Ichimaru E, Tanoue M, Tani M, Tani Y, Kaneko T, Iwasaki Y, Kunimatsu K, Kato I
Department of Periodontology, Nagasaki University School of Dentistry, Japan.
Inflamm Res. 1996 Jun;45(6):277-82. doi: 10.1007/BF02280991.
Cathepsin B (EC 3.4.22.1), a typical lysosomal cysteine proteinase was identified immunologically with anti-human cathepsin B antibody in inflammatory exudate, gingival crevicular fluid (GCF) of adult periodontitis patients. The sensitive enzyme immunoassay (EIA) system initially developed, was rarely influenced by the presence of endogenous cysteine proteinase inhibitors, cystatin(s), indicating that it is possible to quantify the gross amount of cathepsin B including free enzyme forms and enzyme-inhibitor complex forms using this EIA system. The cathepsin B levels in GCF as determined by EIA and the activity measured with Z-Arg-Arg-MCA showed positive and significant correlation with various clinical parameters. Immunoblotting analysis revealed that the molecular form was a 29 kDa mature enzyme. More than 95% of Z-Arg-Arg-MCA hydrolytic activity in each GCF sample was inhibited by CA-074, specific inhibitor of cathepsin B. These results strongly suggested that the gross amount of cathepsin B in GCF as well as its activity level is closely associated with the severity of the disease and that cathepsins B play an important role in the pathogenesis of periodontitis.
组织蛋白酶B（EC 3.4.22.1），一种典型的溶酶体半胱氨酸蛋白酶，在成人牙周炎患者的炎性渗出物、龈沟液（GCF）中通过抗人组织蛋白酶B抗体进行免疫鉴定。最初开发的灵敏酶免疫测定（EIA）系统很少受到内源性半胱氨酸蛋白酶抑制剂胱抑素存在的影响，这表明使用该EIA系统可以对包括游离酶形式和酶-抑制剂复合物形式的组织蛋白酶B总量进行定量。通过EIA测定的GCF中组织蛋白酶B水平以及用Z-Arg-Arg-MCA测量的活性与各种临床参数呈正相关且具有显著相关性。免疫印迹分析表明分子形式为29 kDa的成熟酶。组织蛋白酶B的特异性抑制剂CA-074抑制了每个GCF样品中超过95%的Z-Arg-Arg-MCA水解活性。这些结果强烈表明GCF中组织蛋白酶B的总量及其活性水平与疾病的严重程度密切相关，并且组织蛋白酶B在牙周炎的发病机制中起重要作用。
