Skubitz K M, Wehner N G, Gray B H
Department of Medicine, University of Minnesota Medical School, Minneapolis.
J Leukoc Biol. 1988 Sep;44(3):158-65. doi: 10.1002/jlb.44.3.158.
Neutrophil proteases are believed to play a role in the pathogenesis of a variety of human diseases. While many studies of proteases in models of disease have focused on elastase, neutrophils contain several proteases some of which share a high degree of homology. This report describes the production and characterization of an IgG1 murine monoclonal antibody (AHN-10) that reacts with human neutrophil elastase but not with the other major neutrophil neutral proteases: cathepsin G, proteinase 3, collagenase, or the newly purified neutral protease, esterase N. AHN-10 inhibited the elastinolytic activity of purified human neutrophil elastase and could detect elastase in alcohol-fixed cytospin preparations. The epitope recognized by AHN-10 was resistant to treatment with NaIO4, suggesting that the epitope is not a carbohydrate. AHN-10 should be useful for the immunolocalization of neutrophil elastase in tissue specimens and as a stable source of characterized antibody for quantitative identification of neutrophil elastase.
中性粒细胞蛋白酶被认为在多种人类疾病的发病机制中起作用。虽然在疾病模型中对蛋白酶的许多研究都集中在弹性蛋白酶上，但中性粒细胞含有几种蛋白酶，其中一些具有高度的同源性。本报告描述了一种IgG1小鼠单克隆抗体（AHN - 10）的产生和特性，该抗体与人中性粒细胞弹性蛋白酶反应，但不与其他主要的中性粒细胞中性蛋白酶反应，如组织蛋白酶G、蛋白酶3、胶原酶或新纯化的中性蛋白酶酯酶N。AHN - 10抑制纯化的人中性粒细胞弹性蛋白酶的弹性蛋白分解活性，并能在酒精固定的细胞涂片制剂中检测到弹性蛋白酶。AHN - 10识别的表位对高碘酸钠处理具有抗性，这表明该表位不是碳水化合物。AHN - 10可用于组织标本中中性粒细胞弹性蛋白酶的免疫定位，并作为用于定量鉴定中性粒细胞弹性蛋白酶的特性明确的抗体的稳定来源。
