Cathepsin K

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Cathepsin K
Ribbon diagram of cathepsin K, colored by secondary structure. From PDB 1TU6.
Available structures: 1atk, 1au0, 1au2, 1au3, 1au4, 1ayu, 1ayv, 1ayw, 1bgo, 1by8, 1mem, 1nl6, 1nlj, 1q6k, 1snk, 1tu6, 1u9v, 1u9w, 1u9x, 1vsn, 1yk7, 1yk8, 1yt7, 2ato, 2aux, 2auz, 2bdl, 2f7d, 2ftd, 7pck
Identifiers
Symbols CTSK; CTS02; CTSO; CTSO1; CTSO2; MGC23107; PKND; PYCD
External IDs OMIM: 601105 MGI: 107823 HomoloGene: 68053
RNA expression pattern

More reference expression data
Orthologs
Human Mouse
Entrez 1513 13038
Ensembl ENSG00000143387 ENSMUSG00000028111
Uniprot P43235 Q545T0
Refseq NM_000396 (mRNA)
NP_000387 (protein)		 NM_007802 (mRNA)
NP_031828 (protein)
Location Chr 1: 149.04 - 149.05 Mb Chr 3: 95.58 - 95.59 Mb
Pubmed search [1] [2]

Cathepsin K, also known as CTSK, is a human enzyme controlled by a gene.[1]

Cathepsin K is a protease, which is defined by its high specificity for kinins, is involved in bone resorption. The enzyme's ability to catabolize elastin, collagen, and gelatin allow it to break down bone and cartilage. This catabolic activity is also partially responsible for the loss of lung elasticity and recoil in emphysema. Cathepsin K inhibitors, such as odanacatib, show great potential in the treatment of osteoporosis.

Cathepsin K expression is stimulated by inflammatory cytokines that are released after tissue injury.

Contents

References

  1. ^ "Entrez Gene: CTSK cathepsin K".

Further reading

  • Motyckova G, Fisher DE (2003). "Pycnodysostosis: role and regulation of cathepsin K in osteoclast function and human disease.". Curr. Mol. Med. 2 (5): 407–21. PMID 12125807. 
  • Troen BR (2006). "The regulation of cathepsin K gene expression.". Ann. N. Y. Acad. Sci. 1068: 165–72. doi:10.1196/annals.1346.018. PMID 16831915. 
  • Del Nery E, Chagas JR, Juliano MA, et al. (1996). "Evaluation of the extent of the binding site in human tissue kallikrein by synthetic substrates with sequences of human kininogen fragments.". Biochem. J. 312 ( Pt 1): 233–8. PMID 7492318. 
  • Brömme D, Okamoto K (1995). "Human cathepsin O2, a novel cysteine protease highly expressed in osteoclastomas and ovary molecular cloning, sequencing and tissue distribution.". Biol. Chem. Hoppe-Seyler 376 (6): 379–84. PMID 7576232. 
  • Gelb BD, Edelson JG, Desnick RJ (1995). "Linkage of pycnodysostosis to chromosome 1q21 by homozygosity mapping.". Nat. Genet. 10 (2): 235–7. doi:10.1038/ng0695-235. PMID 7663521. 
  • Polymeropoulos MH, Ortiz De Luna RI, Ide SE, et al. (1995). "The gene for pycnodysostosis maps to human chromosome 1cen-q21.". Nat. Genet. 10 (2): 238–9. doi:10.1038/ng0695-238. PMID 7663522. 
  • Shi GP, Chapman HA, Bhairi SM, et al. (1995). "Molecular cloning of human cathepsin O, a novel endoproteinase and homologue of rabbit OC2.". FEBS Lett. 357 (2): 129–34. PMID 7805878. 
  • Inaoka T, Bilbe G, Ishibashi O, et al. (1995). "Molecular cloning of human cDNA for cathepsin K: novel cysteine proteinase predominantly expressed in bone.". Biochem. Biophys. Res. Commun. 206 (1): 89–96. doi:10.1006/bbrc.1995.1013. PMID 7818555. 
  • Velasco G, Ferrando AA, Puente XS, et al. (1994). "Human cathepsin O. Molecular cloning from a breast carcinoma, production of the active enzyme in Escherichia coli, and expression analysis in human tissues.". J. Biol. Chem. 269 (43): 27136–42. PMID 7929457. 
  • Li YP, Alexander M, Wucherpfennig AL, et al. (1996). "Cloning and complete coding sequence of a novel human cathepsin expressed in giant cells of osteoclastomas.". J. Bone Miner. Res. 10 (8): 1197–202. PMID 8585423. 
  • Bossard MJ, Tomaszek TA, Thompson SK, et al. (1996). "Proteolytic activity of human osteoclast cathepsin K. Expression, purification, activation, and substrate identification.". J. Biol. Chem. 271 (21): 12517–24. PMID 8647860. 
  • Gelb BD, Shi GP, Chapman HA, Desnick RJ (1996). "Pycnodysostosis, a lysosomal disease caused by cathepsin K deficiency.". Science 273 (5279): 1236–8. PMID 8703060. 
  • Johnson MR, Polymeropoulos MH, Vos HL, et al. (1997). "A nonsense mutation in the cathepsin K gene observed in a family with pycnodysostosis.". Genome Res. 6 (11): 1050–5. PMID 8938428. 
  • Littlewood-Evans A, Kokubo T, Ishibashi O, et al. (1997). "Localization of cathepsin K in human osteoclasts by in situ hybridization and immunohistochemistry.". Bone 20 (2): 81–6. PMID 9028530. 
  • McGrath ME, Klaus JL, Barnes MG, Brömme D (1997). "Crystal structure of human cathepsin K complexed with a potent inhibitor.". Nat. Struct. Biol. 4 (2): 105–9. PMID 9033587. 
  • Rood JA, Van Horn S, Drake FH, et al. (1997). "Genomic organization and chromosome localization of the human cathepsin K gene (CTSK).". Genomics 41 (2): 169–76. doi:10.1006/geno.1997.4614. PMID 9143491. 
  • Gelb BD, Shi GP, Heller M, et al. (1997). "Structure and chromosomal assignment of the human cathepsin K gene.". Genomics 41 (2): 258–62. doi:10.1006/geno.1997.4631. PMID 9143502. 
  • 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. PMID 9276160. 
  • Thompson SK, Halbert SM, Bossard MJ, et al. (1998). "Design of potent and selective human cathepsin K inhibitors that span the active site.". Proc. Natl. Acad. Sci. U.S.A. 94 (26): 14249–54. PMID 9405598. 
  • Gelb BD, Willner JP, Dunn TM, et al. (1998). "Paternal uniparental disomy for chromosome 1 revealed by molecular analysis of a patient with pycnodysostosis.". Am. J. Hum. Genet. 62 (4): 848–54. PMID 9529353. 

Additional images

Osteoclast

External links

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Hydrolase: proteases (EC 3.4)
Exopeptidase 3.4.11-19
Endopeptidase 3.4.21-24
Cathepsin 3.4.18,21,22,23
A - B - C - D - E - F - G - H - K - L1/L2 - S - W - Z

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