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Kallikrein

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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:

Fibrinolysis (simplified). Blue arrows denote stimulation, and red arrows inhibition.

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

  1. ^ Bhoola, K.D., Figueroa, C.D., Worthy, K. "Bioregulation of kinins: kallikreins, kininogens, and kininases" Pharmacological Reviews 44: 1-80, 1992.
  2. ^ Borgono, C.A., and Diamandis, E.P. "The emerging roles of human tissue kallikreins in cancer" Nature Reviews Cancer 4: 876-90, 2004.
  3. ^ Diamandis, E.P., and Yousef, G.M. "Human Tissue Kallikreins: A Family of New Cancer Biomarkers" Clinical Chemistry 48: 1198-1205, 2002.

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