Esposito A L, Clark C A, Poirier W J, Kephart P A
Department of Medicine, Boston University Medical Center, Massachusetts.
Exp Lung Res. 1988;14(6):743-56. doi: 10.3109/01902148809087841.
In order to assess the influence of the protease inhibitor eglin-c on superoxide anion (O-2) release by human polymorphonuclear leukocytes (PMN), cells were secured from normal donors and stimulated with phorbol myristate acetate (PMA), opsonized zymosan, or n-formyl-methionyl-leucyl-phenylalanine (FMLP). In the presence of 100 micrograms/ml eglin-c, the activation time was prolonged and the maximum linear rate of O-2 formation was depressed following stimulation with PMA; a concentration of 1000 micrograms/ml eglin-c was required to produce a similar effect with opsonized zymosan. Eglin-c did not influence the activation time following stimulation with FMLP, but at 2000 micrograms/ml, the protease inhibitor attenuated the rate of O-2 production in response to the chemotactic peptide. In the presence of cytochalasin B, the inhibitory effect of eglin-c on O-2 release following stimulation with FMLP became more pronounced. In spite of these alterations in O-2 formation, the protease inhibitor did not impair the bactericidal activity of PMN against Staphylococcus aureus. Therefore, we conclude that although eglin-c can disrupt the activation and the activity of the superoxide-generating system of human PMN, the effect is stimulus dependent and is not associated with an alteration in the microbicidal capacity of neutrophils against S. aureus.
为了评估蛋白酶抑制剂抑肽酶 - c对人多形核白细胞（PMN）释放超氧阴离子（O₂⁻）的影响，从正常供体获取细胞，并用佛波酯肉豆蔻酸酯乙酸酯（PMA）、调理酵母聚糖或N - 甲酰 - 甲硫氨酰 - 亮氨酰 - 苯丙氨酸（FMLP）进行刺激。在存在100微克/毫升抑肽酶 - c的情况下，用PMA刺激后，激活时间延长，O₂形成的最大线性速率降低；对于调理酵母聚糖，需要1000微克/毫升的抑肽酶 - c浓度才能产生类似效果。抑肽酶 - c不影响用FMLP刺激后的激活时间，但在2000微克/毫升时，该蛋白酶抑制剂可减弱对趋化肽的O₂产生速率。在细胞松弛素B存在的情况下，抑肽酶 - c对FMLP刺激后O₂释放的抑制作用变得更加明显。尽管O₂形成有这些变化，但该蛋白酶抑制剂并未损害PMN对金黄色葡萄球菌的杀菌活性。因此，我们得出结论，尽管抑肽酶 - c可以破坏人PMN超氧化物生成系统的激活和活性，但其作用是刺激依赖性的，并且与中性粒细胞对金黄色葡萄球菌的杀菌能力改变无关。
