Myeloma cells, immunoglobulin synthesis

Salmon, S. E., and Smith, B. A., Immunoglobulin synthesis and total body tumor cell number in IgG multiple myeloma. J. Clin. Invest. 49, 1114-1121 (1970). 

A. Bargellesi, G. Damiani, W. M. Kuehl, M. D. Scharff, Synthesis of immunoglobulin by substrate attached mouse myeloma cells, /. Cell. Physiol. 1976, 88, 247-251. 

Sonenshein, G. E., and Brawerman, G., 1976a, Regulation of immunoglobulin synthesis in mouse myeloma cells. Biochemistry 15 5497. 

Conditions for optimal recoveries of poly(A) containing RNA, with minimal contamination from rRNA, were investigated. The poly(A) fractions isolated were effective as an RNA template for the synthesis of complementary DNA with the RNA-dependent DNA polymerase of avian myeloblastosis virus. Poly(dT)-cellulose has also been used both in the purification of a 14 S messenger RNA for the immunoglobulin light chain from microsomes of MOPC 41 mouse myeloma that appeared to code for a precursor protein [117], and in the purification of RNA-dependent DNA polymerase from RNA tumour virus [118]. An example of the use of oligo(dT)-cellulose is provided by the purification of a viral specific RNA from sarcoma virus-transformed nonproducer cells [119]. 

Bence Jones proteins are L chains (monomers or dimers k or X) synthesized by patients with multiple myeloma or, infrequently, with Waldenstrom s disease. The L chains are present in the serum and urine. They are often easy to isolate from urine because of their relatively high concentration and the absence of other immunoglobulins. About 10-15% of patients with multiple myeloma produce only a Bence Jones protein, and about 40% synthesize a myeloma protein without significant amounts of a Bence Jones protein. When both types of protein are present in an individual the Bence Jones protein is generally identical in structure to the L chain of the serum myeloma protein it therefore reflects the synthesis of excess L chains, as compared to H chains, by the malignant clone of cells. 

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