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Gene Review

Ctsk  -  cathepsin K

Rattus norvegicus

Synonyms: Cathepsin K
 Zhao,  Väänänen,  Lark,  Stroup,  James,  Dodds,  Hwang,  Blake,  Lechowska,  Hoffman,  Smith,  Kapadia,  Liang,  Erhard,  Ru,  Dong,  Marquis,  Veber,  Gowen,  Dodds,  Nikawa,  Ikemoto,  Watanabe,  Kitano,  Kano,  Yoshimoto,  Towatari,  Katunuma,  Shizuka,  Kishi,  Marquis,  Ru,  Zeng,  Trout,  LoCastro,  Gribble,  Witherington,  Fenwick,  Garnier,  Tomaszek,  Tew,  Hemling,  Quinn,  Smith,  Zhao,  McQueney,  Janson,  D'Alessio,  Veber,  Nakamura,  Sato,  Hirata,  Yamamoto,  Vääräniemi,  Halleen,  Kaarlonen,  Ylipahkala,  Alatalo,  Andersson,  Kaija,  Vihko,  Väänänen,  Yamashita,  Marquis,  Xie,  Nidamarthy,  Oh,  Jeong,  Erhard,  Ward,  Roethke,  Smith,  Cheng,  Geng,  Lin,  Offen,  Wang,  Nevins,  Head,  Haltiwanger,  Narducci Sarjeant,  Liable-Sands,  Zhao,  Smith,  Janson,  Gao,  Tomaszek,  McQueney,  James,  Gress,  Zembryki,  Lark,  Veber,  Marquis,  Ru,  LoCastro,  Zeng,  Yamashita,  Oh,  Erhard,  Davis,  Tomaszek,  Tew,  Salyers,  Proksch,  Ward,  Smith,  Levy,  Cummings,  Haltiwanger,  Trescher,  Wang,  Hemling,  Quinn,  Cheng,  Lin,  Smith,  Janson,  Zhao,  McQueney,  D'Alessio,  Lee,  Marzulli,  Dodds,  Blake,  Hwang,  James,  Gress,  Bradley,  Lark,  Gowen,  Veber,  Tavares,  Boncek,  Deaton,  Hassell,  Long,  Miller,  Payne,  Miller,  Shewchuk,  Wells-Knecht,  Willard,  Wright,  Zhou,  Li-Korotky,  Swarts,  Hebda,  Doyle,  Altmann,  Cowan-Jacob,  Missbach,  Kishimoto,  Fukumoto,  Nishihara,  Mizumura,  Hirai,  Teshima,  Anway,  Wright,  Zirkin,  Korah,  Mort,  Hermo,  
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Disease relevance of Ctsk


High impact information on Ctsk


Chemical compound and disease context of Ctsk


Biological context of Ctsk


Anatomical context of Ctsk


Associations of Ctsk with chemical compounds

  • Epoxy succinate peptide derivatives, CLIK-066, 088, 112, 121, 148, 181, 185 and 187, are typical specific inhibitors for cathepsin L. Aldehyde derivatives CLIK-060 and CLIK-164 showed specific inhibition against cathepsin S and cathepsin K, respectively [17].
  • Structure-based development of pyridoxal propionate derivatives as specific inhibitors of cathepsin K in vitro and in vivo [18].
  • CLIK-166, in which the position 4 aldehyde of CLIK-071 is replaced by a vinyl radical and position 5 is additionally modified, showed cathepsin K-specific inhibition at 10(-5) M [18].
  • New synthetic pyridoxal propionate derivatives, -162, -163, and -164, in which the methyl arm of position 6 of CLIK-071 was additionally modified, strongly inhibited cathepsin K and cathepsin S weakly, but other cathepsins were not inhibited [18].
  • Starting from the high-throughput screening hit 1a, novel cathepsin K inhibitors have been developed based on a purine scaffold [19].

Other interactions of Ctsk

  • Further, the results suggest that cathepsin K, in both its secreted and lysosomal forms, may play a role in the degradation of Sertoli cell residual bodies [15].
  • MMP-13 may play an important role in degradation of type I collagen in bone matrix, acting in concert with cathepsin K and MMP-9 produced by osteoclasts [20].
  • Quantitative real-time PCR showed that TNF-alpha, RANK and TRAP mRNA expression did not change significantly with time, and that IL-1beta and cathepsin K changed slightly compared with those in the synovium [21].
  • Our results show the presence of vacuolar H+-ATPase, small GTPase rab7 as well as dense aggregates of F-actin at the peripheral ruffled border, where basolaterally endocytosed transferrin and cathepsin K are delivered [22].
  • The proteases MMP-13, cathepsin K, and tartrate-resistant acid phosphatase (TRAP) have collagenolytic activity and have been shown in rat ligament tissues [23].

