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Clin Exp Immunol. 1992 Jan;87(1):122-6.

Primary structure of a monoclonal kappa chain in myeloma with light chain deposition disease.

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CNRS URA 1172, Laboratory of Molecular Immunology, Faculté des Sciences, University Hospital, Poitiers, France.


Previous data suggest that structural abnormalities of immunoglobulin light chains may be responsible for non-amyloid light chain deposition disease (LCDD). We report on the complete primary sequence deduced from complementary (c)DNA analysis of a normal-sized kappa chain in a case of myeloma-associated LCDD. The patient's urine contained a kappa type Bence-Jones protein made of monomers and dimers of an unglycosylated kappa chain. The bone marrow myeloma cells contained intracellular kappa and gamma chains by immunofluorescence. Biosynthesis experiments showed the production of normal-sized gamma chains and of kappa chains with the same apparent molecular mass (Mr) in SDS gels as the urinary kappa chain (26,000-27,000). These kappa chains were secreted as assembled IgG molecules and as a large excess of free monomers and dimers. The complete sequence of two identical cDNA clones derived from a normal-sized kappa messenger RNA indicated that this kappa chain belonged to the rare V kappa IV subgroup. The kappa mRNA had an overall normal structure made up of the V kappa IV sequence rearranged to J kappa 1 and followed by a normal constant exon of the Km(3) allotype. The variable region differed from the V kappa IV-J kappa 1 germline sequence by 17 amino acid substitutions. The peculiar sequence of the variable region of this kappa chain of a rare subgroup might relate to its tissue deposition.

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