Human Genome & Diseases: Review - Alexander disease: Putative mechanisms of an astrocytic encephalopathy

Cellular and Molecular Life Sciences

Volumn 61, Issue 3, 2004, Pages 369-385

  Mignot, C ^a,b   Boespflug Tanguy, O ^c   Gelot, A ^b   Dautigny, A ^a   Pham Dinh, D ^a   Rodriguez, D ^a,b  

^a PITIÉ SALPÊTRIÈRE HOSPITAL   (France)

^b ARMAND TROUSSEAU HOSPITAL   (France)

^c INSERM   (France)

Author keywords

Alexander disease; Astrocytes; Cytoskeleton; Glial fibrillary acidic protein; Intermediate filaments; Leukodystrophy

Indexed keywords

FREE RADICAL; GLIAL FIBRILLARY ACIDIC PROTEIN; GLUTAMIC ACID; MYELIN; SCAVENGER;

ALEXANDER DISEASE; AMINO ACID TRANSPORT; AMINO TERMINAL SEQUENCE; ASTROCYTE; BLOOD BRAIN BARRIER; BRAIN CELL; CARBOXY TERMINAL SEQUENCE; CELL INCLUSION; CELL INTERACTION; CELL LOSS; CENTRAL NERVOUS SYSTEM DISEASE; CLINICAL FEATURE; COGNITIVE DEFECT; DEGENERATIVE DISEASE; DEMYELINATION; DISEASE COURSE; DISEASE MODEL; DYSTROPHY; ENERGY METABOLISM; EPILEPSY; GENE CLUSTER; GENE MUTATION; GENE OVEREXPRESSION; GENETIC CODE; HUMAN; INTERMEDIATE FILAMENT; INTRACRANIAL HYPERTENSION; KNOCKOUT MOUSE; MOLECULAR BIOLOGY; MOTOR DYSFUNCTION; MOUSE MUTANT; NERVE CELL; NERVE CELL NETWORK; NEUROPATHOLOGY; NEUROPHYSIOLOGY; NONHUMAN; NULL ALLELE; OLIGODENDROGLIA; PATHOGENESIS; PATHOLOGY; PATHOPHYSIOLOGY; PHENOTYPE; PROTEIN AGGREGATION; PROTEIN ASSEMBLY; PROTEIN DEFECT; PROTEIN FUNCTION; RADIOLOGY; REVIEW; AMINO ACID SEQUENCE; ANIMAL; BRAIN; GENETICS; GENOME; METABOLISM; MOLECULAR GENETICS; PHYSIOLOGY; SEQUENCE ALIGNMENT;

ALEXANDER DISEASE; AMINO ACID SEQUENCE; ANIMALS; ASTROCYTES; BLOOD-BRAIN BARRIER; BRAIN; DISEASE MODELS, ANIMAL; GENOME, HUMAN; GLIAL FIBRILLARY ACIDIC PROTEIN; GLUTAMIC ACID; HUMANS; MOLECULAR SEQUENCE DATA; SEQUENCE ALIGNMENT;

EID: 1242351783     PISSN: 1420682X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00018-003-3143-3     Document Type: Review

References (162)

