Generation of human endothelin by cathepsin E.
Highly-purified cathepsin D processed human big endothelin1-38 into endothelin-like fragments but did not appear to generate endothelin1-21 under the conditions employed. By contrast, human cathepsin E specifically cleaved human big endothelin into endothelin1-21 and the C-terminal fragment under identical conditions but did not degrade either product further.
Lees
W E
WE
Department of Biochemistry, University of Wales College of Cardiff, UK.
Kalinka
S
S
Meech
J
J
Capper
S J
SJ
Cook
N D
ND
Kay
J
J
D000595:Amino Acid Sequence; D000818:Animals; D002402:Cathepsin D / Q000378:metabolism; D020059:Cathepsin E; D002403:Cathepsins / Q000378:metabolism*; D016232:Endothelins / Q000235:genetics*; D006801:Humans; D008969:Molecular Sequence Data; D011487:Protein Conformation; D011499:Protein Processing, Post-Translational; D051381:Rats; D013154:Spleen / Q000201:enzymology; D013379:Substrate Specificity
D016232:Endothelins; D002403:Cathepsins; D020059:Cathepsin E; D002402:Cathepsin D