Insulin-degrading enzyme (IDE) encodes a zinc metallopeptidase that degrades intracellular insulin, thereby terminating insulin activity as well as participating in intercellular peptide signaling by degrading diverse peptides, such as glucagon, amylin, bradykinin, and
kallidin (19).
As an important element of the kallikrein/kinin system (KKS), tissue kallikrein can cleave low-molecule kininogen into kinins (e.g., bradykinin and
kallidin).
Kallikreins cleave "kininogens" to generate kinins, namely, bradykinin and
kallidin [18].
reported that neurokinin B, cholecystokinin, and chromogranin A were efficiently cleaved by APA, and
kallidin could also be cleaved by APA [16].
BK,
kallidin, and methionyl-lysyl-bradykinin are the members of the kinin family.
In particular, bradykinin and
kallidin are powerful algesic and vasoactive peptides generated locally following the proteolytic cleavage of their precursors, high- and low-molecular-weight cultures and in various regions of the brain including the medulla oblongata, the pons, the cerebral cortex and the hippocampus (Damasceno et al., 2015).