1. Alexander W. S. (1949) Progressive fibrinoid degeneration of fibrillary astrocytes associated with mental retardation in a hydrocephalic infant. Brain 72: 373-381
2. Brenner M., Johnson A. B., Boespflug-Tanguy O., Rodriguez D., Goldman J. E. and Messing A. (2001) Mutations in GFAP, encoding glial fibrillary acidic protein, are associated with Alexander disease. Nat. Genet. 27: 117-120
3. Wohlwill F. J., Bernstein J. and Yakovlev P. I. (1959) Dysmyelinogenic leukodystrophy. Report of a case of a new, presumably familial type of leukodystrophy with megalobarencephaly. J. Neuropathol. Exp. Neurol. 18: 359-383
4. Howard R. S., Greenwood R., Gawler J., Scaravilli F., Marsden C. D. and Harding A. E. (1993) A familial disorder associated with palatal myoclonus, other brainstem signs, tetraparesis, ataxia and Rosenthal fibre formation. J. Neurol. Neurosurg. Psychiatry 56: 977-981
5. Schwankhaus J. D., Parisi J. E., Gulledge W. R., Chin L. and Currier R. D. (1995) Hereditary adult-onset Alexander's disease with palatal myoclonus, spastic paraparesis and cerebellar ataxia. Neurology 45: 2266-2271
6. Honnorat J., Flocard F., Ribot C., Saint-Pierre G., Pineau D., Peysson P. et al. (1993) [Alexander's disease in adults and diffuse cerebral gliomatosis in 2 members of the same family]. Rev. Neurol. (Paris) 149: 781-787
7. Jaeken J. (2001) Alexander disease and intermediate filaments in astrocytes: a fatal gain of function. Eur. J. Paediatr. Neurol. 5: 151-153
8. Messing A., Goldman J. E., Johnson A. B. and Brenner M. (2001) Alexander disease: new insights from genetics. J. Neuropathol. Exp. Neurol. 60: 563-573
9. Li R., Messing A., Goldman J. E. and Brenner M. (2002) GFAP mutations in Alexander disease. Int. J. Dev. Neurosci. 20: 259-268
10. Borrett D. and Becker L. E. (1985) Alexander's disease. A disease of astrocytes. Brain 108 (Pt 2): 367-385
11. Springer S., Erlewein R., Naegele T., Becker I., Auer D., Grodd W. et al. (2000) Alexander disease - classification revisited and isolation of a neonatal form. Neuropediatrics 31: 86-92
12. Pridmore C. L., Baraitser M., Harding B., Boyd S. G., Kendall B. and Brett E. M. (1993) Alexander's disease: clues to diagnosis. J. Child Neurol. 8: 134-144
13. Sawaishi Y., Yano T., Takaku I. and Takada G. (2002) Juvenile Alexander disease with a novel mutation in glial fibrillary acidic protein gene. Neurology 58: 1541-1543
14. Probst E. N., Hagel C., Weisz V., Nagel S., Wittkugel O., Zeumer H. et al. (2003) Atypical focal MRI lesions in a case of juvenile Alexander's disease. Ann. Neurol. 53: 118-120
15. Seil F. J., Schochet S. S. Jr and Earle K. M. (1968) Alexander's disease in an adult. Report of a case. Arch. Neurol. 19: 494-502
16. Namekawa M., Takiyama Y., Aoki Y., Takayashiki N., Sakoe K., Shimazaki H., Taguchi T. et al. (2002) Identification of GFAP gene mutation in hereditary adult-onset Alexander's disease. Ann. Neurol. 52: 779-785
17. Okamoto Y., Mitsuyama H., Jonosono M., Hirata K., Arimura K., Osame M. et al. (2002) Autosomal dominant palatal myoclonus and spinal cord atrophy. J. Neurol. Sci. 195: 71-76
18. Gorospe J. R., Naidu S., Johnson A. B., Puri V., Raymond G. V., Jenkins S. D. et al. (2002) Molecular findings in symptomatic and pre-symptomatic Alexander disease patients. Neurology 58: 1494-1500
19. van der Knaap M. S., Naidu S., Breiter S. N., Blaser S., Stroink H., Springer S. et al. (2001) Alexander disease: diagnosis with MR imaging. Am. J. Neuroradiol. 22: 541-552
20. Crome L. (1953) Megalencephaly associated with hyaline pan-neuropathy. Brain 76: 215-228
21. Friede R. (1964) Alexander's disease. Arch. Neurol. 11: 4414-4422
22. Peiffer J. (1968) Alexander's disease - really a leucodystrophy? Pathol. Eur. 3: 305-312
23. Towfighi J., Young R., Sassani J., Ramer J. and Horoupian D. S. (1983) Alexander's disease: further light-, and electron-microscopic observations. Acta Neuropathol. 61: 36-42
24. Escourolle R., de Baecque C., Gray F., Baumann N. and Hauw J. J. (1979) [Electron microscopic and neurochemical study of Alexander's disease (author's transl)]. Acta Neuropathol. 45: 133-140
25. Head M. W., Corbin E. and Goldman J. E. (1993) Overexpression and abnormal modification of the stress proteins alpha B-crystallin and HSP27 in Alexander disease. Am. J. Pathol. 143: 1743-1753
26. Schochet S. S. Jr, Lampert P. W. and Earle K. M. (1968) Alexander's disease. A case report with electron microscopic observations. Neurology 18: 543-549
