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Genomes and GenesSpecies | Valerie AskanasSummaryAffiliation: University of Southern California Country: USA Publications
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Publications
Transthyretin Val122Ile, accumulated Abeta, and inclusion-body myositis aspects in cultured muscleValerie Askanas
USC Neuromuscular Center, Department of Neurology, University of Southern California Keck School of Medicine, Good Samaritan Hospital, Los Angeles 90017 1912, USA
Neurology 61:257-60. 2003..These abnormalities are never present in normal human CMF. These perturbations were greatly increased after Abeta precursor protein gene transfer. The TTR mutation may be a genetic predisposition factor for the patient's IBM...- Proposed pathogenetic cascade of inclusion-body myositis: importance of amyloid-beta, misfolded proteins, predisposing genes, and agingValerie Askanas
Department of Neurology, University of Southern California, Keck School of Medicine, Good Samaritan Hospital, Los Angeles, California 90017 1912, USA
Curr Opin Rheumatol 15:737-44. 2003.... - Sporadic inclusion-body myositis: a proposed key pathogenetic role of the abnormalities of the ubiquitin-proteasome system, and protein misfolding and aggregationV Askanas
USC Neuromuscular Center, Department of Neurology, University of Southern California Keck School of Medicine, Good Samaritan Hospital, Los Angeles, California 90017 1912, USA
Acta Myol 24:17-24. 2005..This evidence strongly suggests that mechanisms other than the immune/inflammatory response play the important role in s-IBM muscle fiber degeneration... - Inclusion-body myositis: clinical, diagnostic, and pathologic aspectsW King Engel
The Neuromuscular Center, Department of Neurology, University of Southern California Keck School of Medicine, Good Samaritan Hospital, Los Angeles, CA, USA
Neurology 66:S20-9. 2006..Available treatments are of only slight, temporary benefit for only some s-IBM patients, indicating a desperate need for definitive therapies... - Unfolding story of inclusion-body myositis and myopathies: role of misfolded proteins, amyloid-beta, cholesterol, and agingValerie Askanas
USC Neuromuscular Center, Department of Neurology, University of Southern California Keck School of Medicine, Good Samaritan Hospital, Los Angeles, CA 90017 1912, USA
J Child Neurol 18:185-90. 2003..We discuss a potentially very important role of unfolded and/or misfolded proteins as a possible mechanism in the formations of the inclusion bodies and other abnormalities... - Inclusion-body myositis and myopathies: different etiologies, possibly similar pathogenic mechanismsValerie Askanas
USC Neuromuscular Center, Department of Neurology, University of Southern California Keck School of Medicine, Good Samaritan Hospital, Los Angeles, California 90017, USA
Curr Opin Neurol 15:525-31. 2002..Sporadic inclusion-body myositis (s-IBM) and hereditary inclusion body myopathies are progressive muscle diseases that lead to severe disability. We discuss recent advances in illuminating their pathogenic mechanism(s)... - Newest pathogenetic considerations in inclusion-body myositis: possible role of amyloid-beta, cholesterol, relation to aging and to Alzheimer's diseaseValerie Askanas
University of Southern California Neuromuscular Center, Good Samaritan Hospital, 637 South Lucas Avenue, Los Angeles, CA 90017 1912, USA
Curr Rheumatol Rep 4:427-33. 2002..The remarkable pathologic similarities between inclusion-body myositis muscle and Alzheimer's disease brain are discussed... - Homocysteine-induced endoplasmic reticulum protein (Herp) is up-regulated in sporadic inclusion-body myositis and in endoplasmic reticulum stress-induced cultured human muscle fibersAnna Nogalska
USC Neuromuscular Center, Department of Neurology, University of Southern California Keck School of Medicine, Good Samaritan Hospital, Los Angeles, California 90017-1912, USA
J Neurochem 96:1491-9. 2006.... - Endoplasmic reticulum stress induces myostatin precursor protein and NF-kappaB in cultured human muscle fibers: relevance to inclusion body myositisAnna Nogalska
Department of Neurology, USC Neuromuscular Center, University of Southern California Keck School of Medicine, Good Samaritan Hospital, 637 S Lucas Avenue, Los Angeles, CA 90017, USA
Exp Neurol 204:610-8. 2007.... - Amyloid-beta42 is preferentially accumulated in muscle fibers of patients with sporadic inclusion-body myositisGaetano Vattemi
USC Neuromuscular Center, Department of Neurology, University of Southern California Keck School of Medicine, Good Samaritan Hospital, Los Angeles, CA, 90017, USA
