Newest pathogenetic considerations in inclusion-body myositis: possible role of amyloid-beta, cholesterol, relation to aging and to Alzheimer's disease.

被引：13

作者：

Askanas V. ^{[1
]}

Engel W.K. ^{[1
]}

机构：

[1] University of Southern California Neuromuscular Center, Good Samaritan Hospital, 637 South Lucas Avenue, Los Angeles, 90017-1912, CA

来源：

Current Rheumatology Reports | 2002年 / 4卷 / 5期

关键词：

Myositis; Inflammatory Muscle Disease; Pathogenetic Consideration; Vacuolated Muscle Fiber; Abnormal Muscle Fiber;

D O I：

10.1007/s11926-002-0088-8

中图分类号：

学科分类号：

摘要：

This report summarizes clinical features and diagnostic criteria, and the newest advances related to seeking the pathogenic mechanism(s) of sporadic inclusion-body myositis. On the basis of the authors' research, several processes seem to be important in relation to the still-speculative pathogenesis: increased transcription and accumulation of amyloid-b precursor protein and accumulation of its proteolytic fragment amyloid-b; abnormal accumulation of components related to lipid metabolism (eg, low-density lipoprotein receptors and cholesterol; accumulation of cholesterol is possibly caused by its abnormal trafficking); oxidative stress; accumulations of other Alzheimer-related proteins including phosphorylated tau; a milieu of muscle cellular aging in which these changes occur. The authors' basic hypothesis is that overexpression of amyloid-b precursor protein within the aging muscle fibers is an early upstream event causing the subsequent pathogenic cascade. The remarkable pathologic similarities between inclusion-body myositis muscle and Alzheimer's disease brain are discussed.

引用

页码：427 / 433

页数：6

共 136 条

[31]

Askanas V(2000)Cultured muscle fibers from Iranian Jewish patients with quadriceps-sparing autosomalrecessive inclusion-body myopathy (AR1-IBM) express features of IBM phenotype Neurology 54 A438-A438

[32]

Alvarez RB(1998)Impaired innervation of cultured human muscle overexpressing âAPP experimentally and genetically: relevance to inclusion-body myopathies Neuroreport 9 3201-3205

[33]

Mirabella M(1996)The pathogenesis of Alzheimer disease: an alternative to the amyloid hypothesis J Neuropathol Exp Neurol 55 1023-1025

[34]

Engel WK(1998)Fourteen newly recognized proteins at the human neuromuscular junctions— and their non-junctional accumulation in inclusion-body myositis Ann N Y Acad Sci 841 28-56

[35]

Askanas V(1998)Transgenic mice overexpressing the C-99 fragment of betaPP with an alpha-s myopathy similar to human inclusion body myositis Am J Pathol 153 1679-1686

[36]

Serdaroglu P(1998)Amyloid-beta deposition in skeletal muscle of transgenic mice: possible model of inclusion body myopathy Am J Pathol 153 1687-1693

[37]

Engel WK(1999)The mammalian lowdensity lipoprotein receptor family Annu Rev Nutr 19 141-172

[38]

Alvarez RB(2000)Modulation of betaamyloid precursor protein processing by the low density lipoprotein receptor-related protein (LRP): evidence that LRP contributes to the pathogenesis of Alzheimer’s disease J Biol Chem 275 7410-7415

[39]

Prayson RA(2002)Three lipoprotein receptors and cholesterol in inclusion-body myositis muscle Neurology 58 438-445

[40]

Cohen ML(2000)Apolipoprotein E and Alzheimer disease: an update on genetic and functional analyses J Neuropathol Exp Neurol 59 751-758

← 1 2 3 4 5 6 7 8 9 10 →