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Immunoglobulin synthesis in primary and myeloma amyloidosis.
Clin Exp Immunol. 1988 Sep; 73(3):389-94.CE

Abstract

Bone marrow cells from 14 patients with primary amyloidosis and two patients with myeloma amyloidosis were studied by immunofluorescence and biosynthesis experiments after incorporation of radioactive amino acids. Cells from four patients affected with non-myeloma secondary amyloidosis were also studied as controls. In primary amyloidosis, monoclonal plasma cell populations were demonstrated by immunofluorescence in virtually every case, even in patients without serum and urine monoclonal immunoglobulin and with a normal percentage of bone marrow plasma cells. Biosynthesis experiments showed the secretion of large amounts of free light chains, most often of the lambda type, in every primary or myeloma amyloidosis case and the presence of light chain fragments in almost all cases. Special features in certain patients were the synthesis of short gamma chains (two cases), assembly block at the HL half molecule level of a monoclonal IgA (one case) and secretion of decameric abnormally large kappa 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 synthesized, without free light chain secretion and fragments. These data confirm that primary amyloidosis belongs to plasma cell dyscrasias and emphasize the role of free light chains and light chain fragments in the pathogenesis of amyloid deposition.

Authors+Show Affiliations

Laboratory of Immunology and Immunopathology, Poitiers University Hospital, Paris, France.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

3145161

Citation

Preud'homme, J L., et al. "Immunoglobulin Synthesis in Primary and Myeloma Amyloidosis." Clinical and Experimental Immunology, vol. 73, no. 3, 1988, pp. 389-94.
Preud'homme JL, Ganeval D, Grünfeld JP, et al. Immunoglobulin synthesis in primary and myeloma amyloidosis. Clin Exp Immunol. 1988;73(3):389-94.
Preud'homme, J. L., Ganeval, D., Grünfeld, J. P., Striker, L., & Brouet, J. C. (1988). Immunoglobulin synthesis in primary and myeloma amyloidosis. Clinical and Experimental Immunology, 73(3), 389-94.
Preud'homme JL, et al. Immunoglobulin Synthesis in Primary and Myeloma Amyloidosis. Clin Exp Immunol. 1988;73(3):389-94. PubMed PMID: 3145161.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Immunoglobulin synthesis in primary and myeloma amyloidosis. AU - Preud'homme,J L, AU - Ganeval,D, AU - Grünfeld,J P, AU - Striker,L, AU - Brouet,J C, PY - 1988/9/1/pubmed PY - 1988/9/1/medline PY - 1988/9/1/entrez SP - 389 EP - 94 JF - Clinical and experimental immunology JO - Clin. Exp. Immunol. VL - 73 IS - 3 N2 - Bone marrow cells from 14 patients with primary amyloidosis and two patients with myeloma amyloidosis were studied by immunofluorescence and biosynthesis experiments after incorporation of radioactive amino acids. Cells from four patients affected with non-myeloma secondary amyloidosis were also studied as controls. In primary amyloidosis, monoclonal plasma cell populations were demonstrated by immunofluorescence in virtually every case, even in patients without serum and urine monoclonal immunoglobulin and with a normal percentage of bone marrow plasma cells. Biosynthesis experiments showed the secretion of large amounts of free light chains, most often of the lambda type, in every primary or myeloma amyloidosis case and the presence of light chain fragments in almost all cases. Special features in certain patients were the synthesis of short gamma chains (two cases), assembly block at the HL half molecule level of a monoclonal IgA (one case) and secretion of decameric abnormally large kappa 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 synthesized, without free light chain secretion and fragments. These data confirm that primary amyloidosis belongs to plasma cell dyscrasias and emphasize the role of free light chains and light chain fragments in the pathogenesis of amyloid deposition. SN - 0009-9104 UR - https://www.unboundmedicine.com/medline/citation/3145161/Immunoglobulin_synthesis_in_primary_and_myeloma_amyloidosis_ L2 - https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/3145161/ DB - PRIME DP - Unbound Medicine ER -