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Intracellular formation of amyloid fibrils in Myeloma. Cytochemical, immunochemical, and electron microscopic observations

✍ Scribed by Dr. Shigeo Nomura; Tadashi Kanoh; Haruto Uchino

Publisher: John Wiley and Sons
Year: 1984
Tongue: English
Weight: 721 KB
Volume: 54
Category: Article
ISSN: 0008-543X
DOI: 10.1002/1097-0142(19840715)54:2<303::aid-cncr2820540220>3.0.co;2-m

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✦ Synopsis

Needle-like, rod-shaped, and rhomboid intracytoplasmic crystalline inciusions were found in myeloma cells from the bone marrow of a patient with I@-K and Bence Jones-K type multiple myeloma. Cytochemical, immunochemical, and electron microscopic studies revealed that these inclusions consisted of at least three kinds of components: kappa light chain crystals, lysosomal enzymes, and amyloid fibrils. The coexistence of these three kinds of inclusions in one myeloma cell suggests an intracellular site for the formation of amyloid fibrils. From these observations, the authors postulated that the excessively produced light chains were transported to the Golgi apparatus where they were transformed into crystalline inclusions, and thereafter, digested by lysosomal enzymes to form amyloid fibrils. The demonstration of crystalline inclusions which reacted exclusively with antisera against free light chains indicates that the Bence Jones protein is a precursor of amyloid light chain.

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