27. Jacob J., Robertson N. J. and Hilton D. A. (2003) The clinicopathological spectrum of Rosenthal fibre encephalopathy and Alexander's disease: a case report and review of the literature. J. Neurol. Neurosurg. Psychiatry 74: 807-810
28. Weissenbock H., Obermaier G. and Dahme E. (1996) Alexander's disease in a Bernese mountain dog. Acta Neuropathol. 91: 200-204
29. Fankhauser R., Fatzer R., Bestetti G., Deruaz J. P. and Perentes E. (1980) Encephalopathy with Rosenthal fibre formation in a sheep. Acta Neuropathol. 50: 57-60
30. Gomi H., Yokoyama T., Fujimoto K., Ikeda T., Katoh A., Itoh T. et al. (1995) Mice devoid of the glial fibrillary acidic protein develop normally and are susceptible to scrapie prions. Neuron 14: 29-41
31. Pekny M., Leveen P., Pekna M., Eliasson C., Berthold C. H., Westermark B. et al. (1995) Mice lacking glial fibrillary acidic protein display astrocytes devoid of intermediate filaments but develop and reproduce normally. EMBO J. 14: 1590-1598
32. Liedtke W., Edelmann W., Bieri P. L., Chiu F. C., Cowan N. J., Kucherlapati R. et al. (1996) GFAP is necessary for the integrity of CNS white matter architecture and long-term maintenance of myelination. Neuron 17: 607-615
33. McCall M. A., Gregg R. G., Behringer R. R., Brenner M., Delaney C. L., Galbreath E. J. et al. (1996) Targeted deletion in astrocyte intermediate filament (Gfap) alters neuronal physiology. Proc. Natl. Acad. Sci. USA 93: 6361-6366
34. Pekny M. (2001) Astrocytic intermediate filaments: lessons from GFAP and vimentin knock-out mice. Prog. Brain Res. 132: 23-30
35. Messing A. and Brenner M. (2003) GFAP: Functional implications gleaned from studies of genetically engineered mice. Glia 43: 87-90
36. Menet V., Gimenez Y. R. M., Sandillon F. and Privat A. (2000) GFAP null astrocytes are a favorable substrate for neuronal survival and neurite growth. Glia 31: 267-272
37. Menet V., Gimenez y Ribotta M., Chauvet N., Drian M. J., Lannoy J., Colucci-Guyon E. et al. (2001) Inactivation of the glial fibrillary acidic protein gene, but not that of vimentin, improves neuronal survival and neurite growth by modifying adhesion molecule expression. J. Neurosci. 21: 6147-6158
38. Tanaka H., Katoh A., Oguro K., Shimazaki K., Gomi H., Itohara S. et al. (2002) Disturbance of hippocampal long-term potentiation after transient ischemia in GFAP deficient mice. J. Neurosci. Res. 67: 11-20
39. Nawashiro H., Messing A., Azzam N. and Brenner M. (1998) Mice lacking GFAP are hypersensitive to traumatic cerebrospinal injury. Neuroreport 9: 1691-1696
40. Nawashiro H., Brenner M., Fukui S., Shima K. and Hallenbeck J. M. (2000) High susceptibility to cerebral ischemia in GFAP-null mice. J. Cereb. Blood Flow Metab. 20: 1040-1044
41. Liedtke W., Edelmann W., Chiu F. C., Kucherlapati R. and Raine C. S. (1998) Experimental autoimmune encephalomyelitis in mice lacking glial fibrillary acidic protein is characterized by a more severe clinical course and an infiltrative central nervous system lesion. Am. J. Pathol. 152: 251-259
42. Pekny M., Stanness K. A., Eliasson C., Betsholtz C. and Janigro D. (1998) Impaired induction of blood-brain barrier properties in aortic endothelial cells by astrocytes from GFAP-deficient mice. Glia 22: 390-400
43. Pekny M., Eliasson C., Siushansian R., Ding M., Dixon S. J., Pekna M. et al. (1999) The impact of genetic removal of GFAP and/or vimentin on glutamine levels and transport of glucose and ascorbate in astrocytes. Neurochem. Res. 24: 1357-1362
44. Messing A., Head M. W., Galles K., Galbreath E. J., Goldman J. E. and Brenner M. (1998) Fatal encephalopathy with astrocyte inclusions in GFAP transgenic mice. Am. J. Pathol. 152: 391-398
45. Eng L. F., Lee Y. L., Kwan H., Brenner M. and Messing A. (1998) Astrocytes cultured from transgenic mice carrying the added human glial fibrillary acidic protein gene contain Rosenthal fibers. J. Neurosci. Res. 53: 353-360
46. Quinlan R. (2001) Cytoskeletal catastrophe causes brain degeneration. Nat. Genet. 27: 10-11
47. Eng L. F. (1995) Intermediate filaments in astrocytes. In: Neuroglia, pp. 650-667, Kettenmann H. and Ransom B. R. (eds), Oxford University Press, New York
48. Galea E., Dupouey P and Feinstein D. L. (1995) Glial fibrillary acidic protein mRNA isotypes: expression in vitro and in vivo. J. Neurosci. Res. 41: 452-461