Acta Neuropathol 117:569-74. 2009..Thus, in s-IBM muscle fibers, Abeta42 is accumulated more than Abeta40. We suggest that Abeta42 oligomers and their cytotoxicity may play an important role in the s-IBM pathogenesis... - p62/SQSTM1 is overexpressed and prominently accumulated in inclusions of sporadic inclusion-body myositis muscle fibers, and can help differentiating it from polymyositis and dermatomyositisAnna Nogalska
Department of Neurology, USC Neuromuscular Center, Good Samaritan Hospital, University of Southern California Keck School of Medicine, Los Angeles, CA 90017 1912, USA
Acta Neuropathol 118:407-13. 2009.... - Inclusion-body myositis: a myodegenerative conformational disorder associated with Abeta, protein misfolding, and proteasome inhibitionValerie Askanas
USC Neuromuscular Center, Department of Neurology, University of Southern California Keck School of Medicine, Good Samaritan Hospital, Los Angeles, CA, USA
Neurology 66:S39-48. 2006.... - NOGO is increased and binds to BACE1 in sporadic inclusion-body myositis and in A beta PP-overexpressing cultured human muscle fibersSlawomir Wojcik
USC Neuromuscular Center, Department of Neurology, University of Southern California Keck School of Medicine, Good Samaritan Hospital, 637 S Lucas Ave, Los Angeles, CA 90017 1912, USA
Acta Neuropathol 114:517-26. 2007..However, the increase of Nogo-B seems insufficient because A beta continues to accumulate and the disease progresses. We propose that manipulations, which increase Nogo-B in s-IBM muscle might offer a new therapeutic opportunity... - Sporadic inclusion-body myositis: conformational multifactorial ageing-related degenerative muscle disease associated with proteasomal and lysosomal inhibition, endoplasmic reticulum stress, and accumulation of amyloid-?42 oligomers and phosphorylated tauValerie Askanas
University of Southern California Keck School of Medicine, Good Samaritan Hospital, USC Neuromuscular Centre, Department of Neurology, Los Angeles, CA 90017, USA
Presse Med 40:e219-35. 2011..Muscle biopsy diagnostic criteria are also described and illustrated... - Endoplasmic reticulum stress and unfolded protein response in inclusion body myositis muscleGaetano Vattemi
Department of Neurology, University of Southern California Neuromuscular Center, University of Southern California Keck School of Medicine, Good Samaritan Hospital, Los Angeles, California 90017-1912, USA
Am J Pathol 164:1-7. 2004.... - In AbetaPP-overexpressing cultured human muscle fibers proteasome inhibition enhances phosphorylation of AbetaPP751 and GSK3beta activation: effects mitigated by lithium and apparently relevant to sporadic inclusion-body myositisChiara Terracciano
Department of Neurology, USC Neuromuscular Center, University of Southern California Keck, School of Medicine, Good Samaritan Hospital, Los Angeles, California 90017, USA
J Neurochem 112:389-96. 2010..2) In biopsied s-IBM muscle fibers, GSK3beta is significantly activated and AbetaPP is phosphorylated on Thr724. Accordingly, treatment with lithium, or other GSK3beta inhibitors, might benefit s-IBM patients... - Novel demonstration of conformationally modified tau in sporadic inclusion-body myositis muscle fibersAnna Nogalska
USC Neuromuscular Center, Department of Neurology, University of Southern California Keck School of Medicine, Good Samaritan Hospital, 637 S Lucas Ave, Los Angeles, CA 90017 1912, USA
Neurosci Lett 503:229-33. 2011..This first demonstration of conformational tau in s-IBM, because of its abundance in non-atrophic muscle fibers, suggests that it might play an early role in s-IBM PHFs formation and thus be pathogenically important... - AbetaPP-overexpression and proteasome inhibition increase alphaB-crystallin in cultured human muscle: relevance to inclusion-body myositisSlawomir Wojcik
USC Neuromuscular Center, Department of Neurology, University of Southern California Keck School of Medicine, Good Samaritan Hospital, Los Angeles, CA 90017 1912, USA
Neuromuscul Disord 16:839-44. 2006..We propose that increased AbetaPP is a stressor increasing alphaBC expression in s-IBM muscle fibers. Determining the consequences of alphaBC association with Abeta oligomers could have clinical therapeutic relevance... - Cystatin C colocalizes with amyloid-beta and coimmunoprecipitates with amyloid-beta precursor protein in sporadic inclusion-body myositis musclesGaetano Vattemi
USC Neuromuscular Center, Department of Neurology, University of Southern California Keck School of Medicine, Good Samaritan Hospital, Los Angeles, California 90017 1912, USA
J Neurochem 85:1539-46. 2003..Our studies (i) demonstrate for the first time that CC physically associates with A beta PP, and (ii) suggest that CC may play a novel role in the s-IBM pathogenesis, possibly by influencing A beta PP processing and A beta deposition... - Molecular pathology and pathogenesis of inclusion-body myositisValerie Askanas
