Functional intersection of the kallikrein-related peptidases (KLKs) and thrombostasis axis

Michael Blaber, Hyesook Yoon, Maria A. Juliano, Isobel A. Scarisbrick, Sachiko I. Blaber

Research output: Contribution to journalArticlepeer-review

18 Scopus citations


A large body of emerging evidence indicates a functional interaction between the kallikrein-related peptidases (KLKs) and proteases of the thrombostasis axis. These interactions appear relevant for both normal health as well as pathologies associated with inflammation, tissue injury, and remodeling. Regulatory interactions between the KLKs and thrombostasis proteases could impact several serious human diseases, including neurodegeneration and cancer. The emerging network of specific interactions between these two protease families appears to be complex, and much work remains to elucidate it. Complete understanding how this functional network resolves over time, given specific initial conditions, and how it might be controllably manipulated, will probably contribute to the emergence of novel diagnostics and therapeutic agents for major diseases.

Original languageEnglish (US)
Pages (from-to)311-320
Number of pages10
JournalBiological Chemistry
Issue number4
StatePublished - Apr 1 2010


  • Activation cascade
  • Kallikrein
  • Kallikrein-related peptidase (KLK)
  • Plasmin
  • Thrombogenesis
  • Thrombolysis
  • Thrombostasis

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Clinical Biochemistry


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