胰岛素降解酶对松弛素家族肽的降解作用。
Degradation of relaxin family peptides by insulin-degrading enzyme.
作者信息
Bennett Robert G, Heimann Dean G, Hamel Frederick G
机构信息
VA Medical Center, Omaha, Nebraska 68105, USA.
出版信息
Ann N Y Acad Sci. 2009 Apr;1160:38-41. doi: 10.1111/j.1749-6632.2008.03782.x.
Insulin-degrading enzyme (IDE) is a ubiquitously expressed metalloproteinase responsible for the intracellular degradation of insulin. IDE also interacts with other members of the insulin superfamily, including relaxin, but no studies have been reported regarding the interaction of other relaxin-like peptides with IDE. In this study, we determined that relaxin, relaxin-3, and InsL3 all competitively inhibited the degradation of insulin by IDE to different degrees, and all inhibited covalent cross-linking of insulin to IDE. Each of the peptides was degraded by IDE to various degrees (insulin > relaxin > InsL3 = relaxin-3). In summary, relaxin, InsL3, and relaxin-3 all bound to IDE, competed for the binding and degradation of insulin, and were all substrates for the proteolytic activity of IDE. Therefore, it is possible that in addition to insulin, IDE may be important for the cellular proteolysis of relaxin, InsL3, and relaxin-3.
胰岛素降解酶（IDE）是一种广泛表达的金属蛋白酶，负责胰岛素的细胞内降解。IDE还与胰岛素超家族的其他成员相互作用，包括松弛素，但尚未有关于其他类松弛素肽与IDE相互作用的研究报道。在本研究中，我们确定松弛素、松弛素-3和胰岛素样肽3（InsL3）均不同程度地竞争性抑制IDE对胰岛素的降解，并且均抑制胰岛素与IDE的共价交联。每种肽均被IDE不同程度地降解（胰岛素>松弛素>InsL3 =松弛素-3）。总之，松弛素、InsL3和松弛素-3均与IDE结合，竞争胰岛素的结合和降解，并且都是IDE蛋白水解活性的底物。因此，除胰岛素外，IDE可能对松弛素、InsL3和松弛素-3的细胞内蛋白水解也很重要。
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