USC Neuromuscular Center, Department of Neurology, University of Southern California Keck School of Medicine, Good Samaritan Hospital, Los Angeles, California 90017 1912, USA
Microsc Res Tech 67:114-20. 2005..Our basic hypothesis is that overexpression of AbetaPP within the aging muscle fibers is an early upstream event causing a subsequent pathogenic cascade... - Proteasome inhibition and aggresome formation in sporadic inclusion-body myositis and in amyloid-beta precursor protein-overexpressing cultured human muscle fibersPietro Fratta
Department of Neurology, USC Neuromuscular Center, Good Samaritan Hospital, Los Angeles, CA 90017-1912, USA
Am J Pathol 167:517-26. 2005..Accordingly, proteasome dysfunction in s-IBM muscle fibers may play a role in accumulation of misfolded, potentially cytotoxic proteins and may be induced by increased intracellular AbetaPP/Abeta... - Impaired autophagy in sporadic inclusion-body myositis and in endoplasmic reticulum stress-provoked cultured human muscle fibersAnna Nogalska
USC Neuromuscular Center, Department of Neurology, University of Southern California Keck School of Medicine, Good Samaritan Hospital, Los Angeles, CA 90017 1912, USA
Am J Pathol 177:1377-87. 2010..Thus, unblocking protein degradation in s-IBM muscle fibers may be a desirable therapeutic strategy... - BACE1 and BACE2 in pathologic and normal human muscleGaetano Vattemi
USC Neuromuscular Center, Department of Neurology, University of Southern California Keck School of Medicine, Good Samaritan Hospital, Los Angeles 90017 1912, USA
Exp Neurol 179:150-8. 2003..Accordingly, BACE1 and BACE2 participate in normal and abnormal processes of human muscle, suggesting that their functions are broader than previously thought... - Increased BACE1 mRNA and noncoding BACE1-antisense transcript in sporadic inclusion-body myositis muscle fibers--possibly caused by endoplasmic reticulum stressAnna Nogalska
USC Neuromuscular Center, Department of Neurology, University of Southern California Keck School of Medicine, Good Samaritan Hospital, Los Angeles, CA, USA
Neurosci Lett 474:140-3. 2010..Accordingly, decreasing BACE1 through a targeted downregulation of its regulatory BACE1-AS, or reducing ER stress, might be therapeutic strategies in s-IBM, assuming that it would not impair any normal cellular functions of BACE1... - Abnormalities of NBR1, a novel autophagy-associated protein, in muscle fibers of sporadic inclusion-body myositisCarla D'Agostino
Department of Neurology, USC Neuromuscular Center, University of Southern California Keck School of Medicine, Good Samaritan Hospital, Los Angeles, 90017 1912, USA
Acta Neuropathol 122:627-36. 2011..Accordingly, attempts to unblock defective protein degradation might be a therapeutic strategy for s-IBM patients... - Decreased SIRT1 deacetylase activity in sporadic inclusion-body myositis muscle fibersAnna Nogalska
Department of Neurology, University of Southern California Keck School of Medicine, Good Samaritan Hospital, Los Angeles, CA 90017 1912, USA
Neurobiol Aging 31:1637-48. 2010..Improving SIRT1 action by treatment with known SIRT1 activators might benefit s-IBM patients... - Inclusion body myositis: a degenerative muscle disease associated with intra-muscle fiber multi-protein aggregates, proteasome inhibition, endoplasmic reticulum stress and decreased lysosomal degradationValerie Askanas
USC Neuromuscular Center, Department of Neurology, University of Southern California Keck School of Medicine, Good Samaritan Hospital, Los Angeles, CA 90017 1912, USA
Brain Pathol 19:493-506. 2009..Together, these appear to lead to the s-IBM-specific vacuolar degeneration, and muscle fiber atrophy, concluding with muscle fiber death... - In inclusion-body myositis muscle fibers Parkinson-associated DJ-1 is increased and oxidizedChiara Terracciano
Department of Neurology, USC Neuromuscular Center, University of Southern California Keck School of Medicine, Good Samaritan Hospital, 637 S Lucas Avenue, Los Angeles, CA 90017 1912, USA
Free Radic Biol Med 45:773-9. 2008..In s-IBM muscle fibers, DJ-1 could be protecting these fibers against oxidative stress, including protection of mitochondria... - Inclusion-body myositis: muscle-fiber molecular pathology and possible pathogenic significance of its similarity to Alzheimer's and Parkinson's disease brainsValerie Askanas
Department of Neurology, USC Neuromuscular Center, Good Samaritan Hospital, University of Southern California Keck School of Medicine, 637 South Lucas Avenue, Los Angeles, CA 90017 1912, USA