49. Zelenika D., Grima B., Brenner M. and Pessac B. (1995) A novel glial fibrillary acidic protein mRNA lacking exon 1. Brain Res. Mol. Brain Res. 30: 251-258
50. Nielsen A. L., Holm I. E., Johansen M., Bonven B., Jorgensen P and Jorgensen A. L. (2002) A new splice variant of glial fibrillary acidic protein, GFAP epsilon, interacts with the presenilin proteins. J. Biol. Chem. 277: 29983-29991
51. Strelkov S. V., Herrmann H., Geisler N., Wedig T., Zimbelmann R., Aebi U. et al. (2002) Conserved segments 1A and 2B of the intermediate filament dimer: their atomic structures and role in filament assembly. EMBO J. 21: 1255-1266
52. Burkhard P., Stetefeld J. and Strelkov S. V. (2001) Coiled coils: a highly versatile protein folding motif. Trends Cell Biol. 11: 82-88
53. Stewart M., Quinlan R. A. and Moir R. D. (1989) Molecular interactions in paracrystals of a fragment corresponding to the alpha-helical coiled-coil rod portion of glial fibrillary acidic protein: evidence for an antiparallel packing of molecules and polymorphism related to intermediate filament structure. J. Cell Biol. 109: 225-234
54. Quinlan R. A., Moir R. D. and Stewart M. (1989) Expression in Escherichia coli of fragments of glial fibrillary acidic protein: characterization, assembly properties and paracrystal formation. J. Cell Sci. 93 (Pt 1): 71-83
55. Herrmann H. and Aebi U. (2000) Intermediate filaments nd their associates: multi-talented structural elements specifying cytoarchitecture and cytodynamics. Curr. Opin. Cell Biol. 12: 79-90
56. Parry D. A., Marekov L. N. and Steinert P M. (2001) Subfilamentous protofibril structures in fibrous proteins: cross-linking evidence for protofibrils in intermediate filaments. J. Biol. Chem. 276: 39253-39258
57. Goldman R. D., Chou Y. H., Prahlad V. and Yoon M. (1999) Intermediate filaments: dynamic processes regulating their assembly, motility and interactions with other cytoskeletal systems. FASEB J. 13 Suppl. 2: S261-S265
58. Herrmann H., Strelkov S. V., Feja B., Rogers K. R., Brettel M., Lustig A. et al. (2000) The intermediate filament protein consensus motif of helix 2B: its atomic structure and contribution to assembly. J. Mol. Biol. 298: 817-832
59. Ralton J. E., Lu X., Hutcheson A. M. and Quinlan R. A. (1994) Identification of two N-terminal non-alpha-helical domain motifs important in the assembly of glial fibrillary acidic protein. J. Cell Sci. 107 (Pt 7): 1935-1948
60. Chen W. J. and Liem R. K. (1994) The endless story of the glial fibrillary acidic protein. J. Cell Sci. 107 (Pt 8): 2299-2311
61. Iwaki A., Iwaki T., Goldman J. E., Ogomori K., Tateishi J. and Sakaki Y. (1992) Accumulation of alpha B-crystallin in brains of patients with Alexander's disease is not due to an abnormality of the 5′-flanking and coding sequence of the genomic DNA. Neurosci. Lett. 140: 89-92
62. Rodriguez D., Gauthier F., Bertini E., Bugiani M., Brenner M., N'Guyen S. et al. (2001) Infantile Alexander disease: spectrum of GFAP mutations and genotype-phenotype correlation. Am. J. Hum. Genet. 69: 1134-1140
63. Meins M., Brockmann K., Yadav S., Haupt M., Sperner J., Stephani U. et al. (2002) Infantile Alexander disease: a GFAP mutation in monozygotic twins and novel mutations in two other patients. Neuropediatrics 33: 194-198
64. Shiroma N., Kanazawa N., Kato Z., Shimozawa N., Imamura A., Ito M. et al. (2003) Molecular genetic study in Japanese patients with Alexander disease: a novel mutation, R79L. Brain Dev. 25: 116-121
65. Schroder R., Goudeau B., Simon M. C., Fischer D., Eggermann T., Clemen C. S. et al. (2003) On noxious desmin: functional effects of a novel heterozygous desmin insertion mutation on the extrasarcomeric desmin cytoskeleton and mitochondria. Hum. Mol. Genet. 12: 657-669
66. Smith F. J., Eady R. A., Leigh I. M., McMillan J. R., Rugg E. L., Kelsell D. P. et al. (1996) Plectin deficiency results in muscular dystrophy with epidermolysis bullosa. Nat. Genet. 13: 450-457
67. Norgett E. E., Hatsell S. J., Carvajal-Huerta L., Cabezas J. C., Common J., Purkis P. E. et al. (2000) Recessive mutation in desmoplakin disrupts desmoplakin-intermediate filament interactions and causes dilated cardiomyopathy, woolly hair and keratoderma. Hum. Mol. Genet. 9: 2761-2766
68. Bomont P., Cavalier L., Blondeau F., Ben Hamida C., Belal S., Tazir M. et al. (2000) The gene encoding gigaxonin, a new member of the cytoskeletal BTB/kelch repeat family, is mutated in giant axonal neuropathy. Nat. Genet. 26: 370-374
