Regular Articleβ-Amyloid Peptide Expression Is Sufficient for Myotube Death: Implications for Human Inclusion Body Myopathy
References (73)
- et al.
Impairment in learning and memory accompanied by neurodegeneration in mice transgenic for the carboxyl-terminus of the amyloid precursor protein
Mol. Brain Res.
(1999) Apoptosis decision cascades and neuronal degeneration in Alzheimer's disease
Neurobiol. Aging
(1998)- et al.
Generation of bA4 from the amyloid precursor and fragments thereof
FEBS Lett.
(1993) - et al.
Amyloid-beta deposition in skeletal muscle of transgenic mice. Possible model of Inclusion Body Myopathy
Am. J. Pathol.
(1998) - et al.
Filamentous nerve cell inclusions in neurodegenerative diseases
Curr. Opin. Neurobiol.
(1998) - et al.
Transgenic mice over-expressing the C-99 fragment of βPP with an α-secretase site mutation develop a myopathy similar to human inclusion body myositis
Am. J. Pathol.
(1998) - et al.
Beta-amyloid induces apoptosis in human-derived neurotypic Sh-SY5Y cells
Brain Res.
(1996) - et al.
A novel substrate for analyzing Alzheimer's disease gamma-secretase
FEBS Lett.
(1999) - et al.
Neuronal expression of β-amyloid precursor protein Alzheimer mutations causes intracellular accumulation of a C-terminal fragment containing both the amyloid β and cytoplasmic domains
J. Biol. Chem.
(1997) - et al.
Alzheimer's disease: A reexamination of the amyloid hypothesis
Trends Neurosci.
(1998)
Bcl-2 and Bax protein expression in human myopathies
J. Neurol. Sci.
Huntingtin acts in the nucleus to induce apoptosis but death does not correlate with formation of intranuclear inclusions
Cell
Aberrant expression of bcl-2 gene family in Down's syndrome brains
Brain Res. Mol. Brain Res.
Evidence for apoptotic cell death in Alzheimer's disease
Exp. Neurol.
Cytotoxicity mediated by conditional expression of a carboxyl-terminal derivative of the β-amyloid precursor protein
Mol. Brain Res.
Endonuclease activities associated with high molecular weight and internucleosomal DNA fragmentation in apoptosis
Exp. Cell. Res.
Caspace cleavage of gene products associated with triplet expansion disorders generates truncated fragments containing the polyglutamine tract
J. Biol. Chem.
Intracellular generation and accumulation of amyloid β-peptide terminating at amino acid 42
J. Biol. Chem.
Signal Sequences: The same yet different
Cell
Myogenin expression, cell cycle withdrawal and phenotypic differentiation are temporally separable events that precede cell fusion upon myogenesis
J. Cell Biol.
β-Amyloid precursor epitopes in muscle fibers of inclusion body myositis
Ann. Neurol.
Use of anti-neurofilament antibody to identify paired-helical filaments in inclusion-body myositis
Ann. Neurol.
Sporadic inclusion-body myositis and hereditary inclusion-body myopathies
Arch. Neurol.
New advances in the understanding of sporadic inclusion-body myositis and hereditary inclusion-body myopathies
Curr. Opin. Rheumatol.
Light and electron microscopic localization of β-amyloid protein in muscle biopsies of patients with inclusion-body myositis
Am. J. Pathol.
Twisted tubulofilaments of inclusion-body myositis muscle resemble paired helical filaments of Alzheimer brain and contain hyperphosphorylated tau
Am. J. Pathol.
Inclusion body myositis: Explanation for poor response to immunosuppressive therapy
Neurology
Synergistic effect of β-amyloid protein and interferon gamma on nitric oxide production by C2C12 muscle cells
Brain
Cytotoxic mechanisms in inflammatory myopathies
Brain
Determination of the length of the histological stages of apoptosis in normal liver and in altered hepatic foci of rats
Carcinogenesis
Overexpression in neurons of human presenilin-1 or a presenilin-1 familial Alzheimer's disease mutant does not enhance apoptosis
J. Neurosci.
Alzheimer's Aβ(1–42) is generated in the endoplasmic reticulum/intermediate compartment of NT2N cells
Nature Med.
