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Kallikrein-related peptidase 5
Human Kallikrein 5 in complex with leupeptin. Rendered from PDb 2PSX.
Available structures
PDB Ortholog search: PDBe, RCSB
Symbols KLK5 ; KLK-L2; KLKL2; SCTE
External IDs OMIM605643 MGI1915918 HomoloGene75000 ChEMBL: 4447 GeneCards: KLK5 Gene
RNA expression pattern
PBB GE KLK5 222242 s at tn.png
More reference expression data
Species Human Mouse
Entrez 25818 68668
Ensembl ENSG00000167754 ENSMUSG00000074155
UniProt Q9Y337 Q9D140
RefSeq (mRNA) NM_001077491 NM_026806
RefSeq (protein) NP_001070959 NP_081082
Location (UCSC) Chr 19:
50.94 – 50.95 Mb
Chr 7:
43.84 – 43.85 Mb
PubMed search [1] [2]

Kallikrein-related peptidase 5 (KLK5), formerly known as stratum corneum tryptic enzyme (SCTE), is a serine protease expressed in the epidermis. In humans it is encoded by the KLK5 gene.[1][2][3][4][5][6][7] This gene is one of the fifteen kallikrein subfamily members located in a cluster on chromosome 19. Its expression is up-regulated by estrogens and progestins. Alternative splicing results in multiple transcript variants encoding the same protein.[7]

KLK5 has been suggested to regulate cell shedding (desquamation) in conjunction with KLK7 and KLK14, given its ability to degrade proteins which form the extracellular component of cell junctions in the stratum corneum. It is proposed that KLK5 regulates this process since it is able to self-activate in addition to activating KLK7 and KLK14.[8]


  1. ^ Brattsand M, Egelrud T (Nov 1999). "Purification, molecular cloning, and expression of a human stratum corneum trypsin-like serine protease with possible function in desquamation". J Biol Chem 274 (42): 30033–40. doi:10.1074/jbc.274.42.30033. PMID 10514489. 
  2. ^ Yousef GM, Diamandis EP (Feb 2000). "The new kallikrein-like gene, KLK-L2. Molecular characterization, mapping, tissue expression, and hormonal regulation". J Biol Chem 274 (53): 37511–6. doi:10.1074/jbc.274.53.37511. PMID 10608802. 
  3. ^ Zulkifli SN, Paine LL, Greener DL, Subramaniam R (Oct 1991). "Trends in selected obstetric complications from University Hospital, Kuala Lumpur, Malaysia". Int J Gynaecol Obstet 35 (1): 29–36. doi:10.1016/0020-7292(91)90059-E. PMID 1680072. 
  4. ^ Wiesmann UN, DiDonato S, Herschkowitz NN (Jan 1976). "Effect of chloroquine on cultured fibroblasts: release of lysosomal hydrolases and inhibition of their uptake". Biochem Biophys Res Commun 66 (4): 1338–43. doi:10.1016/0006-291X(75)90506-9. PMID 4. 
  5. ^ 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. PMID 16800723. 
  6. ^ Yamasaki K, Schauber J, Coda A, Lin H, Dorschner RA, Schechter NM, Bonnart C, Descargues P, Hovnanian A, Gallo RL (Oct 2006). "Kallikrein-mediated proteolysis regulates the antimicrobial effects of cathelicidins in skin". FASEB J 20 (12): 2068–80. doi:10.1096/fj.06-6075com. PMID 17012259. 
  7. ^ a b "Entrez Gene: KLK5 kallikrein-related peptidase 5". 
  8. ^ Brattsand M, Stefansson K, Lundh C, et al. (2005). "A proteolytic cascade of kallikreins in the stratum corneum". J. Invest. Dermatol. 124 (1): 198–203. doi:10.1111/j.0022-202X.2004.23547.x. PMID 15654974. 

Further reading[edit]

External links[edit]

  • The MEROPS online database for peptidases and their inhibitors: S01.017