Amyloid Filaments in Inclusion Body Myositis: Novel Findings Provide Insight Into Nature of Filaments

doi:10.1001/archneur.1991.00530240033013

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Vol. 48 No. 12, December 1991

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Amyloid Filaments in Inclusion Body Myositis

Novel Findings Provide Insight Into Nature of Filaments

Jerry R. Mendell, MD; Zarife Sahenk, MD; Tracy Gales, MS; Laura Paul

Arch Neurol. 1991;48(12):1229-1234.

Abstract

• Inclusion body myositis (IBM) represents a serious debilitatingdisease of muscle without identifiable cause or treatment. Musclebiopsy specimens have characteristic rimmed vacuoles, varyingdegrees of inflammation, and, most importantly, cytoplasmicand intranuclear filamentous inclusions of unknown composition.Fresh-frozen sections of muscle biopsy specimens from 24 IBMcases were stained with Congo red dye (pH, 10.5 to 11.0). Controlbiopsy specimens included polymyositis, dermatomyositis, hereditaryvacuolar myopathies of unknown cause, acid maltase deficiency,distal myopathy, oculopharyngeal dystrophy, and chloroquinemyopathy. Sections were also immunostained with antibody totransthyretin, human P component, and immunoglobulin light chains.In the vacuolated fibers in IBM, amyloidogenic green-birefringentdeposits were seen. Some deposits were delicate and wispy appearing,and others were plaque-like. The size of deposits varied, measuring1 x 2 to 8 µm, and rarely up to 20 µm in length.The number of amyloid-positive fibers correlated with the numberof vacuolated fibers. Similar deposits were seen in one caseof distal myopathy and one hereditary vacuolar myopathy. Othercontrol cases were negative for amyloid deposits. Antibody stainingfor known amyloidogenic proteins was negative. This study demonstratesthat the filaments in IBM share properties with amyloid proteins.The location implies that this amyloid material is formed intracellularly,rather than having a systemic derivation. The association ofamyloid deposits with autophagic vacuoles in IBM raises thelikely possibility that the filaments represent a modificationof a normal protein within an acidic degradative vacuolar compartment.An alternative possibility, considering the shared propertiesof IBM filaments and prions (which include size and amyloidogenicproperties), is that IBM represents a human prion disease. Furtherstudies will be required to resolve the nature of the amyloidogenicfilaments in IBM, but these findings may provide clues to thepathogenesis of this poorly understood disorder. In addition,the findings should facilitate the clinical diagnosis of IBM.

Author Affiliations

From the Division of Neuromuscular Disease, Department of Neurology, College of Medicine, The Ohio State University, Columbus.

Footnotes

Accepted for publication July 17, 1991.

Reprint requests to Room 463, Means Hall, The Ohio State University,1654 Upham Dr, Columbus, OH 43210 (Dr Mendell).

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