The specificity of the early immune response. I. A comparison of the specificity of delayed hypersensitivity and humoral responses following immunization with human gammaG globulin.
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Biomedical subjects
Publications and source records attributed to C S Henney.
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Two distinct but distantly related complementary DNAs encoding proteins sharing human interleukin-1 (IL-1) activity (termed IL-1 alpha and IL-1 beta), were isolated from a macrophage cDNA library. The primary translation products of the genes are 271 and 269 amino acids long, although expression in Escherichia coli of the carboxy-terminal 159 and 153 amino acids produces IL-1 biological activity.
Interleukin-1 (IL-1) is a factor that can induce proliferation of murine T lymphocytes and can elicit a variety of other biological responses. These include bone resorption, fibroblast proliferation, acute phase protein release from hepatocytes, cartilage breakdown and fever. This spectrum of activities is consistent with a role for IL-1 as a mediator of inflammation. Recently, sequence data have shown that there are at least two members of the IL-1 family; these distantly related proteins have been termed IL-1 alpha and IL-1 beta. We have found previously that both murine T cells and fibroblasts possess a relative molecular mass (Mr) approximately 80,000 (80K) plasma membrane receptor for human IL-1 beta. We show here that the receptor for IL-1 alpha on both murine and human cells is identical to that for IL-1 beta. This result raises the issue of what separation, if any, there might be between the biological activities of IL-1 alpha and IL-1 beta.
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