Secretion of antileucoprotease from a human lung tumor cell line

FEBS Letters

Appelhans, H.²  Sachse, G.²  Nikiforov, T.²  Appelhans, B.²  Ender, B.²  Ebert, W.¹ 

[1] Thoraxklinikum, Amalienstr. 5, 6900 Heidelberg-Rohrbach, FRG;Institut für Organische Chemie und Biochemie, Petersenstr. 22, Technische Hochschule, 6100 Darmstadt FRG

关键词: Secretion;    Serine protease inhibitor;    Antileucoprotease;    (Lung tumor cell);    TCM;    tumor-conditioned medium;    ALP;    antileucoprotease;    PBS;    phosphate-buffered saline;    HPSTI;    human pancreatic secretory trypsin inhibitor;    SSC;    sodium chloride;    sodium citrate;    synthetic substrates are abbreviated according to the IUPAC-IUB rules for abbreviation of amino acids;    substituents;    ??? methoxy;    Suc;    3-carboxypropionyl;    Bz;    benzoyl;    pNa;    p-nitroanilide;   

DOI  :  10.1016/0014-5793(87)80413-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown