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Title: Signal transduction by the IL-2 receptor involves the activation of a tyrosine protein kinase

Miscellaneous ·
OSTI ID:6365750

Interleukin-2 (IL-2) interacts with specific high-affinity membrane receptors to induce proliferation and/or differentiation of T lymphocytes. The ability of IL-2 to activate a tyrosine protein kinase in vivo was assessed by using antibodies to phosphotyrosine in conjunction with immunoblots. Stimulation of IL-2-dependent helper and cytotoxic T cell lines and primary cultures of human T cells with the lymphokine resulted in an increase of tyrosine phosphorylation of several proteins with molecular weights ranging from 38,000 to 120,000. The tyrosine phosphorylation in the various proteins increased in a concentrations fashion and reached a maximum level within 15 minutes. The concentrations of IL-2 required for inducing these phosphorylations and for stimulating ({sup 3}H)thymidine uptake were similar, indicating that the increase in tyrosine phosphorylation correlated with the ability of IL-2 to stimulate proliferation. Neither protein kinase C activation nor increased levels of intracellular cAMP or calcium could reproduce or inhibit the IL-2-induced tyrosine phosphorylations.

Research Organization:
Rochester Univ., NY (USA)
OSTI ID:
6365750
Resource Relation:
Other Information: Thesis (Ph. D.)
Country of Publication:
United States
Language:
English

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