Abstract
Bone marrow cells from patients with light chain deposition disease (LCDD) or primary or myeloma amyloidosis were studied by immunofluorescence and biosynthesis experiments after incorporation of radioactive aminoacids. Monoclonal plasma cell populations were demonstrated even in patients without serum and urine monoclonal immunoglobulins and with a normal percentage of plasma cells. Structurally abnormal immunoglobulins were produced in several LCDD patients: abnormal light chains (by their short or large size, glycosylation and polymerization in vivo and in vitro) and abnormal (short) heavy chains. In other cases, light chains were normal sized and unglycosylated but they also showed a strong tendency to polymerize. The secretion of free light chains featured every amyloidosis case and the presence of light chain fragments almost all cases. Additional features in amyloidosis were synthesis of short γ chains (two cases), assembly block at the HL half molecule level of a monoclonal IgA (one case) and secretion of decameric enlarged k chains (one case). This is in contrast with non-myelomatous secondary amyloidosis where the distribution of bone marrow plasma cells was normal by immunofluorescence and where normal sized immunoglobulins were synthesised, without free light chain secretion and fragments.
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© 1988 Kluwer Academic Publishers, Dordrecht
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Preud’Homme, JL. (1988). Immunoglobulin synthesis in plasma cell dyscrasias with renal lesions. In: Minetti, L., D’Amico, G., Ponticelli, C. (eds) The Kidney in Plasma Cell Dyscrasias. Developments in Nephrology, vol 22. Springer, Dordrecht. https://doi.org/10.1007/978-94-009-1315-8_3
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DOI: https://doi.org/10.1007/978-94-009-1315-8_3
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