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Neurology 2003;61:257-260
© 2003 American Academy of Neurology
Brief Communications

Transthyretin Val122Ile, accumulated Aß, and inclusion-body myositis aspects in cultured muscle

Valerie Askanas, MD PhD, W. King Engel, MD, Janis McFerrin, BSc and Gaetano Vattemi, MD

From the USC Neuromuscular Center, Department of Neurology, University of Southern California Keck School of Medicine, Good Samaritan Hospital, Los Angeles.

Address correspondence and reprint requests to Dr. Valerie Askanas, USC Neuromuscular Center, Good Samaritan Hospital, 637 S. Lucas Ave., Los Angeles, CA 90017-1912; e-mail: askanas{at}hsc.usc.edu

Cultured muscle fibers (CMF) from a patient with inclusion-body myositis (IBM) and cardiac amyloidosis associated with the transthyretin (TTR) Val122Ile mutation contained aspects of the IBM phenotype: vacuolation, congophilic inclusions, and clusters of immunocolocalizing amyloid ß-peptide (Aß) and TTR accumulations. These abnormalities are never present in normal human CMF. These perturbations were greatly increased after Aß precursor protein gene transfer. The TTR mutation may be a genetic predisposition factor for the patient’s IBM.




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