Plasma kallikrein possesses a unique protein structure
with four apple domains and a trypsin domain, which evolved
before coagulation factor XI. Tissue kallikreins are trypsinbased enzymes, and some members are highly correlated with
prostate cancer. The evidence that human urine induces hypotension
when injected intravenously into anesthetized dogs was
first described in 1909. Two major kallikreins, plasma kallikrein (KLKB1) and tissue (glandular) kallikrein (KLK),
were found in mammals, and they were transcribed by
different genes. Glandular KLK was an old name and
was replaced by tissue KLK in the modern nomenclature.
Verwenden
Kallikrein from porcine pancreas has been used:
as a matrix metalloproteinase-9 (MMP-9) zymogen activator
as a component of cell culture to test its effect on rat subventricular zone (SVZ) cells and oligodendrocyte progenitor cells (OPC) proliferation and survival
as a model enzyme to track kinetic data and visual detection limits of hydrolysis by hydrolytic enzymes in the two-phases array
Allgemeine Beschreibung
Kallikrein exists as an inactive prokallikrein in the porcine pancreas. The porcine kallikrein gene region is localized on chromosome 6q12-q21.
Biochem/physiol Actions
Kallikrein active forms are generated by the enzymatic action of trypsin. It is a serine protease that mediates the activation of growth factors and substrates.
Clinical Use
Kallikreins are drug targets for the control of hypertension, inflammation, and blood coagulation diseases. They
are also possible biomarkers for cancer. KLK2 and KLK3 [prostate-specific antigen (PSA)] are
used as the serum biomarker for prostate cancer.
Kallikrein Upstream-Materialien And Downstream Produkte
