Control of immunoglobulin secretion in the murine plasmacytoma line MOPC 315.
Cells of the 315LV-1 (derived from NP1) variant line of MOPC 315 contain approximately 1% the normal intracellular level of the heavy (alpha) chain of IgA and no detectable light (lambda2) chain. The synthesis rate of alpha-chain in the variant, however, is similar to that in cells of the parent line. Moreover the relative amount of translatable alpha-chain mRNA that can be extracted from 315LV-1 cells is about the same as for parental cells. No light-chain synthesis can be detected either in vivo or in vitro in a wheat germ cell-free system. The 315LV-1 heavy chain synthesized in vivo or in vitro has slightly greater electrophoretic mobility than normal H chain and turns over rapidly intracellularly. The variant fails to secrete any of its heavy chain, despite the fact that its H chain mRNA is bound to membranes, as one would expect for a secretory protein message. Fusion of 315LV-1 cells with cells of a kappa-producing MPC 11 variant line leads to stabilization of the intracellular H chain and also to full recovery of secretion of the H chain as an H2L2 molecule.
D000818:Animals; D002460:Cell Line; D007143:Immunoglobulin Heavy Chains / Q000096:biosynthesis*; D007137:Immunoglobulin alpha-Chains / Q000096:biosynthesis*; D007146:Immunoglobulin lambda-Chains / Q000096:biosynthesis; D066298:In Vitro Techniques; D051379:Mice; D008807:Mice, Inbred BALB C; D010954:Plasmacytoma / Q000235:genetics / Q000276:immunology*; D012333:RNA, Messenger; D012334:RNA, Neoplasm
D007143:Immunoglobulin Heavy Chains; D007137:Immunoglobulin alpha-Chains; D007146:Immunoglobulin lambda-Chains; D012333:RNA, Messenger; D012334:RNA, Neoplasm