of Alzheimer's disease. Arch Neurol 1993;50:1164-72
75. Kosik KS. Alzheimer's disease: A cell biological perspective. Science 1992;256:780-83
76. Ponte P, Gonzalez-DeWhitt P, Schilling J, et al. A new A4 amyloid mRNA contains a domain homologous to serine protease inhibitors. Nature 1988;331:525-27
77. Tanzi RE, McClatchey AI, Lamperti ED, Villa-Komaroff L, Gusella JF, Neve RL. Protease inhibitor domain encoded by an amyloid protein precursor mRNA associated with Alzheimer's disease. Nature 1988;331:528-30
78. Kitaguchi N, Takahashi Y, Tokushima Y, Shiojiri S, Ito H. Novel precursor of Alzheimer's disease amyloid protein shows inhibitory protease activity. Nature 1988;331:530-32
79. Golde TE, Estus S, Younkin L, Selkoe DJ, Younkin SG. Processing of the amyloid protein precursor to potentially amyloidogenic derivatives. Science 1992,255:728-30
80. Weidemann A, König G, Bunke D, et al. Identification, biogenesis, and localization of precursors of Alzheimer's disease A4 amyloid protein. Cell 1989;57:115-26
81. De Sauvage F, Octave J-N. A novel mRNA of the A4 amyloid precursor gene coding for a possibly secreted protein. Science 1989;245:651-53
82. Oltersdorf T, Fritz LC, Schenk DB, et al. The secreted form of the Alzheimer's amyloid precursor protein with the Kunitz domain is protease nexin-II. Nature 1989;341:144-47
83. Van Nostrand WE, Wagner SL, Suzuki M, et al. Protease nexin-II, a potent antichymotrypsin, shows identity to amyloid β-protein precursor. Nature 1989;341:546-49
84. Podlisny MB, Mammen AL, Schlossmacher MG, Palmert MR, Younkin SG, Selkoe DJ Detection of soluble forms of the β-amyloid precursor protein in human plasma. Biochem Biophys Res Commun 1990;167:1094-1101
85. Van Nostrand WE, Wagner SL, Farrow JS, Cunningham DD. Immunopurification and protease inhibitory properties of protease nexin-2/amyloid β-protein precursor. J Biol Chem 1990;265: 9591-94
86. Palmert MR, Podlisny MB, Witker DS, et al. The β-amyloid protein precursor of Alzheimer disease has soluble derivatives found in human brain and cerebrospinal fluid. Proc Natl Acad Sci USA 1989;86:6338-42
87. Schubert D, Cole G, Saitoh T, Oltesdorf T. Amyloid beta protein precursor is a mitogen. Biochem Biophys Res Commun 1989;162: 83-88
88. Schubert D, Jin L-W, Saitoh T, Cole G. The regulation of amyloid â protein secretion and its modulatory role in cell adhesion. Neuron 1989;3:689-94
89. Nishimoto I, Okamoto T, Matsuura Y, Murayama Y, Ogata E Alzheimer amyloid protein precursor complexes with brain GTP-binding protein G(o). Nature 1993;362:75-79
90. Koo EH, Sisodia SS, Archer DR, et al. Precursor of amyloid protein in Alzheimer disease undergoes fast anterograde axonal transport. Proc Natl Acad Sci USA 1990;87:1561-65
91. Tanaka S, Shiojiri S, Takahashi Y, et al. Tissue-specific expression of three types of β-protein precursor mRNA: Enhancement of protease inhibitor-harboring types in Alzheimer's disease brain. Biochem Biophys Res Commun 1989;165:1406-14
92. Selkoe DJ. Normal and abnormal biology of the β-amyloid precursor protein. Annu Rev Neurosci 1994;17:489-517
93. Ashall F, Goate AM. Role of the β-amyloid precursor protein in Alzheimer's disease. Trends Biochcm Sci 1994;19:42-46
94. Askanas V, Engel WK, Alvarez RB. Light and electron microscopic localization of beta-amyloid protein in muscle biopsies of patients with inclusion-body myositis. Am J Pathol 1992;141. 31-36
95. Askanas V, Alvarez RB, Engel WK. β-Amyloid precursor epitopes in muscle fibers of inclusion body myositis. Ann Neurol 1993;34: 551-60
96. Griggs RC, Askanas V, Dimauro S, et al. Inclusion body myositis and myopathies. Ann Neurol 1995;38:705-13
97. Sarkozi E, Askanas V, Johnson SA, Engel WK, Alvarez RB. β-Amyloid precursor protein mRNA is increased in inclusion-body myositis muscle. Neuroreport 1993;4:815-18