69. Irvine A. D. and McLean W. H. (1999) Human keratin diseases: the increasing spectrum of disease and subtlety of the phenotype-genotype correlation. Br. J. Dermatol. 140: 815-828
70. Mehrani T., Wu K. C., Morasso M. I., Bryan J. T., Marekov L. N., Parry D. A. and Steinert P. M. (2001) Residues in the 1A rod domain segment and the linker L2 are required for stabilizing the A11 molecular alignment mode in keratin intermediate filaments. J. Biol. Chem. 276: 2088-2097
71. Herrmann H., Wedig T., Porter R. M., Lane E. B. and Aebi U. (2002) Characterization of early assembly intermediates of recombinant human keratins. J. Struct. Biol. 137: 82-96
72. Wu K. C., Bryan J. T., Morasso M. I., Jang S. I., Lee J. H., Yang J. M. et al. (2000) Coiled-coil trigger motifs in the 1B and 2B rod domain segments are required for the stability of keratin intermediate filaments. Mol. Biol. Cell 11: 3539-3558
73. McClintock K. A. and Shaw G. S. (2000) A logical sequence search for S100B target proteins. Protein Sci. 9: 2043-2046
74. Donato R. (1999) Functional roles of S100 proteins, calcium-binding proteins of the EF-hand type. Biochim. Biophys. Acta 1450: 191-231
75. Kirfel J., Magin T. M. and Reichelt J. (2003) Keratins: a structural scaffold with emerging functions. Cell. Mol. Life Sci. 60: 56-71
76. Brownlees J., Ackerley S., Grierson A. J., Jacobsen N. J., Shea K., Anderton B. H. et al. (2002) Charcot-Marie-Tooth disease neurofilament mutations disrupt neurofilament assembly and axonal transport. Hum. Mol. Genet. 11: 2837-2844
77. Nielsen A. L., Jorgensen P. and Jorgensen A. L. (2002) Mutations associated with a childhood leukodystrophy, Alexander disease, cause deficiency in dimerization of the cytoskeletal protein GFAP. J. Neurogenet. 16: 175-179
78. Sjoberg G., Saavedra-Matiz C. A., Rosen D. R., Wijsman E. M., Borg K., Horowitz S. H. et al. (1999) A missense mutation in the desmin rod domain is associated with autosomal dominant distal myopathy, and exerts a dominant negative effect on filament formation. Hum. Mol. Genet. 8: 2191-2198
79. Tian R., Brenner M. and Goldman J. E. (2003) Expression of Alexander disease mutant in human astrocyte results in disruption of the normal intermediate filament. J. Neurochem. 85 (Suppl. 1): 14
80. Eliasson C., Sahlgren C., Berthold C. H., Stakeberg J., Celis J. E., Betsholtz C. et al. (1999) Intermediate filament protein partnership in astrocytes. J. Biol. Chem. 274: 23996-24006
81. Castellani R. J., Perry G., Brenner D. S. and Smith M. A. (1999) Alexander disease: Alzheimer disease of the developing brain? Alzheimer Dis. Assoc. Disord. 13: 232-235
82. Wakabayashi K., Hayashi S., Yoshimoto M., Kudo H. and Takahashi H. (2000) NACP/alpha-synuclein-positive filamentous inclusions in astrocytes and oligodendrocytes of Parkinson's disease brains. Acta Neuropathol. 99: 14-20
83. Berry R. W., Quinn B., Johnson N., Cochran E. J., Ghoshal N. and Binder L. I. (2001) Pathological glial tau accumulations in neurodegenerative disease: review and case report. Neurochem. Int. 39: 469-479
84. Higuchi M., Ishihara T., Zhang B., Hong M., Andreadis A., Trojanowski J. et al. (2002) Transgenic mouse model of tauopathies with glial pathology and nervous system degeneration. Neuron 35: 433-446
85. Pramatarova A., Laganiere J., Roussel J., Brisebois K. and Rouleau G. A. (2001) Neuron-specific expression of mutant superoxide dismutase 1 in transgenic mice does not lead to motor impairment. J. Neurosci. 21: 3369-3374
86. Goldman J. E. and Corbin E. (1991) Rosenthal fibers contain ubiquitinated alpha B-crystallin. Am. J. Pathol. 139: 933-938
87. Dukan S., Farewell A., Ballesteros M., Taddei F., Radman M. and Nystrom T. (2000) Protein oxidation in response to increased transcriptional or translational errors. Proc. Natl. Acad. Sci. USA 97: 5746-5749
88. Butterfield D. A. and Kanski J. (2001) Brain protein oxidation in age-related neurodegenerative disorders that are associated with aggregated proteins. Mech. Ageing Dev. 122: 945-962
89. Castellani R. J., Perry G., Harris P. L., Cohen M. L., Sayre L. M., Salomon R. G. et al. (1998) Advanced lipid peroxidation end-products in Alexander's disease. Brain Res. 787: 15-18
90. Castellani R. J., Perry G., Harris P. L., Monnier V. M., Cohen M. L. and Smith M. A. (1997) Advanced glycation modification of Rosenthal fibers in patients with Alexander disease. Neurosci. Lett. 231: 79-82