Analytical, diagnostic and therapeutic context of Ctsk


  1. Cathepsin gene expression profile in rat acute pneumococcal otitis media. Li-Korotky, H.S., Swarts, J.D., Hebda, P.A., Doyle, W.J. Laryngoscope (2004) [Pubmed]
  2. Cathepsin K, but not cathepsins B, L, or S, is abundantly expressed in human osteoclasts. Drake, F.H., Dodds, R.A., James, I.E., Connor, J.R., Debouck, C., Richardson, S., Lee-Rykaczewski, E., Coleman, L., Rieman, D., Barthlow, R., Hastings, G., Gowen, M. J. Biol. Chem. (1996) [Pubmed]
  3. Design of potent, selective, and orally bioavailable inhibitors of cysteine protease cathepsin k. Tavares, F.X., Boncek, V., Deaton, D.N., Hassell, A.M., Long, S.T., Miller, A.B., Payne, A.A., Miller, L.R., Shewchuk, L.M., Wells-Knecht, K., Willard, D.H., Wright, L.L., Zhou, H.Q. J. Med. Chem. (2004) [Pubmed]
  4. A cysteine protease inhibitor prevents suspension-induced declines in bone weight and strength in rats. Nikawa, T., Ikemoto, M., Watanabe, C., Kitano, T., Kano, M., Yoshimoto, M., Towatari, T., Katunuma, N., Shizuka, F., Kishi, K. Journal of physiological anthropology and applied human science. (2002) [Pubmed]
  5. Proteolytic excision of a repressive loop domain in tartrate-resistant acid phosphatase by cathepsin K in osteoclasts. Ljusberg, J., Wang, Y., Lång, P., Norgård, M., Dodds, R., Hultenby, K., Ek-Rylander, B., Andersson, G. J. Biol. Chem. (2005) [Pubmed]
  6. Analysis of the kinetics of osteoclastogenesis in arthritic rats. Schett, G., Stolina, M., Bolon, B., Middleton, S., Adlam, M., Brown, H., Zhu, L., Feige, U., Zack, D.J. Arthritis Rheum. (2005) [Pubmed]
  7. Acidification of the osteoclastic resorption compartment provides insight into the coupling of bone formation to bone resorption. Karsdal, M.A., Henriksen, K., Sørensen, M.G., Gram, J., Schaller, S., Dziegiel, M.H., Heegaard, A.M., Christophersen, P., Martin, T.J., Christiansen, C., Bollerslev, J. Am. J. Pathol. (2005) [Pubmed]
  8. Pharmacological sequestration of intracellular cholesterol in late endosomes disrupts ruffled border formation in osteoclasts. Zhao, H., Väänänen, H.K. J. Bone Miner. Res. (2006) [Pubmed]
  9. Peptide aldehyde inhibitors of cathepsin K inhibit bone resorption both in vitro and in vivo. Votta, B.J., Levy, M.A., Badger, A., Bradbeer, J., Dodds, R.A., James, I.E., Thompson, S., Bossard, M.J., Carr, T., Connor, J.R., Tomaszek, T.A., Szewczuk, L., Drake, F.H., Veber, D.F., Gowen, M. J. Bone Miner. Res. (1997) [Pubmed]
  10. A potent small molecule, nonpeptide inhibitor of cathepsin K (SB 331750) prevents bone matrix resorption in the ovariectomized rat. Lark, M.W., Stroup, G.B., James, I.E., Dodds, R.A., Hwang, S.M., Blake, S.M., Lechowska, B.A., Hoffman, S.J., Smith, B.R., Kapadia, R., Liang, X., Erhard, K., Ru, Y., Dong, X., Marquis, R.W., Veber, D., Gowen, M. Bone (2002) [Pubmed]
  11. A cytochemical assay for osteoclast cathepsin K activity. Dodds, R.A. Cell Biochem. Funct. (2003) [Pubmed]
  12. Cyclic ketone inhibitors of the cysteine protease cathepsin K. Marquis, R.W., Ru, Y., Zeng, J., Trout, R.E., LoCastro, S.M., Gribble, A.D., Witherington, J., Fenwick, A.E., Garnier, B., Tomaszek, T., Tew, D., Hemling, M.E., Quinn, C.J., Smith, W.W., Zhao, B., McQueney, M.S., Janson, C.A., D'Alessio, K., Veber, D.F. J. Med. Chem. (2001) [Pubmed]
