KLK5

Revision as of 18:52, 4 September 2012 by WikiBot (talk | contribs) (Robot: Automated text replacement (-{{WikiDoc Cardiology Network Infobox}} +, -<references /> +{{reflist|2}}, -{{reflist}} +{{reflist|2}}))
(diff) ← Older revision | Latest revision (diff) | Newer revision → (diff)
Jump to navigation Jump to search


Kallikrein-related peptidase 5
Identifiers
Symbols KLK5 ; KLK-L2; KLKL2; SCTE
External IDs Template:OMIM5 Template:MGI HomoloGene75000
RNA expression pattern
File:PBB GE KLK5 222242 s at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

Kallikrein-related peptidase 5, also known as KLK5, is a human gene.[1]

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. Its expression is up-regulated by estrogens and progestins. The encoded protein is secreted and may be involved in desquamation in the epidermis. Alternative splicing results in multiple transcript variants encoding the same protein.[1]

References

  1. 1.0 1.1 "Entrez Gene: KLK5 kallikrein-related peptidase 5".

Further reading

  • Diamandis EP, Yousef GM, Luo LY; et al. (2001). "The new human kallikrein gene family: implications in carcinogenesis". Trends Endocrinol. Metab. 11 (2): 54–60. PMID 10675891.
  • Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. PMID 8125298.
  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K; et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. PMID 9373149.
  • Brattsand M, Egelrud T (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. PMID 10514489.
  • Yousef GM, Diamandis EP (2000). "The new kallikrein-like gene, KLK-L2. Molecular characterization, mapping, tissue expression, and hormonal regulation". J. Biol. Chem. 274 (53): 37511–6. PMID 10608802.
  • Yousef GM, Luo LY, Diamandis EP (2000). "Identification of novel human kallikrein-like genes on chromosome 19q13.3-q13.4". Anticancer Res. 19 (4B): 2843–52. PMID 10652563.
  • Harvey TJ, Hooper JD, Myers SA; et al. (2001). "Tissue-specific expression patterns and fine mapping of the human kallikrein (KLK) locus on proximal 19q13.4". J. Biol. Chem. 275 (48): 37397–406. doi:10.1074/jbc.M004525200. PMID 10969073.
  • Gan L, Lee I, Smith R; et al. (2001). "Sequencing and expression analysis of the serine protease gene cluster located in chromosome 19q13 region". Gene. 257 (1): 119–30. PMID 11054574.
  • Kim H, Scorilas A, Katsaros D; et al. (2001). "Human kallikrein gene 5 (KLK5) expression is an indicator of poor prognosis in ovarian cancer". Br. J. Cancer. 84 (5): 643–50. doi:10.1054/bjoc.2000.1649. PMID 11237385.
  • Yousef GM, Scorilas A, Chang A; et al. (2002). "Down-regulation of the human kallikrein gene 5 (KLK5) in prostate cancer tissues". Prostate. 51 (2): 126–32. doi:10.1002/pros.10067. PMID 11948967.
  • Yousef GM, Obiezu CV, Jung K; et al. (2003). "Differential expression of Kallikrein gene 5 in cancerous and normal testicular tissues". Urology. 60 (4): 714–8. PMID 12385949.
  • Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
  • Dong Y, Kaushal A, Brattsand M; et al. (2004). "Differential splicing of KLK5 and KLK7 in epithelial ovarian cancer produces novel variants with potential as cancer biomarkers". Clin. Cancer Res. 9 (5): 1710–20. PMID 12738725.
  • Yousef GM, Kapadia C, Polymeris ME; et al. (2003). "The human kallikrein protein 5 (hK5) is enzymatically active, glycosylated and forms complexes with two protease inhibitors in ovarian cancer fluids". Biochim. Biophys. Acta. 1628 (2): 88–96. PMID 12890555.
  • Clark HF, Gurney AL, Abaya E; et al. (2003). "The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment". Genome Res. 13 (10): 2265–70. doi:10.1101/gr.1293003. PMID 12975309.
  • Caubet C, Jonca N, Brattsand M; et al. (2004). "Degradation of corneodesmosome proteins by two serine proteases of the kallikrein family, SCTE/KLK5/hK5 and SCCE/KLK7/hK7". J. Invest. Dermatol. 122 (5): 1235–44. doi:10.1111/j.0022-202X.2004.22512.x. PMID 15140227.
  • Gerhard DS, Wagner L, Feingold EA; et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.
  • 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.
  • Ishida-Yamamoto A, Deraison C, Bonnart C; et al. (2005). "LEKTI is localized in lamellar granules, separated from KLK5 and KLK7, and is secreted in the extracellular spaces of the superficial stratum granulosum". J. Invest. Dermatol. 124 (2): 360–6. doi:10.1111/j.0022-202X.2004.23583.x. PMID 15675955.

Template:WikiDoc Sources