91. Iwaki T., Kume-Iwaki A., Liem R. K. and Goldman J. E. (1989) Alpha B-crystallin is expressed in non-lenticular tissues and accumulates in Alexander's disease brain. Cell 57: 71-78
92. Haslbeck M. (2002) sHsps and their role in the chaperone network. Cell. Mol. Life Sci. 59: 1649-1657
93. Bonini N. M. (2002) Chaperoning brain degeneration. Proc. Natl. Acad. Sci. USA 99 Suppl. 4: 16407-16411
94. Richter-Landsberg C. and Goldbaum O. (2003) Stress proteins in neural cells: functional roles in health and disease. Cell. Mol. Life Sci. 60: 337-349
95. Sharp F. R., Bernaudin M., Bartels M. and Wagner K. R. (2001) Glial expression of heat shock proteins (HSPs) and oxygen-regulated proteins (ORPs). Prog. Brain Res. 132: 427-440
96. MacRae T. H. (2000) Structure and function of small heat shock/alpha-crystallin proteins: established concepts and emerging ideas. Cell. Mol. Life Sci. 57: 899-913
97. Head M. W. and Goldman J. E. (2000) Small heat shock proteins, the cytoskeleton, and inclusion body formation. Neuropathol. Appl. Neurobiol. 26: 304-312
98. Perng M. D., Cairns L., van den I. P., Prescott A., Hutcheson A. M. and Quinlan R. A. (1999) Intermediate filament interactions can be altered by HSP27 and alphaB-crystallin. J. Cell Sci. 112 (Pt 13): 2099-2112
99. Koyama Y. and Goldman J. E. (1999) Formation of GFAP cytoplasmic inclusions in astrocytes and their disaggregation by alphaB-crystallin. Am. J. Pathol. 154: 1563-1572
100. Mehlen P., Kretz-Remy C., Preville X. and Arrigo A. P. (1996) Human hsp27, Drosophila hsp27 and human alphaB-crystallin expression-mediated increase in glutathione is essential for the protective activity of these proteins against TNFalpha-induced cell death. EMBO J. 15: 2695-2706
101. Garrido C., Gurbuxani S., Ravagnan L. and Kroemer G. (2001) Heat shock proteins: endogenous modulators of apoptotic cell death. Biochem. Biophys. Res. Commun. 286:433-442
102. Auluck P. K., Chan H. Y., Trojanowski J. Q., Lee V. M. and Bonini N. M. (2002) Chaperone suppression of alpha-synuclein toxicity in a Drosophila model for Parkinson's disease. Science 295: 865-868
103. Baumann N. and Pham-Dinh D. (2001) Astrocytes. In: Encyclopedia of the Human Brain, pp. 251-268, Ramachandran V. S. (ed.), Academic Press, New York
104. Joo F. (1996) Endothelial cells of the brain and other organ systems: some similarities and differences. Prog. Neurobiol. 48: 255-273
105. Abbott N. J. (2002) Astrocyte-endothelial interactions and blood-brain barrier permeability. J. Anat. 200: 629-638
106. Bauer H. C. and Bauer H. (2000) Neural induction of the blood-brain barrier: still an enigma. Cell. Mol. Neurobiol. 20: 13-28
107. Mi H., Haeberle H. and Barres B. A. (2001) Induction of astrocyte differentiation by endothelial cells. J. Neurosci. 21: 1538-1547
108. Yoder E. J. (2002) Modifications in astrocyte morphology and calcium signaling induced by a brain capillary endothelial cell line. Glia 38: 137-145
109. Pellerin L. and Magistretti P. J. (1994) Glutamate uptake into astrocytes stimulates aerobic glycolysis: a mechanism coupling neuronal activity to glucose utilization. Proc. Natl. Acad. Sci. USA 91: 10625-10629
110. Brookes N. (2000) Functional integration of the transport of ammonium, glutamate and glutamine in astrocytes. Neurochem. Int. 37: 121-129
111. Sanchez-Abarca L. I., Tabernero A. and Medina J. M. (2001) Oligodendrocytes use lactate as a source of energy and as a precursor of lipids. Glia 36: 321-329
112. Steinhauser C. and Gallo V. (1996) News on glutamate receptors in glial cells. Trends Neurosci. 19: 339-345
113. Yuan X., Eisen A. M., McBain C. J. and Gallo V. (1998) A role for glutamate and its receptors in the regulation of oligodendrocyte development in cerebellar tissue slices. Development 125: 2901-2914
114. Hardin-Pouzet H., Krakowski M., Bourbonniere L., DidierBazes M., Tran E. et al. (1997) Glutamate metabolism is down-regulated in astrocytes during experimental allergic encephalomyelitis. Glia 20: 79-85
115. Akaoka H., Szymocha R., Beurton-Marduel P., Bernard A., Belin M. F. and Giraudon P. (2001) Functional changes in astrocytes by human T-lymphotropic virus type-1 T-lymphocytes. Virus Res. 78: 57-66
116. Werner P., Pitt D. and Raine C. S. (2001) Multiple sclerosis: altered glutamate homeostasis in lesions correlates with oligodendrocyte and axonal damage. Ann. Neurol. 50: 169-180
