Appelhans B, Ender B, Sachse G, Nikiforov T, Appelhans H, Ebert W
Institut für Organische Chemie und Biochemie, Technische Hochschule, Darmstadt, FRG.
FEBS Lett. 1987 Nov 16;224(1):14-8. doi: 10.1016/0014-5793(87)80413-1.
Two human tumor cell lines were analyzed for the production of human antileucoprotease (ALP). One of them, a human squamous lung carcinoma cell line (HS-24) synthesized, as confirmed by Western blot analysis, high amounts of ALP in serum-free medium. The supernatant inhibited elastase, chymotrypsin and trypsin. Northern blot analysis with an 18-mer radiolabelled oligonucleotide, derived from an ALP specific cDNA clone, revealed a specific mRNA of about 700-800 nucleotides in HS-24 tumor cells. In contrast, a secondary human lung tumor cell line (SB-3), derived from the adrenal cortex, did not synthesize ALP when assayed under identical conditions. The supernatant inhibited only trypsin and chymotrypsin.
对两种人类肿瘤细胞系进行了人抗白细胞蛋白酶（ALP）产生情况的分析。其中之一，一种人肺鳞状癌细胞系（HS - 24），经蛋白质免疫印迹分析证实，在无血清培养基中能合成大量ALP。其培养上清液可抑制弹性蛋白酶、胰凝乳蛋白酶和胰蛋白酶。用一个源自ALP特异性cDNA克隆的18聚体放射性标记寡核苷酸进行Northern印迹分析，结果显示HS - 24肿瘤细胞中有一条约700 - 800个核苷酸的特异性mRNA。相比之下，另一种源自肾上腺皮质的人肺肿瘤细胞系（SB - 3），在相同条件下检测时不合成ALP。其培养上清液仅能抑制胰蛋白酶和胰凝乳蛋白酶。
