Resistance of tropoelastin and elastin peptides to degradation by alpha 2-macroglobulin-protease complexes.
Resistance of tropoelastin and elastin peptides to degradation by alpha 2-macroglobulin-protease complexes.
复制标题
原弹性蛋白和弹性蛋白肽对 α2-巨球蛋白-蛋白酶复合物降解的抵抗力。
DOI：
10.1016/0003-9861(81)90439-2
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发表时间：
1981
影响因子：
3.9
通讯作者：
Rosenbloom,J
中科院分区：
文献类型：
--
作者：
Kueppers,F;Abrams,WR;Weinbaum,G;Rosenbloom,J
以前的研究表明，中性粒细胞弹性蛋白酶和α2-巨球蛋白的复合体可以降解原弹性蛋白，原弹性蛋白是不溶性弹性蛋白生物合成中的70,000道尔顿可溶性中间体。因此，这种复合体可能在肺气肿的发展中发挥重要作用。因此，通过凝胶过滤层析分离了人α-2-巨球蛋白与均一的人中性粒细胞弹性蛋白酶、猪胰腺弹性蛋白酶或牛胰蛋白酶的复合物，并测试了它们降解原弹性蛋白的能力。虽然原弹性蛋白被游离酶迅速降解，但不受络合物的影响。然而，分子量在8500或更小的多肽，由不溶性弹性蛋白的温和酸解制备，与复合体中的催化活性酶相互作用，而较大的多肽不相互作用。这些发现表明，α-2-巨球蛋白-弹性酶复合体本身并不在原弹性蛋白或不溶性弹性蛋白的初始降解中发挥作用。
Previous studies have suggested that the complex of neutrophil elastase andα2-macroglobulin can degrade tropoelastin, the 70,000-dalton soluble intermediate in the biosynthesis of insoluble elastin. Such complexes could, therefore, play an important role in the development of emphysema. Therefore, complexes of humanα2-macroglobulin with homogeneous human neutrophil elastase, porcine pancreatic elastase, or bovine trypsin were isolated by gel filtration chromatography and tested for their ability to degrade tropoelastin. While tropoelastin was rapidly degraded by the free enzymes, it was not affected by the complexes. However, peptides of molecular weight 8500 or less, prepared by mild acid hydrolysis of insoluble elastin, interacted with the catalytically active enzyme in the complex, while larger peptides did not. These findings suggest thatα2-macroglobulin-elastase complexes do not, themselves, play a role in the initial degradation of either tropoelastin or insoluble elastin.