A monoclonal V kappa l light chain responsible for XXXX .

@entity1 @entity8 @entity14104 @entity1522 @entity1582 @entity34004 @entity1391 @entity460 @entity4434
@entity460 and @entity1391 metabolism abnormalities are frequent in @entity1582 @entity1 and the role of @entity8 in such ionic perturbations may have been overlooked. The authors herein report the complete primary structure of a Bence Jones Vkappal light chain responsible for @entity8 with increased @entity14104 . Plasma and serum biochemical evaluations indicated a proximal tubular dysfunction mainly manifested as @entity34004 and @entity1391 loss. The study of a kidney biopsy showed @entity8 with numerous @entity1582 casts and peculiar features of the proximal tubular cells, which carried numerous phagolysosomal inclusions with occasional crystalline periodic striation. The nephrotoxic light chain primary structure was deduced from the bone marrow monoclonal plasma cells RNA. The kappal sequence was highly homologous to kappa chains previously characterized in @entity1 with @entity4434 . It was related to the Vkappal subgroup and was composed of a variable segment encoded by the O8/O18 germline gene rearranged to Jkappa4. The primary sequence presented unusual features restricted to the variable region, including substitutions of residues 28 and 31 in the complementary determining region 1 (CDR1) by @entity1522 of different charge. An unusual conformation of the kappal domain, likely resulting from somatic hypermutation, could alter the catabolism of the protein after its internalization and result in the tubular cell dysfunction. Comparison with @entity4434 studies suggests that Vkappal Bence Jones proteins may damage proximal tubular cells to an extent varying according to light chain (LC) sequence and structure, either leading to crystal formation and @entity4434 or inducing partial inhibition of proximal tubule function.