Acta Neuropathol 116:583-95. 2008..Similarities include, in the respective tissues, cellular aging, mitochondrial abnormalities, oxidative and endoplasmic-reticulum stresses, proteasome inhibition and multiprotein aggregates... - Mutant ubiquitin UBB+1 is accumulated in sporadic inclusion-body myositis muscle fibersP Fratta
USC Neuromuscular Center, Department of Neurology, University of Southern California Keck School of Medicine, Good Samaritan Hospital, Los Angeles, CA 90017 1912, USA
Neurology 63:1114-7. 2004..In s-IBM, UBB+1 may be pathogenic by inhibiting proteasome, thereby promoting accumulation of cytotoxic misfolded amyloid-beta and phosphorylated-tau... - Novel demonstration of amyloid-? oligomers in sporadic inclusion-body myositis muscle fibersAnna Nogalska
Department of Neurology, USC Neuromuscular Center, Good Samaritan Hospital, University of Southern California Keck School of Medicine, Los Angeles, CA 90017 1912, USA
Acta Neuropathol 120:661-6. 2010..This novel demonstration of A?42 oligomers in s-IBM muscle biopsy provides additional evidence that intra-muscle fiber accumulation of A?42 oligomers in s-IBM may contribute importantly to s-IBM pathogenic cascade... - Inclusion-body myositis, a multifactorial muscle disease associated with aging: current concepts of pathogenesisValerie Askanas
USC Neuromuscular Center, Department of Neurology, University of Southern California Keck School of Medicine, Good Samaritan Hospital, Los Angeles, California 90017 1912, USA
Curr Opin Rheumatol 19:550-9. 2007..About 100 papers related to the subject were published in 2006 and the first part of 2007 (we cite only articles most relevant to this review)... - Parkin and its association with alpha-synuclein and AbetaPP in inclusion-body myositis and AbetaPP-overexpressing cultured human muscle fibersO Paciello
USC Neuromuscular Center, Department of Neurology, University of Southern California Keck School of Medicine, Good Samaritan Hospital, Los Angeles 90017-1912, USA
Acta Myol 25:13-22. 2006..2. The small increase of parkin relative to the much larger increase of alpha-synuclein might be insufficient to secure complete ubiquitination and consequent degradation of alpha-syn. 3. AbetaPP might be a novel substrate of parkin... - Three lipoprotein receptors and cholesterol in inclusion-body myositis muscleM Jaworska-Wilczynska
USC Neuromuscular Center, Department of Neurology, University of Southern California Keck School of Medicine, Good Samaritan Hospital, 637 S. Lucas Ave, Los Angeles, CA 90017-1912, USA
Neurology 58:438-45. 2002..3) Increased LDLR and free cholesterol in some regenerating and necrotizing muscle fibers suggest a role for them in human muscle fiber growth and repair and necrotic death... - Association of active extracellular signal-regulated protein kinase with paired helical filaments of inclusion-body myositis muscle suggests its role in inclusion-body myositis tau phosphorylationG M Wilczynski
Department of Neurology, University of Southern California Keck School of Medicine, Good Samaritan Hospital, Los Angeles, CA 90017 1912, USA
Am J Pathol 156:1835-40. 2000..The ERK localized in nonjunctional regions of IBM fibers may underlie the known pathological up-regulation of junctional proteins there... - Inclusion-body myositis: newest concepts of pathogenesis and relation to aging and Alzheimer diseaseV Askanas
USC Neuromuscular Center, Department of Neurology, University of Southern California Keck School of Medicine, Good Samaritan Hospital, Los Angeles 90017-1912, USA
J Neuropathol Exp Neurol 60:1-14. 2001..The remarkable pathologic similarities between s-IBM muscle and Alzheimer disease (AD) brain are discussed, and the possible cause and significance are addressed... - Novel cytoplasmic immunolocalization of RNA polymerase II in inclusion-body myositis muscleG M Wilczynski
USC Neuromuscular Center, Department of Neurology, University of Southern California, Keck School of Medicine, Good Samaritan Hospital, 637 South Lucas Ave, Los Angeles, CA 90017-1912, USA
Neuroreport 12:1809-14. 2001.... - Paired helical filaments of inclusion-body myositis muscle contain RNA and survival motor neuron proteinA Broccolini
University of Southern California Neuromuscular Center, Los Angeles, California 90017 1712, USA
Am J Pathol 156:1151-5. 2000..This study demonstrates two novel components of the IBM paired helical filaments, which may lead to better understanding of their pathogenesis... - Unicorns, dragons, polymyositis, and other mythical beastsValerie Askanas
Neurology 63:403-4; author reply 404. 2004 - Expression of Nogo-A in human muscle fibers is not specific for amyotrophic lateral sclerosisValerie Askanas
Ann Neurol 62:676-7; author reply 677. 2007