Kallikrein
From Wikipedia, the free encyclopedia
Kallikreins (tissue and plasma kallikrein) are peptidases (enzymes that cleave peptide bonds in proteins), a subgroup of the serine protease family.
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[edit] Functions
They liberate kinins (BK and KD) from the kininogens.[1]
It also generates plasmin from plasminogen:
Prekallikrein is the precursor of plasma kallikrein. It can only activate kinins after being activated itself by factor XII or other stimuli.
[edit] Genes
There are 15 known kallikreins: KLK1, KLK2, KLK3, KLK4, KLK5, KLK6, KLK7, KLK8, KLK9, KLK10, KLK11, KLK12, KLK13, KLK14, KLK15
[edit] Clinical significance
Kallikreins are targets of active investigation by drug researchers as possible biomarkers for cancer.[2][3]
Prostate-specific antigen (PSA; hk3, human kallikrein gene 3) and human glandular kallikrein (hK2) are used as tumor markers for prostate cancer.
[edit] See also
[edit] References
- ^ Oikonomopoulou, K., Hansen, K.K., Saifeddine, M., Tea, I., Blaber, M., Blaber, S.I., Scarisbrick, I., Andrade-Gordon, P., Cottrell, G.S., Bunnett, N.W., Diamandis, E.P., and Hollenberg, M.D. "Proteinase-activated receptors, targets for kallikrein signaling" Journal of Biological Chemistry. 281: 32095-112, 2006.
- ^ Borgono, C.A., and Diamandis, E.P. "The emerging roles of human tissue kallikreins in cancer" Nature Reviews Cancer 4: 876-90, 2004.
- ^ Diamandis, E.P., and Yousef, G.M. "Human Tissue Kallikreins: A Family of New Cancer Biomarkers" Clinical Chemistry 48: 1198-1205, 2002.
[edit] External links
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