Banda M J, Clark E J, Werb Z
J Exp Med. 1980 Dec 1;152(6):1563-70. doi: 10.1084/jem.152.6.1563.
Inflammatory mouse peritoneal macrophages secrete a metalloproteinase that is not inhibited by alpha 1-proteinase inhibitor. This proteinase, macrophage elastase, recognizes alpha 1-proteinase inhibitor with macrophage elastase does not involve a stable proteinase-inhibitor complex and results in the proteolytic removal of a peptide of apparent molecular weight 4,000-5,000 from the inhibitor. After degradation by macrophage elastase, alpha 1-proteinase inhibitor is no longer able to inhibit human granulocyte elastase, a serine proteinase implicated in the pathogenesis of emphysema. Macrophage elastase apparently does not degrade human granulocyte elastase-alpha 1-proteinase inhibitor complexes or release active granulocyte elastase from these complexes. The ability of macrophage elastase to degrade alpha 1-proteinase inhibitor is inhibited by EDTA and alpha 2-macroglobulin.
炎性小鼠腹腔巨噬细胞分泌一种金属蛋白酶,该酶不受α1-蛋白酶抑制剂的抑制。这种蛋白酶即巨噬细胞弹性蛋白酶,它识别α1-蛋白酶抑制剂的方式并不涉及稳定的蛋白酶-抑制剂复合物,而是导致从该抑制剂上蛋白水解去除一个表观分子量为4000-5000的肽段。经巨噬细胞弹性蛋白酶降解后,α1-蛋白酶抑制剂不再能够抑制人粒细胞弹性蛋白酶,后者是一种与肺气肿发病机制有关的丝氨酸蛋白酶。巨噬细胞弹性蛋白酶显然不会降解人粒细胞弹性蛋白酶-α1-蛋白酶抑制剂复合物,也不会从这些复合物中释放出活性粒细胞弹性蛋白酶。EDTA和α2-巨球蛋白可抑制巨噬细胞弹性蛋白酶降解α1-蛋白酶抑制剂的能力。