Secretion of antileucoprotease from a human lung tumor cell line |
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Authors: | B Appelhans B Ender G Sachse T Nikiforov H Appelhans W Ebert |
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Affiliation: | Institut für Organische Chemie und Biochemie, Technische Hochschule, Darmstadt, FRG. |
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Abstract: | 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. |
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