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Ultrastructure of myeloma cells in a case with crystalcryoglobulinemia
Author(s) -
Kalderon Albert E.,
Bogaars Hendrick A.,
Diamond Israel,
Cummings Fancis J.,
Kaplan Stephen R.,
Calabresi Paul
Publication year - 1977
Publication title -
cancer
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.052
H-Index - 304
eISSN - 1097-0142
pISSN - 0008-543X
DOI - 10.1002/1097-0142(197704)39:4<1475::aid-cncr2820390419>3.0.co;2-s
Subject(s) - cryoglobulin , endoplasmic reticulum , ultrastructure , cytoplasm , organelle , ribosome , intracellular , pathology , electron microscope , multiple myeloma , microbiology and biotechnology , medicine , biophysics , biology , biochemistry , immunology , cryoglobulinemia , hepatitis c virus , rna , virus , physics , gene , optics
The bone marrow of a patient with multiple myeloma of the IgG 2 Kappa type with spontaneously crystallizing cryoglobulin was studied by electron microscopy. The ultrastructure of the myeloma cells disclosed the presence of a crystalline material in the cytoplasm within the rough endoplasmic reticulum (RER) as well as in extracisternal sites. The crystalline material was also seen extracellulary with a distinctly unique subunit structure. The tubular units measured 200 ± 10 AÅ (SEM) externally with an internal diameter of 100 ± AÅ (SEM). The intracellular distribution did not indicate a characteristic organelle association usually observed in protein synthesizing cells. It is suggested, based on the present observations and the findings of others, that the crystalline material may represent polymerized protein synthesized by free ribosomes mostly in extracisternal locations, a pattern often seen in neoplastic plasma cells. Diffusion to extracisternal sites of precrystalline material through the membranes of the RER is a possible alternative mechanism.