Molecular characterization of human and bovine endothelin converting enzyme (ECE‐1)

FEBS Letters

Schmidt, Martin¹  Otter, Rainer¹  Subkowski, Thomas¹  Kröger, Burkhard¹  Hillen, Heinz¹  Seulberger, Harald¹  Jacob, Elard¹  Meyer, Thomas¹  Schmalzing, Günther² 

[1] Department of Pharmaceutical Research, BASF Aktiengesellschaft, D-67056 Ludwigshafen, Germany;Max-Planck-Institute for Biophysics, D-60528 Frankfurt, Germany

关键词: Endothelin-1;    Endothelin converting enzyme;    ET-1;    endothelin-1;    big ET-1;    big endothelin-1;    ECE-1;    endothelin-1 converting enzyme;    RT-PCR;    reverse transcript PCR;    SDS-PAGE;    sodium dodecylsulphate polyacrylamide gelelectrophoresis;    DIFP;    diisopropyl fluorophosphate;    kDA;    kilo dalton;    kb;    kilo base(pair);    DIG;    digoxigenin;    CHO;    chinese hamster ovary;    RACE;    rapid amplification of CDNA ends;   

DOI  :  10.1016/0014-5793(94)01277-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A membrane-bound protease activity that specifically converts Big endothelin-1 has been purified from bovine endothelial cells (FBHE) The enzyme was cleaved with trypsin and the peptide sequencing analysis confirmed it to be a zinc chelating metalloprotease containing the typical HEXXH (HELTH) motif. RT-PCR and cDNA screens were employed to isolate the complete cDNAs of the bovine and human enzymes. This human metalloprotease was expressed heterologously in cell culture oocytes. The catalytic activity of the recombinant enzyme is the same as that determined for the natural enzyme. The data suggest that the characterized enzyme represents the functional human endothelin converting enzyme ECE-1.

【 授权许可】

Unknown