Kallikreins are a subgroup of serine proteases having diverse physiological functions. Growing evidence suggests that many kallikreins are implicated in carcinogenesis and some have potential as novel cancer and other disease biomarkers. This gene is one of the fifteen kallikrein subfamily members located in a cluster on chromosome 19. This protein is functionally conserved in its capacity to release the vasoactive peptide, Lys-bradykinin, from low molecular weight kininogen.[4]
References
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↑Lundwall A, Band V, Blaber M, Clements JA, Courty Y, Diamandis EP, Fritz H, Lilja H, Malm J, Maltais LJ, Olsson AY, Petraki C, Scorilas A, Sotiropoulou G, Stenman UH, Stephan C, Talieri M, Yousef GM (Jun 2006). "A comprehensive nomenclature for serine proteases with homology to tissue kallikreins". Biol Chem. 387 (6): 637–41. doi:10.1515/BC.2006.082. PMID16800724.
↑Diamandis, Eleftherios P.; Deperthes, David; Lundwall, Åke (Jun 2006). "Proceedings of the 1st International Symposium on Kallikreins, Lausanne, Switzerland, September 1-3 , 2005". Biol Chem. 387 (6): 635–824. doi:10.1515/BC.2006.081. PMID16800723.
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Fukushima D, Kitamura N, Nakanishi S (1986). "Nucleotide sequence of cloned cDNA for human pancreatic kallikrein". Biochemistry. 24 (27): 8037–43. doi:10.1021/bi00348a030. PMID3004571.
Kellermann J, Lottspeich F, Geiger R, Deutzmann R (1988). "Human urinary kallikrein--amino acid sequence and carbohydrate attachment sites". Protein Seq. Data Anal. 1 (3): 177–82. PMID3163150.
Takahashi S, Irie A, Katayama Y, et al. (1986). "N-terminal amino acid sequence of human urinary prokallikrein". J. Biochem. 99 (3): 989–92. PMID3635530.
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Lin FK, Lin CH, Chou CC, et al. (1993). "Molecular cloning and sequence analysis of the monkey and human tissue kallikrein genes". Biochim. Biophys. Acta. 1173 (3): 325–8. doi:10.1016/0167-4781(93)90131-v. PMID7916636.
Gomes RA, Juliano L, Chagas JR, Hial V (1997). "Characterization of kininogenase activity of an acidic proteinase isolated from human kidney". Can. J. Physiol. Pharmacol. 75 (6): 757–61. doi:10.1139/cjpp-75-6-757. PMID9276160.
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Chen VC, Chao L, Chao J (2000). "Reactive-site specificity of human kallistatin toward tissue kallikrein probed by site-directed mutagenesis". Biochim. Biophys. Acta. 1479 (1–2): 237–46. doi:10.1016/S0167-4838(00)00044-3. PMID10862973.
External links
The MEROPS online database for peptidases and their inhibitors: S01.160