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A contra-IL-2 cytokine derived from mice suppressed for collagen-induced arthritis
1Department of Medicine, Miriam Hospital, Providence, Rhode Island.
The present study identifies and characterizes a cytokine derived from a T cell hybridoma which inhibits interleukin-2 (IL-2) function. The T cell hybridoma, T101N, was derived from somatic cell hybridization of lymphoid cells from mice suppressed for collagen-induced arthritis. Serial dilution of T101N cell culture medium reveals a concentration-dependent inhibition of recombinant IL-2 induced proliferation. Physiochemical properties of the inhibitor indicate that the contra-IL-2 activity is optimally resolved at 37 degrees C and neutral pH. Analysis of the molecular characteristics of the contra-IL-2 activity indicate that the cytokine activity is most biologically active as a pentimeric molecule of high molecular weight. Apparent molecular weight of monomeric contra-IL-2 is approximately 30,000-35,000 Da.
The present study identifies and characterizes a cytokine derived from a T cell hybridoma which inhibits interleukin-2 (IL-2) function. The T cell hybridoma, T101N, was derived from somatic cell hybridization of lymphoid cells from mice suppressed for collagen-induced arthritis. Serial dilution of T101N cell culture medium reveals a concentration-dependent inhibition of recombinant IL-2 induced proliferation. Physiochemical properties of the inhibitor indicate that the contra-IL-2 activity is optimally resolved at 37 degrees C and neutral pH. Analysis of the molecular characteristics of the contra-IL-2 activity indicate that the cytokine activity is most biologically active as a pentimeric molecule of high molecular weight. Apparent molecular weight of monomeric contra-IL-2 is approximately 30,000-35,000 Da.