  13. Structure activity relationships of 5-, 6-, and 7-methyl-substituted azepan-3-one cathepsin K inhibitors. Yamashita, D.S., Marquis, R.W., Xie, R., Nidamarthy, S.D., Oh, H.J., Jeong, J.U., Erhard, K.F., Ward, K.W., Roethke, T.J., Smith, B.R., Cheng, H.Y., Geng, X., Lin, F., Offen, P.H., Wang, B., Nevins, N., Head, M.S., Haltiwanger, R.C., Narducci Sarjeant, A.A., Liable-Sands, L.M., Zhao, B., Smith, W.W., Janson, C.A., Gao, E., Tomaszek, T., McQueney, M., James, I.E., Gress, C.J., Zembryki, D.L., Lark, M.W., Veber, D.F. J. Med. Chem. (2006) [Pubmed]
  14. Azepanone-based inhibitors of human and rat cathepsin K. Marquis, R.W., Ru, Y., LoCastro, S.M., Zeng, J., Yamashita, D.S., Oh, H.J., Erhard, K.F., Davis, L.D., Tomaszek, T.A., Tew, D., Salyers, K., Proksch, J., Ward, K., Smith, B., Levy, M., Cummings, M.D., Haltiwanger, R.C., Trescher, G., Wang, B., Hemling, M.E., Quinn, C.J., Cheng, H.Y., Lin, F., Smith, W.W., Janson, C.A., Zhao, B., McQueney, M.S., D'Alessio, K., Lee, C.P., Marzulli, A., Dodds, R.A., Blake, S., Hwang, S.M., James, I.E., Gress, C.J., Bradley, B.R., Lark, M.W., Gowen, M., Veber, D.F. J. Med. Chem. (2001) [Pubmed]
  15. Expression and localization of cathepsin k in adult rat sertoli cells. Anway, M.D., Wright, W.W., Zirkin, B.R., Korah, N., Mort, J.S., Hermo, L. Biol. Reprod. (2004) [Pubmed]
  16. Intracellular machinery for matrix degradation in bone-resorbing osteoclasts. Vääräniemi, J., Halleen, J.M., Kaarlonen, K., Ylipahkala, H., Alatalo, S.L., Andersson, G., Kaija, H., Vihko, P., Väänänen, H.K. J. Bone Miner. Res. (2004) [Pubmed]
  17. Study of the functional share of lysosomal cathepsins by the development of specific inhibitors. Katunuma, N., Matsui, A., Kakegawa, T., Murata, E., Asao, T., Ohba, Y. Adv. Enzyme Regul. (1999) [Pubmed]
  18. Structure-based development of pyridoxal propionate derivatives as specific inhibitors of cathepsin K in vitro and in vivo. Katunuma, N., Matsui, A., Inubushi, T., Murata, E., Kakegawa, H., Ohba, Y., Turk, D., Turk, V., Tada, Y., Asao, T. Biochem. Biophys. Res. Commun. (2000) [Pubmed]
  19. Novel purine nitrile derived inhibitors of the cysteine protease cathepsin K. Altmann, E., Cowan-Jacob, S.W., Missbach, M. J. Med. Chem. (2004) [Pubmed]
  20. Immunolocalization of matrix metalloproteinase-13 on bone surface under osteoclasts in rat tibia. Nakamura, H., Sato, G., Hirata, A., Yamamoto, T. Bone (2004) [Pubmed]
  21. Gene expression relevant to osteoclastogenesis in the synovium and bone marrow of mature rats with collagen-induced arthritis. Kishimoto, Y., Fukumoto, S., Nishihara, S., Mizumura, H., Hirai, K., Teshima, R. Rheumatology (Oxford, England) (2004) [Pubmed]
  22. Osteoclast ruffled border has distinct subdomains for secretion and degraded matrix uptake. Mulari, M.T., Zhao, H., Lakkakorpi, P.T., Väänänen, H.K. Traffic (2003) [Pubmed]
  23. Blockade of the sympathetic nervous system degrades ligament in a rat MCL model. Dwyer, K.W., Provenzano, P.P., Muir, P., Valhmu, W.B., Vanderby, R. J. Appl. Physiol. (2004) [Pubmed]
  24. New insights into the regulation of cathepsin K gene expression by osteoprotegerin ligand. Corisdeo, S., Gyda, M., Zaidi, M., Moonga, B.S., Troen, B.R. Biochem. Biophys. Res. Commun. (2001) [Pubmed]
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