Inclusion body myositis: Pathologic changes
Apoptosis mediated neurotoxicity induced by chronic application of β amyloid fragment 25–35
NeuroReport
Upregulation of Fas/Fas ligand in inclusion body myositis
Ann. Neurol.
βPP and Tau interaction. A possible link between amyloid and neurofibrillary tangles in Alzheimer's disease
Am. J. Pathol.
Cited by (40)
Detection of Aβ-interacting proteins via a novel Aβ-adsorbents that use immobilized regular comb polymer
2014, Journal of Chromatography B: Analytical Technologies in the Biomedical and Life SciencesCitation Excerpt :Aβ is the main component of amyloid plaques in the brains of AD patients. Similar Aβ plaques are also found in some variants of Lewy body dementia [7] and inclusion body myositis [8]. Furthermore, Aβ aggregates can coat cerebral blood vessels in cerebral amyloid angiopathy [9].
Foxo/Atrogin induction in human and experimental myositis
2012, Neurobiology of DiseaseCitation Excerpt :Necrosis and inflammation are generally more pronounced in PM. Muscle myofiber apoptosis, whether nonexistent (Nagaraju et al., 2000; Schneider et al., 1996) or present but rare in sIBM and hereditary (h)IBM (Hutchinson, 1998; Querfurth et al., 2001; Yan et al., 2001) cannot account for the loss. Yet, the possibility that the extent of apoptosis in degenerative muscle diseases is underrated has been raised (Amsili et al., 2007; Tews, 2002).
Peracetylated N-acetylmannosamine, a synthetic sugar molecule, efficiently rescues muscle phenotype and biochemical defects in mouse model of sialic acid-deficient myopathy
2012, Journal of Biological ChemistryCitation Excerpt :However, hyposialylation of NEP, a catabolic enzyme for Aβ peptides, has been hypothesized to cause disturbance of amyloid metabolism at least in DMRV/hIBM (26). As amyloid deposits within myofibers precede the occurrence of rimmed vacuoles and muscle degeneration in DMRV/hIBM mice (18) and amyloid has been shown to exert toxicity in muscle cells (44), the NEP hypothesis may be a reasonable platform to explain the pathomechanism of DMRV/hIBM on the basis of hyposialylation and its effect on the progression of the disease. In this study, we demonstrated that NEP is hyposialylated and has reduced enzyme activity, and this occurs together with the increase in the amyloid burden within skeletal muscles in symptomatic DMRV/hIBM mice.
Amyloid beta peptides in human plasma and tissues and their significance for Alzheimer's disease
2009, Alzheimer's and DementiaCitation Excerpt :The cholinergic neuromuscular junctions of skeletal muscle are another potentially rich source of Aβ peptides [2,60,61]. The production of Aβ peptides is exacerbated in inclusion body myositis, the most common skeletal muscle inflammatory disease among the elderly [61–63]. Our studies revealed significant differences in Aβ42 and total Aβ between AD and ND control populations.
Amyloid toxicity in skeletal myoblasts: Implications for inclusion-body myositis
2008, Archives of Biochemistry and BiophysicsCitation Excerpt :IBM is a debilitating disorder, its diagnostic method and molecular basis of pathogenesis remains poorly defined. It has been previously reported that cytotoxicity of overexpressed β-amyloid in cultured skeletal muscle fibers [56]. Increased amount of deposition of multiple subfragments of β-amyloid precursor protein as amyloid aggregates were observed in muscle fibers from IBM biopsies [57].
Inclusion body myositis
2008, Revue du Rhumatisme (Edition Francaise)
- 1
To whom correspondence and reprint requests should be addressed. Fax: (617) 789-5177. E-mail: [email protected].