Human Pre-interleukin 1α and β : Structural Features Revealed by Limited Proteolysis

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Both pre-interleukin 1α and β (pre IL 1αand β) are proteolytically processed into extracellular mature forms of IL 1α and β. Since pre IL 1α and is shown to be biologically active, there may be other reasons for the proteolytic processing of IL 1α and presumably, for IL 1β also. In order to examine the possibility that structural stabilization may be associated with the proteolytic processing of pre IL 1α and β, we investigated the structural featuers of pre IL 1α and β by the combination of limited proteolysis and immunoprecipitation with antibodies to the NH_2-terminal halves or COOH-terminal halves of pre IL 1α or β. Both trypsin and V8 protease digested the NH_2-terminal halves of pre IL 1α and β more easily than the COOH-terminal halves of pre IL α and β, yielding structurally stabilized "mature" forms of IL 1. Both trypsin and V8 protease yielded a fragment similar in size to mature IL 1α from pre IL 1α. In contrast, trypsin digested pre IL 1β into fragments smaller in size tham mature IL 1β, while V8 protease yielded a fragment similar in size to mature IL 1β. Furthermore, mature IL 1β, once processed and released from cells, was resistant to trypsim. Since the COOH-terminal half of pre IL 1β is more susceptible to protease digestion than the extracellular mature form of IL 1β, which consists of the same COOH-half, the proteolytic processing of pre IL 1β appears to yield mature IL 1β with a more protease-resistant stable tertiary structure.
公益社団法人日本薬学会の論文
1991-06-25

Human Pre-interleukin 1α and β : Structural Features Revealed by Limited Proteolysis

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