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, Michael Blaber

Research output: Contribution to journalArticlepeer-review

43 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)373-377
Number of pages5
JournalBiological Chemistry
Issue number4
StatePublished - Apr 1 2009


  • Activation cascade
  • Activome
  • Kallikrein
  • Kallikrein-related peptidases (KLKs)
  • Protease

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Clinical Biochemistry


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