NR AAUW
AU Askanas,V.; Engel,W.K.
TI New advances in inclusion-body myositis
QU Current Opinion in Rheumatology 1993 Nov; 5(6): 732-41
PT journal article; review; review, tutorial
AB The major new advances in seeking the pathogenic mechanisms of sporadic inclusion-body myositis and hereditary inclusion-body myopathy are discussed. Hypotheses are presented regarding the possible causes and significance of amyloid deposits in sporadic inclusion-body myositis and the roles of abnormally accumulated ubiquitin, beta-amyloid protein, beta-amyloid precursor protein, alpha 1-antichymotrypsin, hyperphosphorylated tau, and prion protein in the vacuolated muscle fibers in both sporadic inclusion-body myositis and hereditary inclusion-body myopathy. Because hereditary inclusion-body myopathy is virtually free of Congophilic amyloid deposits but, like sporadic inclusion-body myositis, contains large accumulations of beta-amyloid protein, it is possible that the lesions in hereditary inclusion-body myopathy may represent "early" changes. There are striking similarities between the pathology of inclusion-body myositis muscle and brains affected by Alzheimer's disease in regard to accumulation of ubiquitin, beta-amyloid protein and its precursor protein, alpha 1-antichymotrypsin, and hyperphosphorylated tau.
ZR 61
MH Amyloid/analysis; Human; Inclusion Bodies/*chemistry; Male; Microscopy, Electron; Middle Age; Muscles/ultrastructure; Polymyositis/complications/genetics/*pathology; Support, Non-U.S. Gov't; Support, U.S. Gov't, P.H.S.; Ubiquitins/analysis; alpha 1-Antichymotrypsin/analysis
AD University of Southern California School of Medicine, Los Angeles.
SP englisch
PO USA