Werle B, Ebert W, Klein W, Spiess E
Thoraxklinik Heidelberg-Rohrbach, Germany.
Anticancer Res. 1994 May-Jun;14(3A):1169-76.
Human lung tumors of different histologic cell types and adjacent normal lung parenchyma, purified lung parenchyma, purified lung macrophages and three human lung-derived cell lines were investigated in an attempt to identify tumor specific premature and mature cathepsin B species. By polyacrylamide gel electrophoresis and immunoblotting techniques with specific antibodies we detected mature cathepsin B forms with molecular masses of 31 kDa and 32 kDa in tissues. Reductive conditions revealed in these populations single and double chain 31/32 kDa forms. The latter were recognized by their heavy part, the 26/27 kDa molecule forms. Qualitative differences in the pattern of cathepsin B species between tumor and corresponding normal material or between different histologies of lung tumors were not found. However, tumor material is considerably richer in cathepsin B activity than normal material. Isolated alveolar macrophage populations and established cell lines showed the same cathepsin B pattern as tissues. All these cells released cathepsin B proforms of 44 to 46 kDa into the culture medium, indicating that the release of pro-cathepsin B cannot be considered a tumor-specific mechanism. The secreted proforms were sensitive to in vitro activation by pepsin.
研究了不同组织学细胞类型的人肺肿瘤及相邻正常肺实质、纯化的肺实质、纯化的肺巨噬细胞和三种人肺源性细胞系，以试图鉴定肿瘤特异性的组织蛋白酶B的早熟和成熟形式。通过聚丙烯酰胺凝胶电泳和使用特异性抗体的免疫印迹技术，我们在组织中检测到分子量为31 kDa和32 kDa的成熟组织蛋白酶B形式。还原条件下，在这些群体中显示出单链和双链31/32 kDa形式。后者通过其重链部分，即26/27 kDa分子形式被识别。未发现肿瘤与相应正常材料之间或肺肿瘤不同组织学之间组织蛋白酶B形式模式的定性差异。然而，肿瘤材料中的组织蛋白酶B活性比正常材料丰富得多。分离的肺泡巨噬细胞群体和已建立的细胞系显示出与组织相同的组织蛋白酶B模式。所有这些细胞将44至46 kDa的组织蛋白酶B前体形式释放到培养基中，表明组织蛋白酶B前体的释放不能被认为是一种肿瘤特异性机制。分泌的前体形式对胃蛋白酶的体外激活敏感。
