Cichy J, Potempa J, Chawla R K, Travis J
Department of Microbiology and Immunology, Jagiellonian University, Kraków, Poland.
J Clin Invest. 1995 Jun;95(6):2729-33. doi: 10.1172/JCI117975.
Although it is a well known fact that hepatocytes are the primary source of plasma proteinase inhibitors, including alpha 1-antichymotrypsin, this protein has also been detected in lung epithelial cells, which may suggest its local production. We have demonstrated that lung-derived epithelial cells are capable of synthesizing high levels of alpha 1-antichymotrypsin. In normal bronchial epithelial cells, as well as in the HTB55 human adenocarcinoma cell line, alpha 1-antichymotrypsin synthesis was under the control of inflammatory cytokines, of which oncostatin M was the most potent stimulator. This finding is consistent with a role for this inhibitor in protecting the lung epithelium from damage by chymotrypsin-like enzymes released from phagocytes such as neutrophils following pathogen invasion.
尽管肝细胞是血浆蛋白酶抑制剂(包括α1-抗糜蛋白酶)的主要来源,这是一个众所周知的事实,但这种蛋白质也在肺上皮细胞中被检测到,这可能表明它是在局部产生的。我们已经证明,肺源性上皮细胞能够合成高水平的α1-抗糜蛋白酶。在正常支气管上皮细胞以及HTB55人腺癌细胞系中,α1-抗糜蛋白酶的合成受炎性细胞因子的控制,其中制瘤素M是最有效的刺激因子。这一发现与该抑制剂在保护肺上皮细胞免受病原体入侵后从中性粒细胞等吞噬细胞释放的类糜蛋白酶样酶损伤方面的作用是一致的。