Black R A, Kronheim S R, Sleath P R
Department of Protein Chemistry, Immunex Corporation, Seattle, WA 98101.
FEBS Lett. 1989 Apr 24;247(2):386-90. doi: 10.1016/0014-5793(89)81376-6.
The proteolytic generation of mature interleukin-1 beta (IL-1 beta) from its inactive precursor does not proceed by a conventional pathway for hormonal processing. Pro-IL-1 beta is found dispersed in the cytoplasm, and there are no basic amino acid residues or other commonly recognized processing sites adjoining the mature N-terminus. Processing appears to occur during release of the hormone. In the present study, we have identified a specific protease that generates mature IL-1 beta from the precursor. This enzyme is co-induced with the hormone, and it differs in its cleavage specificity and inhibitor sensitivity from all known proteases.
成熟白细胞介素-1β(IL-1β)从其无活性前体的蛋白水解生成过程并非通过传统的激素加工途径进行。前白细胞介素-1β分散存在于细胞质中,且在成熟N端附近没有碱性氨基酸残基或其他常见的加工位点。加工过程似乎发生在激素释放期间。在本研究中,我们鉴定出一种从前体生成成熟IL-1β的特异性蛋白酶。这种酶与激素共同诱导产生,其切割特异性和抑制剂敏感性与所有已知蛋白酶不同。