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Gene Review

Ctsh  -  cathepsin H

Rattus norvegicus

Synonyms: Pro-cathepsin H
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Disease relevance of Ctsh


High impact information on Ctsh

  • The 252-residue sequence of cathepsin B and the 220-residue sequence of cathepsin H were determined largely by automated Edman degradation of their intact polypeptide chains and of the two chains of each enzyme generated by limited proteolysis [4].
  • A glycopeptide containing 3 amino acids, 2 glucosamines, and 6 mannoses was isolated from cathepsin H [5].
  • It inhibits most thiol proteinases such as cathepsin H, L, B, and C, papain, and ficin, but not calcium-activated neutral proteinase or serine proteinases or carboxyl proteinases [6].
  • Treatment of heavily infected animals with co-trimoxazole cleared the lungs of P. carinii, and this was accompanied by a marked reduction in proteinase activity, in particular, cathepsin H-like activity, which fell from 108- to 3-fold the mean control value following drug treatment [7].
  • We also identified several genes involved with stress responses (cathepsin H, UBC2E, IGFBP3, smoothelin) [8].

Chemical compound and disease context of Ctsh


Biological context of Ctsh

  • The amino acid sequence in the pro-peptide region, in particular, residues Phe-(-41) to Ser-(-29) of cathepsin H, is highly homologous to the pro-peptide regions of other cysteine proteinases [10].
  • 1. A rat cathepsin H cDNA was isolated from a rat liver cDNA library with synthetic oligonucleotide probes [1].
  • 5. The activity of cathepsin H does not change throughout this period nor do the cathepsins exhibit marked changes in activity in the placenta during this same period or in the PYS from days 12.5 to 14.5 of gestation [11].
  • Under the optimal conditions the rate of leukotriene D4 transformation by cathepsin H was about 3% of the hydrolysis rate of alpha-N-benzoyl-DL-arginine-2-naphthylamide which is commonly utilized as a very efficient substrate to test the peptidase activity of the enzyme [12].
  • This enzyme displayed a clear difference in substrate specificity when compared with other thiol proteases such as cathepsin B, cathepsin H, and cathepsin L, known to be present in the kidney [13].

Anatomical context of Ctsh

  • The activities of cathespins B, L, and/or J were similar to those of liver or kidney lysosomes, but the levels of cathepsin H activity were much lower than those of liver or kidney lysosomes [14].
  • Staining of cathepsin H was strong in panlobular hepatocytes, especially in the periphery of the cytoplasm, possibly representing the peribiliary dense bodies; and weaker in periportal sinusoidal cells, possibly Kupffer cells [15].
  • Immunodeposits for cathepsin H only were demonstrated in lamellar bodies of Type II alveolar epithelial cells, suggesting the cosecretion of surfactants and cathepsin H from the cells into the alveolar space [16].
  • Moreover, the presence of cathepsin H in secretory granules of the cells may indicate that the enzyme participates in the activation of secretory products [17].
  • Moreover, immunoreactivity for cathepsin B appeared mainly in principal cells and was more intense in the head of the epididymis than in the tail, whereas that for cathepsin H appeared in both principal and clear cells and was more intense in the tail than the head [18].

