Control of J Chain Biosynthesis in Relation to Heavy and Light Chain Synthesis, Polymerization and Secretion

Mouse myeloma tumors and some variants derived from them were labeled in vitro with tritiated leucine and the radioactive J chain was assayed in cell lysates by precipitation with an antiserum specific for mouse J chain. The major findings were: 1) J chain can be found in an IgG2b-secreting cells (M...

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Veröffentlicht in:The Journal of immunology (1950) 1975-04, Vol.114 (4), p.1218-1220
Hauptverfasser: Kaji, Hideko, Parkhouse, R. M. E
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container_title The Journal of immunology (1950)
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creator Kaji, Hideko
Parkhouse, R. M. E
description Mouse myeloma tumors and some variants derived from them were labeled in vitro with tritiated leucine and the radioactive J chain was assayed in cell lysates by precipitation with an antiserum specific for mouse J chain. The major findings were: 1) J chain can be found in an IgG2b-secreting cells (MPC-11). These data, together with previous findings suggest that cells secreting all classes of IgG synthesize J chain, even though there is no apparent requirement for J chain in assembly of the IgG molecule. Hence production of J chain does not depend upon secretion of a polymeric immunoglobulin. 2) Intracellular J chain can be found in myeloma variants that do not produce heavy chains showing that production of J chain may not coordinately be linked to the synthesis of heavy chain. 3) J chain was found in cells synthesizing, but not secreting, immunoglobulin. Thus production of J chain is not linked to secretion of immunoglobulin. 4) J chain could not be detected in plasma cells that do not produce immunoglobulins. It was also not found in mouse leukemic cells, suggesting that production of J chain is probably linked in some way to immunoglobulin production.
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M. E</creatorcontrib><title>Control of J Chain Biosynthesis in Relation to Heavy and Light Chain Synthesis, Polymerization and Secretion</title><title>The Journal of immunology (1950)</title><addtitle>J Immunol</addtitle><description>Mouse myeloma tumors and some variants derived from them were labeled in vitro with tritiated leucine and the radioactive J chain was assayed in cell lysates by precipitation with an antiserum specific for mouse J chain. The major findings were: 1) J chain can be found in an IgG2b-secreting cells (MPC-11). These data, together with previous findings suggest that cells secreting all classes of IgG synthesize J chain, even though there is no apparent requirement for J chain in assembly of the IgG molecule. Hence production of J chain does not depend upon secretion of a polymeric immunoglobulin. 2) Intracellular J chain can be found in myeloma variants that do not produce heavy chains showing that production of J chain may not coordinately be linked to the synthesis of heavy chain. 3) J chain was found in cells synthesizing, but not secreting, immunoglobulin. Thus production of J chain is not linked to secretion of immunoglobulin. 4) J chain could not be detected in plasma cells that do not produce immunoglobulins. 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subjects Animals
Antibody Formation
Cell Line
Cells, Cultured
Goats - immunology
Immune Sera
Immunoglobulin A - biosynthesis
Immunoglobulin Fragments - biosynthesis
Immunoglobulin G - biosynthesis
Immunoglobulin Heavy Chains - biosynthesis
Immunoglobulin J-Chains - biosynthesis
Immunoglobulin M
Leucine - metabolism
Leukemia, Experimental - immunology
Mice
Multiple Myeloma - immunology
Polymers
Precipitin Tests
Rabbits - immunology
Tritium
title Control of J Chain Biosynthesis in Relation to Heavy and Light Chain Synthesis, Polymerization and Secretion
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