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Insulin Receptor Expression in the Burkitt Lymphoma Cells Daudi and Raji

Burnet Clinical Research Unit, Walter and Eliza Hall Institute of Medical Research, Royal Melbourne Hospital Parkville, 3050, Australia

Address requests for reprints to: Dr. J. D. Newman, Burnet Clinical Research Unit, Walter and Eliza Hall Institute of Medical Research, Royal Melbourne Hospital, Parkville, Victoria 3050, Australia.

Abstract

The specific binding of insulin to either intact or Triton-solubilized Daudi cells (a Burkitt lymphoma cell line) was reduced by over 95% compared to that to control IM-9 lymphocytes due to a decrease in receptor number without a change in affinity. Analysis by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and autoradiography revealed that ¹²⁵I-labeled Daudi cells had reduced amounts (1/20th) of immunoprecipitable binding () subunit [mol wt (M_r), 130,000] of the receptor and a relatively abundant 210,000 M_r form not seen in IM-9 cells. The transmembranous (β) subunit (M_r, 90,000) of the receptor, although not detected by ¹²⁵I surface labeling, could be phosphorylated and, together with the 210,000 M_r form, exhibited the same 2-fold stimulation of phosphorylation by insulin as that in IM-9 cells. Northern blot hybridization revealed a decrease in Daudi cells of all four major species of insulin receptor mRNA. The Raji cell, another Burkitt lymphoma cell line, also exhibited reduced protein and genetic expression of the insulin receptor, indicating that reduced insulin receptor expression may be representative of other Burkitt lymphoma cell lines.

Received for publication January 5, 1988. Revision received July 25, 1988. Accepted for publication August 11, 1988.