Casein-Induced Murine Amyloidosis: Amyloid and Immunoglobulin Production and Proliferative Capacity of Splenocytes

Abstract

A study of the chemical composition and immunological reactivity of amyloid fibrils in human amyloidosis has revealed 2 classes of amyloid (1, 2). The amyloid derived from primary amyloidosis and multiple myeloma consists of immunoglobulin (Ig) light (L) chains or the variable region fragments of L chains. The amyloid obtained from secondary amyloidosis consists of a non-Ig protein. Soluble circulating components which cross-react with amyloid may represent precursors of the tissue deposits (3, 4). These observations suggest possibilities as to the pathogenesis of amyloid formation. The present studies seek to determine how murine amyloidosis can serve to elucidate the pathogenesis of human amyloidosis. Attention will focus on lymphocytes and reticuloendothelial cells since they are the probable producers of amyloid.