Functional intersection of the kallikrein-related peptidases (KLKs) and thrombostasis axis.
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.
Department of Biomedical Sciences, Florida State University, Tallahassee, 32306-4300, USA. michael.blaber@med.fsu.edu <michael.blaber@med.fsu.edu>
Michael
M
Blaber
Hyesook
H
Yoon
Maria A
MA
Juliano
Isobel A
IA
Scarisbrick
Sachiko I
SI
Blaber
D043168:Angiostatins / Q000737:chemistry / Q000378:metabolism; D000818:Animals; D004789:Enzyme Activation; D006801:Humans; D007610:Kallikreins / Q000378:metabolism*; D011480:Protease Inhibitors / Q000378:metabolism; D044462:Receptors, Proteinase-Activated / Q000378:metabolism; D013927:Thrombosis / Q000378:metabolism*
D011480:Protease Inhibitors; D044462:Receptors, Proteinase-Activated; D043168:Angiostatins; D007610:Kallikreins