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Amyloidoma of the CNS

II.Immunohistochemical and biochemical study

Department of Pathology (Drs. Vidal, Ghiso, Gallo, and Frangione), New York university Medical Center, New York, NY; and the Division of Neuropathology, Institute of Pathology (Drs. Cohen and Gambetti), Case Western Reserve University, Cleveland, OH.

We present the immunohistochemical and biochemical identification of an amyloidoma localized to the cerebral white matter in a patient who shows no evidence of systemic or extracranial localized amyloid deposits. Immunohistologic and immunochemical studies, using antibodies against biochemically different amyloid fibrils and amyloid-associated proteins, showed reactivity with antibodies only to lambda light chain and serum amyloid P-component. Amino acid sequence analysis of the purified amyloid fibrils extracted from the brain tumor indicates that the amyloid protein is an unusual immunoglobulin lambda light chain, starting at residue five of the variable domain. These fibrils consist of lambda chain fragments of different lengths (10 to 30 kd) very likely arising by polymerization of the amyloid subunit or sequential proteolytic cleavage of the light chain, or both. After exposure to denaturing agents, the 10-kd subunit retains the characteristics of native amyloid fibrils by electron microscopy.

Address correspondence and reprint requests to Dr. Blas Frangione, Department of Pathology, New York University Medical Center, 550 First Avenue, New York, NY 10016.

Supported by National Institutes of Health Grant #AR 02594 to B.F. and NIH NIA AG08992 and NIH NIA 7 R01 AGNS08155 to P.G.

Received January 8, 1992. Accepted for publication in final form March 26, 1992.

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