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Journal of Signal Transduction
Volume 2010 (2010), Article ID 375345, 8 pages
http://dx.doi.org/10.1155/2010/375345
Review Article

Posttranslational Processing and Modification of Cathepsins and Cystatins

Institute for Health Sciences, Tokushima Bunri University, 180 Nishihamabouji, Yamashiro-cho, Tokushima City, Tokushima 770-8514, Japan

Received 24 May 2010; Accepted 9 August 2010

Academic Editor: Hsiang-fu Kung

Copyright © 2010 Nobuhiko Katunuma. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

  1. K. Hara, E. Kominami, and N. Katunuma, “Effect of proteinase inhibitors on intracellular processing of cathepsin B, H and L in rat macrophages,” FEBS Letters, vol. 231, no. 1, pp. 229–231, 1988. View at Google Scholar
  2. K. Ii, K. Hizawa, and E. Kominami, “Different immunolocalizations of cathepsins B, H, and L in the liver,” Journal of Histochemistry and Cytochemistry, vol. 33, no. 11, pp. 1173–1175, 1985. View at Google Scholar
  3. E. Kominami, T. Tsukahara, Y. Bando, and N. Katanuma, “Distribution of cathepsins B and H in rat tissues and peripheral blood cells,” Journal of Biochemistry, vol. 98, no. 1, pp. 87–93, 1985. View at Google Scholar
  4. E. Kominami and N. Katunuma, “Immunological studies on cathepsins B and H from rat liver,” Journal of Biochemistry, vol. 91, no. 1, pp. 67–71, 1982. View at Google Scholar
  5. E. Kominami, T. Tsukahara, K. Hara, and N. Katunuma, “Biosyntheses and processing of lysosomal cysteine proteinases in rat macrophages,” FEBS Letters, vol. 231, no. 1, pp. 225–228, 1988. View at Google Scholar
  6. S. J. Chan, S. B. Segundo, M. B. McCormick, and D. F. Steiner, “Nucleotide and predicted amino acid sequences of cloned human and mouse preprocathepsin B cDNAs,” Proceedings of the National Academy of Sciences of the United States of America, vol. 83, pp. 7721–7725, 1986. View at Google Scholar
  7. N. Katunuma and E. Kominami, “Structures and functions of lysosomal thiol proteinases and their endogenous inhibitor,” Current Topics in Cellular Regulation, vol. 22, pp. 71–101, 1983. View at Google Scholar
  8. K. Ishidoh, S. Imajoh, Y. Emori et al., “Molecular cloning and sequencing of cDNA for rat cathepsin H Homology in pro-peptide regions of cysteine proteinases,” FEBS Letters, vol. 226, no. 1, pp. 33–37, 1987. View at Google Scholar
  9. K. Ishidoh, E. Kominami, K. Suzuki, and N. Katunuma, “Gene structure and 5'-upstream sequence of rat cathepsin L,” FEBS Letters, vol. 259, no. 1, pp. 71–74, 1989. View at Publisher · View at Google Scholar
  10. T. Towatari and N. Katunuma, “Amino acid sequence of rat liver cathepsin L,” FEBS Letters, vol. 236, no. 1, pp. 57–61, 1988. View at Publisher · View at Google Scholar
  11. K. Takio, T. Towatari, N. Katunuma, and K. Titani, “Primary structure study of rat liver cathepsin B: a striking resemblance to papain,” Biochemical and Biophysical Research Communications, vol. 97, no. 1, pp. 340–346, 1980. View at Google Scholar
  12. T. Towatari and N. Katunuma, “Crystallization and amino acid composition of cathepsin B from rat liver lysosomes,” Biochemical and Biophysical Research Communications, vol. 83, no. 2, pp. 513–520, 1978. View at Google Scholar
  13. T. Towatari, Y. Kawabata, and N. Katunuma, “Crystallization and properties of cathepsin B from rat liver,” European Journal of Biochemistry, vol. 102, no. 1, pp. 279–289, 1979. View at Google Scholar