117. Chan H., Hazell A. S., Desjardins P and Butterworth R. F. (2000) Effects of ammonia on glutamate transporter (GLAST) protein and mRNA in cultured rat cortical astrocytes. Neurochem. Int. 37: 243-248
118. Lievens J. C., Woodman B., Mahal A., Spasic-Boscovic O., Samuel D., Kerkerian-Le Goff L. et al. (2001) Impaired glutamate uptake in the R6 Huntington's disease transgenic mice. Neurobiol. Dis. 8: 807-821
119. Trotti D., Rolfs A., Danbolt N. C., Brown R. H. Jr and Hediger M. A. (1999) SOD1 mutants linked to amyotrophic lateral sclerosis selectively inactivate a glial glutamate transporter. Nat. Neurosci. 2: 848
120. Fern R. and Moller T. (2000) Rapid ischemic cell death in immature oligodendrocytes: a fatal glutamate release feedback loop. J. Neurosci. 20: 34-42
121. Tekkok S. B. and Goldberg M. P. (2001) Ampa/kainate receptor activation mediates hypoxic oligodendrocyte death and axonal injury in cerebral white matter. J. Neurosci. 21: 4237-4248
122. Matute C., Sanchez-Gomez M. V., Martinez-Millan L. and Miledi R. (1997) Glutamate receptor-mediated toxicity in optic nerve oligodendrocytes. Proc. Natl. Acad. Sci. USA 94: 8830-8835
123. Matute C., Alberdi E., Domercq M., Perez-Cerda F., Perez-Samartin A. and Sanchez-Gomez M. V. (2001) The link between excitotoxic oligodendroglial death and demyelinating diseases. Trends Neurosci. 24: 224-230
124. McDonald J. W., Althomsons S. P., Hyrc K. L., Choi D. W. and Goldberg M. P. (1998) Oligodendrocytes from forebrain are highly vulnerable to AMPA/kainate receptor-mediated excitotoxicity. Nat. Med. 4: 291-297
125. Volterra A., Trotti D., Tromba C., Floridi S. and Racagni G. (1994) Glutamate uptake inhibition by oxygen free radicals in rat cortical astrocytes. J. Neurosci. 14: 2924-2932
126. Trotti D., Rossi D., Gjesdal O., Levy L. M., Racagni G., Danbolt N. C. et al. (1996) Peroxynitrite inhibits glutamate transporter subtypes. J. Biol.Chem. 271: 5976-5979
127. Trotti D., Danbolt N. C. and Volterra A. (1998) Glutamate transporters are oxidant-vulnerable: a molecular link between oxidative and excitotoxic neurodegeneration? Trends Pharmacol. Sci. 19: 328-334
128. Peuchen S., Bolanos J. P., Heales S. J., Almeida A., Duchen M. R. and Clark J. B. (1997) Interrelationships between astrocyte function, oxidative stress and antioxidant status within the central nervous system. Prog. Neurobiol. 52: 261-281
129. Dringen R. (2000) Metabolism and functions of glutathione in brain. Prog. Neurobiol. 62: 649-671
130. Husain J. and Juurlink B. H. (1995) Oligodendroglial precursor cell susceptibility to hypoxia is related to poor ability to cope with reactive oxygen species. Brain Res. 698: 86-94
131. Mouzannar R., Miric S. J., Wiggins R. C. and Konat G. W. (2001) Hydrogen peroxide induces rapid digestion of oligodendrocyte chromatin into high molecular weight fragments. Neurochem. Int. 38: 9-15
132. Smith K. J., Kapoor R. and Felts P. A. (1999) Demyelination: the role of reactive oxygen and nitrogen species. Brain Pathol. 9: 69-92
133. Juurlink B. H., Thorburne S. K. and Hertz L. (1998) Peroxide-scavenging deficit underlies oligodendrocyte susceptibility to oxidative stress. Glia 22: 371-378
134. Yonezawa M., Back S. A., Gan X., Rosenberg P. A. and Volpe J. J. (1996) Cystine deprivation induces oligodendroglial death: rescue by free radical scavengers and by a diffusible glial factor. J. Neurochem. 67: 566-573
135. Corley S. M., Ladiwala U., Besson A. and Yong V W. (2001) Astrocytes attenuate oligodendrocyte death in vitro through an alpha(6) integrin-laminin-dependent mechanism. Glia 36: 281-294
136. Araque A., Carmignoto G. and Haydon P G. (2001) Dynamic signaling between astrocytes and neurons. Annu. Rev. Physiol. 63: 795-813
137. Bezzi P. and Volterra A. (2001) A neuron-glia signalling network in the active brain. Curr. Opin. Neurobiol. 11: 387-394
138. Rouach N., Glowinski J. and Giaume C. (2000) Activity-dependent neuronal control of gap-junctional communication in astrocytes. J. Cell. Biol. 149: 1513-1526
139. Ullian E. M., Sapperstein S. K., Christopherson K. S. and Barres B. A. (2001) Control of synapse number by glia. Science 291: 657-661
140. Nishiyama H., Knopfel T., Endo S. and Itohara S. (2002) Glial protein S100B modulates long-term neuronal synaptic plasticity. Proc. Natl. Acad. Sci. USA 99: 4037-4042
