Accumulation of tau in autophagic vacuoles in chloroquine myopathy

Journal of Neuropathology and Experimental Neurology

Volumn 57, Issue 7, 1998, Pages 664-673

  Murakami, Nobuyuki ^a,b   Oyama, Fumitaka ^c   Gu, Yongjun ^c   McLennan, Ian S ^a   Nonaka, Ikuya ^b   Ihara, Yasuo ^c,d  

^a UNIVERSITY OF OTAGO   (New Zealand)

^b NATIONAL INSTITUTE OF MENTAL HEALTH   (Japan)

^c UNIVERSITY OF TOKYO   (Japan)

^d JAPAN SCIENCE AND TECHNOLOGY AGENCY   (Japan)

Author keywords

Alzheimer disease; Chloroquine myopathy; Lysosome; Paired helical filaments; Rimmed vacuole; Tau

Indexed keywords

AMYLOID PRECURSOR PROTEIN; CHLOROQUINE; MESSENGER RNA; TAU PROTEIN;

ALZHEIMER DISEASE; ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; ARTICLE; AUTOPHAGY; BIOACCUMULATION; CELL VACUOLE; CONTROLLED STUDY; IMMUNOCYTOCHEMISTRY; IMMUNOELECTRON MICROSCOPY; LYSOSOME; MALE; MYOPATHY; NONHUMAN; PRIORITY JOURNAL; RAT;

EID: 0031864997     PISSN: 00223069     EISSN: None     Source Type: Journal    
DOI: 10.1097/00005072-199807000-00003     Document Type: Article

References (46)