  14. T. Taniguchi, T. Mizuochi, and T. Towatari, “Structural studies on the carbohydrate moieties of rat liver cathepsins B and H,” Journal of Biochemistry, vol. 97, no. 3, pp. 973–976, 1985. View at Google Scholar
  15. K. Ishidoh, E. Kominami, N. Katunuma, and K. Suzuki, “Gene structure of rat cathepsin H,” FEBS Letters, vol. 253, no. 1-2, pp. 103–107, 1989. View at Publisher · View at Google Scholar
  16. E. Kominami, Y. Bando, N. Wakamatsu, and N. Katunuma, “Different tissue distributions of two types of thiol proteinase inhibitors from rat liver and epidermis,” Journal of Biochemistry, vol. 96, no. 5, pp. 1437–1442, 1984. View at Google Scholar
  17. H. Kido, K. Izumi, and H. Otsuka, “A chymotrypsin-type serine protease in rat basophilic leukemia cells: evidence for its immunologic identity with atypical mast cell protease,” Journal of Immunology, vol. 136, no. 3, pp. 1061–1065, 1986. View at Google Scholar
  18. T. Towatari and N. Katunuma, “Selective cleavage of peptide bonds by cathepsins L and B from rat liver,” Journal of Biochemistry, vol. 93, no. 4, pp. 1119–1128, 1983. View at Google Scholar
  19. N. Katunuma and E. Kominami, “Molecular basis of intracellular regulation of thiol proteinase inhibitors,” Current Topics in Cellular Regulation, vol. 27, pp. 345–360, 1985. View at Google Scholar
  20. K. Takio, E. Kominami, Y. Bando, N. Katunuma, and K. Titani, “Amino acid sequence of rat epidermal thiol proteinase inhibitor,” Biochemical and Biophysical Research Communications, vol. 121, no. 1, pp. 149–154, 1984. View at Google Scholar
  21. K. Takio, E. Kominami, N. Wakamatsu, N. Katunuma, and K. Titani, “Amino acid sequence of rat liver thiol proteinase inhibitor,” Biochemical and Biophysical Research Communications, vol. 115, no. 3, pp. 902–908, 1983. View at Google Scholar
  22. N. Wakamatsu, E. Kominami, and N. Katunuma, “Comparison of properties of thiol proteinase inhibitors from rat serum and liver,” Journal of Biological Chemistry, vol. 257, no. 24, pp. 14653–14656, 1982. View at Google Scholar
  23. M. Takahashi, T. Tezuka, T. Towatari, and N. Katunuma, “Identification of hematoxylin-stainable protein in epidermal keratohyalin granules as phosphorylated cystatin α by protein kinase C,” FEBS Letters, vol. 287, no. 1-2, pp. 178–180, 1991. View at Publisher · View at Google Scholar
  24. M. Takahashi, T. Tezuka, T. Towatari, and N. Katunuma, “Properties and nature of a cysteine proteinase inhibitor located in keratohyalin granules of rat epidermis,” FEBS Letters, vol. 267, no. 2, pp. 261–264, 1990. View at Publisher · View at Google Scholar · View at Scopus
  25. Y. Ike, M. Yamato, E. Kominami, and N. Katunuma, “Total synthesis of cystatin-α gene and its expression in E. Coli,” in Intracellular Proteolysis: Mechanisms and Regulations, N. Katunuma and E. Kominami, Eds., pp. 391–393, Japan Scientific Societies Press, Tokyo, Japan, 1989. View at Google Scholar
  26. N. Katunuma and E. Kominami, “Regulation of inhibitory activity of cysteine proteinase inhibitor (cystatin β) by glutathione mediated covalent modification, glutathione centennial,” in Molecular Perspectives and Clinical Implications, pp. 89–100, Academic Press, New York, NY, USA, 1989. View at Google Scholar
  27. N. Wakamatsu, E. Kominami, K. Takio, and N. Katunuma, “Three forms of thiol proteinase inhibitor from rat liver formed depending on the oxidation-reduction state of a sulfhydryl group,” Journal of Biological Chemistry, vol. 259, no. 22, pp. 13832–13838, 1984. View at Google Scholar