Transfer of a cloned immunoglobulin light-chain gene to mutant hybridoma cells restores specific antibody production.
The expression of immunoglobulin (Ig) genes is regulated at several levels. For example, although kappa-chain production requires a DNA rearrangement that juxtaposes variable and joining segments, this rearrangement is not sufficient for kappa-chain gene expression; that is, some cell types do not permit immunoglobulin production. The mechanisms responsible for the regulation of the expression of rearranged immunoglobulin genes are poorly understood. The technique of modifying cloned genes in vitro and transferring the modified genes to cells in culture provides a tool for identifying the structural features required for gene expression. To analyse immunoglobulin genes in this manner, however, it is first necessary to use, as recipients, cells that normally permit immunoglobulin production. We report here that a cloned kappa-chain gene is expressed in immunoglobulin-producing hybridoma cells. Furthermore, the product of the transferred kappa-chain gene is capable of restoring specific antibody production to the transformed cells.
D000818:Animals; D000918:Antibody Specificity; D003001:Cloning, Molecular; D005786:Gene Expression Regulation; D006825:Hybridomas / Q000276:immunology; D007147:Immunoglobulin Light Chains / Q000235:genetics*; D007075:Immunoglobulin M / Q000235:genetics; D007145:Immunoglobulin kappa-Chains / Q000235:genetics; D051379:Mice; D009194:Myeloma Proteins / Q000235:genetics*; D009578:Nitrobenzenes / Q000276:immunology; D009876:Operon
D007147:Immunoglobulin Light Chains; D007075:Immunoglobulin M; D007145:Immunoglobulin kappa-Chains; D009194:Myeloma Proteins; D009578:Nitrobenzenes