Startseite Lebenswissenschaften A completed KLK activome profile: investigation of activation profiles of KLK9, 10, and 15
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A completed KLK activome profile: investigation of activation profiles of KLK9, 10, and 15

  • Hyesook Yoon , Sachiko I. Blaber , Mekdes Debela , Peter Goettig , Isobel A. Scarisbrick und Michael Blaber
Veröffentlicht/Copyright: 17. Dezember 2008
Biological Chemistry
Aus der Zeitschrift Band 390 Heft 4

Abstract

We previously reported the activation profiles of the human kallikrein-related peptidases (KLKs) as determined from a KLK pro-peptide fusion-protein system. That report described the activity profiles of 12 of the 15 mature KLKs versus the 15 different pro-KLK sequences. The missing profiles in the prior report, involving KLK9, 10, and 15, are now described. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis, mass spectrometry, and N-terminal sequence analyses show that KLK9 and 10 exhibit low hydrolytic activities towards all of the 15 pro-KLK sequences, while KLK15 exhibits significant activity towards both Arg- and Lys-containing KLK pro-sequences. The ability of KLK15 to activate pro-KLK8, 12, and 14 is confirmed using recombinant pro-KLK proteins, and shown to be significant for activation of pro-KLK8 and 14, but not 12. These additional data for KLK9, 10, and 15 now permit a completed KLK activome profile, using a KLK pro-peptide fusion-protein system, to be described. The results suggest that KLK15, once activated, can potentially feed back into additional pro-KLK activation pathways. Conversely, KLK9 and 10, once activated, are unlikely to participate in further pro-KLK activation pathways, although similar to KLK1 they may activate other bioactive peptides.


Corresponding author

Received: 2008-10-28
Accepted: 2008-11-29
Published Online: 2008-12-17
Published in Print: 2009-04-01

©2009 by Walter de Gruyter Berlin New York

Heruntergeladen am 5.2.2026 von https://www.degruyterbrill.com/document/doi/10.1515/BC.2009.026/pdf
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