98. Bilak M, Askanas V, Engel WK. Strong immunoreactivity of α1-antichymotrypsin co-localizes with β-amyloid protein and ubiquitin in vacuolaled fibers in inclusion body myositis. Act Neuropathol 1993;85:378-82
99. Glenner GG. Amyloid deposits and amyloidosis. The β-fibrilloses. N Engl J Mcd 1980;302:1283-92
100. de la Chapelle A, Tolvanen R, Boysen G, et al. Gelsolin-derived familial amyloidosis caused by asparagine or tyrosine substitution for aspartic acid at residue 187. Nat Genet 1992;2:157-60
101. Haltia M, Prelli F, Ghiso J, et al. Amyloid protein in familial amyloidosis (Finnish type) is homologous to gelsolin, an actin binding protein. Biochem Biophys Res Commun 1990;167:927-32
102. Maury PJ. Gelsolin related amyloidosis. Identification of the amyloid protein in Finnish hereditary amyloidosis as a fragment of variant gelsolin. J Clin Invest 1991;87:1195-99
103. Askanas V, Serdaroglu P, Engel WK, Alvarez RB. Immunolocalization of ubiquitin in muscle biopsies of patients with inclusion body myositis and oculopharyngeal muscular dystrophy. Nurosci Lett 1991;130:73-76
104. Engel AG, Biesecker G. Complement activation in muscle fiber necrosis: Demonstration of the membrane attack complex of complement in necrotic fibers. Ann Neurol 1982;12:289-96
105. Van Muyen GNP, Ruiter DJ, Warnaar SO. Coexpression of intermediate filament polypeptides in human fetal and adult tissues. Lab Invest 1987;57:359-69
106. Ip W, Saeed T. Desmin binding specificities of two desmin CNBr fragments that correspond to the headpiece domain and helix 1B. Cell Biol Int Rep 1990;14:1119-27
107. Winkelmann JC, Costa FF, Linzie BL, Forget BL. β-Spectrin in human skeletal muscle: Tissue-specific differential processing of 3′ β-spectrin pre-mRNA generates a β-spectrin isoform with a unique carboxyl terminus. J Biol Chem 1990;265:20454-99
108. Asijee GM, Sturk A, Bruin T, Wilkinson JM, Ten Cate JW. Vinculin is a permanent component of the membrane skeleton and is incorporated into the (re)organizing cytoskeleton upon platelet activation. Eur J Biochem 1990;189:131-36
109. Otey C, Griffiths W, Burridge K. Characterization of monoclonal antibodies to chicken gizzard talin. Hybridoma 1990;9:57-62
110. Fridlanskaya II, Goncharova EI, Borisov AB, Krylova TA, Pinaev GF. The monoclonal antibody to α-actinin as a marker for the skeletal and cardiac myogenesis. Tsitologia 1989;31:1234-37
111. Tsukada T, Tippens D, Gordon D, Ross R, Gown AM. HHF35, a muscle-actin-specific monoclonal antibody. I. Immunocytochemical and biochemical characterization. Am J Pathol 1987;126:51-60
112. Narusawa M, Fitzsimmons RB, Izumo S, Nadal-Ginard B, Rubinstein NA, Kelly AM. Slow myosin in developing rat skeletal muscle. J Cell Biol 1987;104:447-59
113. Molenaar CE, Muller EJ, Schol D, et al. Expression of NCAM-related syalogycoprotein in small lung cancer and neuroblastoma cell lines H69 and CHP-212. Cancer Res 1990;50:1102-11
114. Dias P, Purham DM, Shapiro DN, Tapscott SJ, Houghton PJ. Monoclonal antibodies to the myogenic regulatory protein MyoD1: Epitope mapping and diagnostic utility. Cancer Res 1992;52:6431-39
115. Ikeda S-I, Wong CW, Allsop D, Landon M, Kidd M, Glenner G. Immunogold labeling of cerebrovascular and neuritic plaque amyloid fibrils in Alzheimer's disease with anti-β protein monoclonal antibody. Lab Invest 1987;57:446-49
116. Kim KS, Wen GY, Bancher C. Detection and quantitation of amyloid β-peptide with 2 monoclonal antibodies Neurosci Res Comm 1990;7:113-22
117. Kim KS, Miller DL, Sapienza VJ. Production and characterization of monoclonal antibodies reactive to synthetic cerebrovascular amyloid peptide. Neurosci Res Comm 1988;2:121-30
118. Podlisny MB, Tolan DR, Selkoe DJ. Homology of the amyloid beta protein precursor in monkey and human supports a primate model for beta amyloidosis in Alzheimer's disease. Am J Pathol 1991;138:1423-35