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Generation of human endothelin by cathepsin E
Author(s) -
Lees Wendy E.,
Kalinka Siân,
Meech John,
Capper Stephen J.,
Cook Neil D.,
Kay John
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)81060-2
Subject(s) - cathepsin e , endothelin receptor , cathepsin , cathepsin o , chemistry , cathepsin l1 , cathepsin a , cleavage (geology) , cathepsin d , cathepsin s , microbiology and biotechnology , biochemistry , biology , enzyme , paleontology , receptor , fracture (geology)
Highly‐purified cathepsin D processed human big endothelin 1–38 into endothelin‐like fragments but did not appear to generate endothelin 1–21 under the conditions employed. By contrast, human cathepsin E specifically cleaved human big endothelin into endothelin 1–21 and the C‐terminal fragment under identical conditions but did not degrade either product further.