Associations of Ctsh with chemical compounds


Regulatory relationships of Ctsh


Other interactions of Ctsh


Analytical, diagnostic and therapeutic context of Ctsh


  1. Molecular cloning of rat precursor cathepsin H and the expression of five lysosomal cathepsins in normal tissues and in a rat carcinosarcoma. Qian, F., Frankfater, A., Miller, R.V., Chan, S.J., Steiner, D.F. Int. J. Biochem. (1990) [Pubmed]
  2. Expression and the role of cathepsin H in human glioma progression and invasion. Sivaparvathi, M., Sawaya, R., Gokaslan, Z.L., Chintala, S.K., Rao, J.S., Chintala, K.S. Cancer Lett. (1996) [Pubmed]
  3. Biochemical properties of thiol proteinase inhibitor purified from psoriatic scales. Ohtani, O., Fukuyama, K., Epstein, W.L. J. Invest. Dermatol. (1982) [Pubmed]
  4. Homology of amino acid sequences of rat liver cathepsins B and H with that of papain. Takio, K., Towatari, T., Katunuma, N., Teller, D.C., Titani, K. Proc. Natl. Acad. Sci. U.S.A. (1983) [Pubmed]
  5. Cathepsins B and H from porcine spleen. Purification, polypeptide chain arrangements, and carbohydrate content. Takahashi, T., Dehdarani, A.H., Schmidt, P.G., Tang, J. J. Biol. Chem. (1984) [Pubmed]
  6. Purification and characterization of thiol proteinase inhibitor from rat liver. Kominami, E., Wakamatsu, N., Katunuma, N. J. Biol. Chem. (1982) [Pubmed]
  7. Alterations in cysteine proteinase content of rat lung associated with development of Pneumocystis carinii infection. Hayes, D.J., Stubberfield, C.R., McBride, J.D., Wilson, D.L. Infect. Immun. (1991) [Pubmed]
  8. Microarray analysis of retinoid-dependent gene activity during rat embryogenesis: increased collagen fibril production in a model of retinoid insufficiency. Flentke, G.R., Baker, M.W., Docterman, K.E., Power, S., Lough, J., Smith, S.M. Dev. Dyn. (2004) [Pubmed]
  9. Poliovirus-encoded proteinase 3C: a possible evolutionary link between cellular serine and cysteine proteinase families. Gorbalenya, A.E., Blinov, V.M., Donchenko, A.P. FEBS Lett. (1986) [Pubmed]
  10. Molecular cloning and sequencing of cDNA for rat cathepsin H. Homology in pro-peptide regions of cysteine proteinases. Ishidoh, K., Imajoh, S., Emori, Y., Ohno, S., Kawasaki, H., Minami, Y., Kominami, E., Katunuma, N., Suzuki, K. FEBS Lett. (1987) [Pubmed]
  11. The activities of thiol proteases in the rat visceral yolk sac increase during late gestation. Grubb, J.D., Koszalk, T.R., Drabick, J.J., Metrione, R.M. Placenta (1991) [Pubmed]
  12. Transformation of leukotriene D4 catalyzed by lysosomal cathepsin H of rat liver. Yokota, K., Shono, F., Yamamoto, S., Kominami, E., Katunuma, N. J. Biochem. (1983) [Pubmed]
  13. Soluble endothelin degradation enzyme activities in various rat tissues. Deng, Y., Jeng, A.Y. Biochem. Cell Biol. (1992) [Pubmed]
  14. Simple preparation of rat brain lysosomes and their proteolytic properties. Ohshita, T., Kido, H. Anal. Biochem. (1995) [Pubmed]
  15. Different immunolocalizations of cathepsins B, H, and L in the liver. Ii, K., Hizawa, K., Kominami, E., Bando, Y., Katunuma, N. J. Histochem. Cytochem. (1985) [Pubmed]
  16. Cysteine proteinases in bronchoalveolar epithelial cells and lavage fluid of rat lung. Ishii, Y., Hashizume, Y., Watanabe, T., Waguri, S., Sato, N., Yamamoto, M., Hasegawa, S., Kominami, E., Uchiyama, Y. J. Histochem. Cytochem. (1991) [Pubmed]
  17. Immunocytochemical localization of cathepsins B and H in corticotrophs and melanotrophs of rat pituitary gland. Uchiyama, Y., Nakajima, M., Muno, D., Watanabe, T., Ishii, Y., Waguri, S., Sato, N., Kominami, E. J. Histochem. Cytochem. (1990) [Pubmed]
  18. Lysosomal cysteine proteinases in rat epididymis. Tomomasa, H., Waguri, S., Umeda, T., Koiso, K., Kominami, E., Uchiyama, Y. J. Histochem. Cytochem. (1994) [Pubmed]
  19. Cysteine proteinase content of rat muscle lysosomes. Evidence for an unusual proteinase activity. Obled, A., Ouali, A., Valin, C. Biochimie (1984) [Pubmed]
  20. Characterisation of a cysteine protease from bloodstream forms of Trypanosoma congolense. Mbawa, Z.R., Gumm, I.D., Shaw, E., Lonsdale-Eccles, J.D. Eur. J. Biochem. (1992) [Pubmed]
  21. Glomerular basement membrane degradation by endogenous cysteine proteinases in isolated rat glomeruli. Baricos, W.H., Cortez, S.L., Le, Q.C., Zhou, Y.W., Dicarlo, R.M., O'Connor, S.E., Shah, S.V. Kidney Int. (1990) [Pubmed]
  22. Functional interface between cathepsins and growth factors in the kidney development. Vattimo, M.d.e. .F., Santos, O.F. Renal failure. (2005) [Pubmed]
  23. Linkage between phosphorylated cystatin alpha and filaggrin by epidermal transglutaminase as a model of cornified envelope and inhibition of cathepsin L activity by cornified envelope and the conjugated cystatin alpha. Takahashi, M., Tezuka, T., Kakegawa, H., Katunuma, N. FEBS Lett. (1994) [Pubmed]
  24. Involvement of a cystatin-alpha-sensitive cysteine proteinase in the degradation of native L-lactate dehydrogenase and serum albumin by rat liver or kidney lysosomes. Ohshita, T., Kido, H. Eur. J. Biochem. (1994) [Pubmed]
  25. Specific localization of lysosomal aminopeptidases in type II alveolar epithelial cells of the rat lung. Yayoi, Y., Ohsawa, Y., Koike, M., Zhang, G., Kominami, E., Uchiyama, Y. Arch. Histol. Cytol. (2001) [Pubmed]
  26. Identification and possible regulation of muscle cell lysosomal protease activity by exogenous protease inhibitors. Stauber, W.T., Gauthier, F., Ong, S.H. Acta Biol. Med. Ger. (1981) [Pubmed]
  27. Prevention of cardiac hypertrophy in experimental chronic renal failure by long-term ACE inhibitor administration: potential role of lysosomal proteinases. Suzuki, H., Schaefer, L., Ling, H., Schaefer, R.M., Dämmrich, J., Teschner, M., Heidland, A. American journal of nephrology. (1995) [Pubmed]
  28. Expression of cathepsin H in differentiating rat spermatids: immunoelectron microscopic study. Haraguchi, C.M., Ishido, K., Kominami, E., Yokota, S. Histochem. Cell Biol. (2003) [Pubmed]
  29. Changes in immunoreactivity for cathepsin H in rat type II alveolar epithelial cells and its proteolytic activity in bronchoalveolar lavage fluid over 24 hours. Ishii, Y., Hashizume, Y., Kominami, E., Uchiyama, Y. Anat. Rec. (1991) [Pubmed]
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