141. Paznekas W. A., Boyadjiev S. A., Shapiro R. E., Daniels O., Wollnik B., Keegan C. E. et al. (2003) Connexin 43 (GJA1) mutations cause the pleiotropic phenotype of oculodentodigital dysplasia. Am. J. Hum. Genet. 72: 408-418
142. Loddenkemper T., Grote K., Evers S., Oelerich M. and Stogbauer F. (2002) Neurological manifestations of the oculodentodigital dysplasia syndrome. J. Neurol. 249: 584-595
143. Bolanos J. P. and Medina J. M. (1996) Induction of nitric oxide synthase inhibits gap junction permeability in cultured rat astrocytes. J. Neurochem. 66: 2091-2099
144. Kommers T., Rodnight R., Boeck C., Vendite D., Oliveira D., Horn J. et al. (2002) Phosphorylation of glial fibrillary acidic protein is stimulated by glutamate via NMDA receptors in cortical microslices and in mixed neuronal/ glial cell cultures prepared from the cerebellum. Brain Res. Dev. Brain Res. 137: 139-148
145. Donato R. (2001) S100: a multigenic family of calcium-modulated proteins of the EF-hand type with intracellular and extracellular functional roles. Int. J. Biochem. Cell Biol. 33: 637-668
146. Cotrina M. L., Lin J. H. and Nedergaard M. (1998) Cytoskeletal assembly and ATP release regulate astrocytic calcium signaling. J. Neurosci. 18: 8794-8804
147. Baumann N. and Pham-Dinh D. (2001) Biology of oligodendrocyte and myelin in the mammalian central nervous system. Physiol. Rev. 81:871-927
148. Schnadelbach O. and Fawcett J. W. (2001) Astrocyte influences on oligodendrocyte progenitor migration. Prog. Brain Res. 132: 97-102
149. Sakurai Y., Nishimura D., Yoshimura K., Tsuruo Y., Seiwa C. and Asou H. (1998) Differentiation of oligodendrocyte occurs in contact with astrocyte. J. Neurosci. Res. 52: 17-26
150. Yoshimura K., Sakurai Y., Nishimura D., Tsuruo Y., Nomura M., Kawato S. et al. (1998) Monoclonal antibody 14F7, which recognizes a stage-specific immature oligodendrocyte surface molecule, inhibits oligodendrocyte differentiation mediated in co-culture with astrocytes. J. Neurosci. Res. 54: 79-96
151. Bhat S. and Pfeiffer S. E. (1986) Stimulation of oligodendrocytes by extracts from astrocyte-enriched cultures. J. Neurosci. Res. 15: 19-27
152. Oh L. Y. and Yong V. W. (1996) Astrocytes promote process outgrowth by adult human oligodendrocytes in vitro through interaction between bFGF and astrocyte extracellular matrix. Glia 17: 237-253
153. Meyer-Franke A., Shen S. and Barres B. A. (1999) Astrocytes induce oligodendrocyte processes to align with and adhere to axons. Mol. Cell. Neurosci. 14: 385-397
154. Komoly S., Hudson L. D., Webster H. D. and Bondy C. A. (1992) Insulin-like growth factor I gene expression is induced in astrocytes during experimental demyelination. Proc. Natl. Acad. Sci. USA 89: 1894-1898
155. Franklin R. J., Crang A. J. and Blakemore W. F. (1993) The role of astrocytes in the remyelination of glia-free areas of demyelination. Adv. Neurol. 59: 125-133
156. Mason J. L., Ye P., Suzuki K., D'Ercole A. J. and Matsushima G. K. (2000) Insulin-like growth factor-1 inhibits mature oligodendrocyte apoptosis during primary demyelination. J. Neurosci. 20: 5703-5708
157. Rash J. E., Yasumura T., Dudek F. E. and Nagy J. I. (2001) Cell-specific expression of connexins and evidence of restricted gap junctional coupling between glial cells and between neurons. J. Neurosci. 21: 1983-2000
158. Barres B. A., Hart I. K., Coles H. S., Burne J. F., Voyvodic J. T., Richardson W. D. et al. (1992) Cell death and control of cell survival in the oligodendrocyte lineage. Cell 70: 31-46
159. Stankoff B., Aigrot M. S., Noel F., Wattilliaux A., Zalc B. and Lubetzki C. (2002) Ciliary neurotrophic factor (CNTF) enhances myelin formation: a novel role for CNTF and CNTF-related molecules. J. Neurosci. 22: 9221-9227
160. John G. R., Shankar S. L., Shafit-Zagardo B., Massimi A., Lee S. C., Raine C. S. et al. (2002) Multiple sclerosis: re-expression of a developmental pathway that restricts oligodendrocyte maturation. Nat. Med. 8: 1115-1121
161. Novelli G., Muchir A., Sangiuolo F., Helbling-Leclerc A., D'Apice M. R., Massart C. et al. (2002) Mandibuloacral dysplasia is caused by a mutation in LMNA-encoding lamin A/C. Am. J. Hum. Genet. 71: 426-431
162. Berry V., Francis P., Reddy M. A., Collyer D., Vithana E., MacKay I. et al. (2001) Alpha-B crystallin gene (CRYAB) mutation causes dominant congenital posterior polar cataract in humans. Am. J. Hum. Genet. 69: 1141-1145