1. Kanai Y, Takemura R, Oshima T, et al. Expression of multiple tau isoforms and microtubule bundle formation in fibroblasts transfected with a single tau cDNA. J Cell Biol 1989;109:1173-84
2. Morishima-Kawashima M, Hasegawa M, Takio K, Suzuki M, Titani K, Ihara Y. Proline-directed and non-proline-directed phosphorylation of PHF-tau. J Biol Chem 1995;270:823-29
3. Couchie D, Mavilia C, Georgieff IS, et al. Primary structure of high molecular weight tau present in the peripheral nervous system. Proc Natl Acad Sci USA 1992;89:4378-81
4. Goedert M, Spillantini MG, Crowther RA. Cloning of a big tau microtubule-associated protein characteristic of the peripheral nervous system. Proc Natl Acad Sci USA 1992;89:1983-87
5. Himmler A. Structure of the bovine tau gene: Alternatively spliced transcripts generate a protein family. Mol Cell Biol 1989;9:1389-96
6. Kosik KS, Orecchio LD, Bakalis S, Neve RL. Developmentally regulated expression of specific tau sequences. Neuron 1989;2: 1389-97
7. Goedert M, Spillantini MG, Jakes R, Rutherford D, Crowther RA. Multiple isoforms of human microtubule-associated protein tau: Sequences and localization in neurofibrillary tangles of Alzheimer's disease. Neuron 1989;3:519-26
8. Askanas V, Engel KW, Bilak M, Alvare RB, Selkoe DJ. Twisted tubulofilaments of inclusion-body myositis muscle resemble paired helical filaments of Alzheimer brain and contain hyperphosphorylated tau. Am J Pathol 1994;144:177-87
9. Murakami N, Ishiguro K, Ihara Y, Nonaka I, Sugita H, Imahori K. Tau protein immunoreactivity in muscle fibers with rimmed vacuoles differs from that in regenerating muscle fibers. Acta Neuropathol 1995;90:467-71
10. Murakami N, Ihara Y, Nonaka I. Chloroquine treated rat: A possible model for Alzheimer's disease. Muscle Nerve 1995;18:123-25
11. Gu Y, Oyama F, Ihara Y. T is widely expressed in rat tissues. J Neurochem 1996;67:1235-44
12. Holtzman E. Lysosomes. New York: Plenum Press, 1989
13. MacDonald RD, Engel AG. Experimental Chloroquine myopathy. J Neuropathol Exp Neurol 1970;29:479-99
14. Sugita H, Higuchi I, Sano M, Ishiura S. Trial of a cysteine protenase inhibitor, EST, in experimental Chloroquine myopathy in rats. Muscle Nerve 1987;10:516-23
15. Neve RL, Rogers J, Higgins GA. The Alzheimer amyloid precursor-related transcript lacking the β/A4 sequence is specifically increased in Alzheimer's disease brain. Neuron 1990;5:329-38
16. Liu W-K, Moore WT, Williams RT, Hall FL, Yen S-H. Application of synthetic phospho-and unphospho-peptides to identify phosphorylation sites in a subregion of the tau molecule, which is modified in Alzheimer's disease. J Neurosci Res 1993;34:371-76
17. Szendrei GI, Lee VM-Y, Otvos L Jr. Recognition of the minimal epitope of monoclonal antibody tau-1 depends upon the presence of phosphate group but not its location. J Neurosci Res 1993;34: 243-49
18. Hasegawa M, Watanabe A, Takio K, et al. Characterization of two distinct monoclonal antibodies to paired helical filaments (PHF) - Further evidence for fetal-type phosphorylation of the tau in PHF -. J Neurochem 1993;60:2068-77
19. Kosik KS, Orecchio LD, Binder L, Trojanowski JQ, Lee VM-Y, Lee G. Epitopes that span the tau molecule are shared with neurofibrillary tangles. Neuron 1988;1:817-25
20. Koo EH, Squazzo SL. Evidence that production and release of amyloid β-protein involves the endocytic pathway. J Biol Chem 1994; 269:17386-89
21. Takio K, Hasegawa M, Titani K, Ihara Y. Identification of β-protein precursor in newborn rat brain. Biochem Biophys Res Commun 1989;160:1296-1301
22. Barka T A simple azo-dye method for histochemical demonstration of acid phosphatase. Nature 1960;187:248-49
23. Tsuzuki K, Fukatsu R, Takamaru Y, et al. Co-localization of amyloid-associated proteins with amyloid β in rat soleus muscle in chloroquine-induced myopathy: A possible model for amyloid β formation in Alzheimer' s disease. Brain Res 1995;699:260-65
24. Haass C, Koo EH, Mellon A, Hung AY, Selkoe DJ. Targeting of cell-surface β-amyloid precursor protein to lysosomes: alternative processing into amyloid-bearing fragments. Nature 1992;359:322-25
25. Golde TE, Estus S, Younkin LH, Selkoe DJ, Younkin SG. Processing of the amyloid protein precursor to potentially amyloido-genic derivatives. Science 1992;255:728-30
26. Oyama F, Shimada H, Oyama R, Titani K, Ihara Y. A novel correlation between the levels of β-amyloid protein precursor and T transcripts in the aged human brain. J Neurochem 1992;59:1117-25
27. Irving EA, Nicoll J, Graham DI, Dewar D. Increased tau immunoreactivity in oligodendrocytes following human stroke and head injury. Neurosci Lett 1996;213:189-92
28. Le WD, Xie WJ, Kong R, Appel SH. β-amyloid-induced neurotoxicity of a hybrid septal cell line associated with increased tau phosphorylation and expression of β-amyloid precursor protein. J Neurochem 1997;69:978-85
29. Mahley RW. Apolipoprotein E: Cholesterol transport protein with expanding role in cell biology. Science 1988;240:622-30
30. Selkoe DJ. Normal and abnormal biology of the β-amyloid precursor protein. Annu Rev Neurosci 1994;17:489-517
31. Caporaso GL, Gandy SE, Buxbaum JD, Greengard P Chloroquine inhibits intracellular degradation but not secretion of Alzheimer β/ A4 amyloid precursor protein. Proc Natl Acad Sci USA 1992;89: 2252-56
32. Gerard KW, Schneider DL. Evidence for degradation of myofibrillar proteins in lysosomes. J Biol Chem 1988;263:18886-90
33. Kumamoto T, Araki S, Watanabe S, Ikebe N, Fukuhara N. Experimental chloroquine myopathy: morphological and biochemical studies. Eur Neurol 1989;29:202-7
34. Ii K, Hizawa K, Nonaka I, Sugita H, Kominami E, Katunuma N. Abnormal increases of lysosomal cysteinine proteinases in rimmed vacuoles in the skeletal muscle. Am J Pathol 1986;122:193-98
35. Kawai M, Cras P, Richey P, et al. Subcellular localization of amyloid precursor protein in senile plaque of Alzheimer's disease. Am J Pathol 1992;255:728-30
36. Terlecky SR, Dice JF. Polypeptide import and degradation by isolated lysosomes. J Biol Chem 1993;268:23490-95
37. Aniento F, Roche E, Cuervo AM, Knecht E. Uptake and degradation of glyceraldehyde-3-phosphate dehydrogenase by rat liver lysosomes. J Biol Chem 1993;268:10463-70
38. Cuervo AM, Terlecky SR, Dice JF, Knecht E. Selective binding and uptake of ribonuclease A and glyceraldehyde-3-phosphate dehydrogenase by isolated rat liver lysosomes. J Biol Chem 1994;269: 26374-80
39. Aniento F, Papavassiliou AG, Knecht E, Roche E. Selective uptake and degradation of c-Fos and v-Fos by rat liver lysosomes. FEBS Lett 1996;390:47-52
40. Chiang H-L, Terlecky SR, Plant CP, Dice JF. A role for a 70-kilodalton heat shock protein in lysosomal degradation of intracellular proteins. Science 1989;246:382-85
41. Cuervo AM, Dice JF A receptor for the selective uptake and degradation of proteins by lysosomes. Science 1996;273:501-3
42. Green LAD, Liem RKH. β-Internexin is a microtubule-associated protein identical to the 70-kDa heat-shock cognate protein and the clathrin uncoating ATPase. J Biol Chem 1989;264:15210-15
43. Hamos JE, Oblas B, Pulaski-Salo D, Welch WJ. Bole DG, Drachman DA. Expression of heat shock proteins in Alzheimer's disease. Neurology 1991;41:345-50
44. Ivy GO, Kitani K, Ihara Y. Anomalous accumulation of tau and ubiquitin immunoreactivities in rat brain caused by protease inhibition and by normal aging: A clue to PHF pathogenesis? Brain Res 1989;498:360-65
45. Cataldo AM, Barnett JL, Berman SA, et al. Gene expression and cellular content of cathepsin D in Alzheimer's disease brain: Evidence for early up-regulation of the endosomal-lysosomal system. Neuron 1995;14:671-80
46. Cataldo AM, Paskevich PA, Kominami E, Nixon RA. Lysosomal hydrolases of different classes are abnormally distributed in brains of patients with Alzheimer's disease. Proc Natl Acad Sci USA 1991;88:10998-11002