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American Journal of Pathology, Vol 129, 536-542, Copyright © 1987 by American Society for Investigative Pathology

REGULAR ARTICLES

Primary amyloidosis A. Immunohistochemical and biochemical characterization

MM Picken, K Pelton, B Frangione and G Gallo
Department of Pathology, New York University Medical Center, New York 10016.

Primary "idiopathic" amyloidosis is usually related to immunoglobulin light chain (AL) associated with immunocytic dyscrasias, while secondary "reactive" amyloidosis (AA) is related to serum amyloid A protein (SAA) and typically occurs with chronic inflammation, malignancy, or familial Mediterranean fever. In the present study, amyloid fibril protein extracted from frozen and paraffin-embedded tissue from a patient (CAR) with primary systemic amyloidosis proved to be AA protein by immunohistochemical, immunochemical, and amino terminal sequence. Extracts from both frozen and formalin-fixed paraffin-embedded kidney and spleen yielded similar monomers and dimers of the AA protein. The additional high-molecular-weight bands and a distinct 12,000-dalton fragment in the amyloid protein extracted from the formalin-fixed paraffin-embedded lung suggest that different processing of proteins, ie, by polymerization and/or degradation, may occur in different organs.


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Copyright © 1987 by the American Society for Investigative Pathology.