Article thumbnail

Posttranslational Processing and Modification of Cathepsins and Cystatins

By Nobuhiko Katunuma

Abstract

Cathepsins are an essential protease family in all living cells. The cathepsins play an essential roles such as protein catabolism and protein synthesis. To targeting to various organella and to regulate their activity, the post translational-processing and modification play an important role Cathepsins are translated in polysome as the pre-pro-mature forms. The pre-peptide is removed cotranslationally and then translocated to Golgi-apparatus and the pro-part is removed and the mature-part is glycosylated, and the mature-part is targeted into the lysosome mediated by mannose-6-phosphate signal and the mature-part is bound with their coenzymes. The degradation of the mature-part is started by the limited proteolysis of the ordered nicked bonds to make hydrophobic peptides. The peptides are incorporated into phagosome or proteasome after ubiquitinated and are degrade into amino-acids. Cystatins are endogenous inhibitors of cathepsins. Cystatin α which is only located in skin is phosphorylated at the near C-terminus by protein kinase-C, and the phosphorylate-cystatin α is incorporated into cornified envelope and conjugated with filaggrin-fiber by transglutaminase to form the linker-fiber of skin. The cystatin α is modified by glutathione or make their dimmer, and they are inactive. Those modifications are regulated by the redox-potential by the glutathione

Topics: Review Article
Publisher: Hindawi Publishing Corporation
OAI identifier: oai:pubmedcentral.nih.gov:3100116
Provided by: PubMed Central

To submit an update or takedown request for this paper, please submit an Update/Correction/Removal Request.

Suggested articles

Citations

  1. (1986). A chymotrypsin-type serine protease in rat basophilic leukemia cells: evidence for its immunologic identity with atypical mast cell protease,”
  2. (1984). a k i o ,E .K o m i n a m i ,Y .B a n d o ,N .K a t u n u m a ,a n dK . Titani, “Amino acid sequence of rat epidermal thiol proteinase inhibitor,”
  3. (1988). Amino acid sequence of rat liver cathepsin
  4. (1983). Amino acid sequence of rat liver thiol proteinase inhibitor,”
  5. (1988). Biosyntheses and processing of lysosomal cysteine proteinases in rat macrophages,”
  6. Comparison of properties of thiol proteinase inhibitors from rat serum and liver,”
  7. (1978). Crystallization and amino acid composition of cathepsin B from rat liver lysosomes,”
  8. (1979). Crystallization and properties of cathepsin B from rat liver,”
  9. (1985). Different immunolocalizations of cathepsins
  10. (1984). Different tissue distributions of two types of thiol proteinase inhibitors from rat liver and epidermis,”
  11. (1988). Effect of proteinase inhibitors on intracellular processing of cathepsin
  12. (1991). Identification of hematoxylin-stainable protein in epidermal keratohyalin granules as phosphorylated cystatin α by protein kinase
  13. Immunological studies on cathepsinsBandHfromratliver,”JournalofBiochemistry,vol.
  14. (1989). Katunuma,“Gene structure and 5’-upstream sequence of rat cathepsin
  15. (1985). Molecular basis of intracellular regulation of thiol proteinase inhibitors,”
  16. (1987). Molecular cloning and sequencing of cDNA for rat cathepsin H Homology in propeptide regions of cysteine proteinases,”
  17. (1986). Nucleotide and predicted amino acid sequences of cloned human and mouse preprocathepsin B cDNAs,”
  18. (1985). o m i n a m i ,T .T s u k a h a r a ,Y .B a n d o ,a n dN .K a t a n u m a , “Distribution of cathepsins B and H in rat tissues and peripheral blood cells,”
  19. (1980). Primary structure study of rat liver cathepsin B: a striking resemblance to papain,”
  20. (1990). Properties and nature of a cysteine proteinase inhibitor located in keratohyalin granules of rat epidermis,”
  21. (1989). Regulation of inhibitory activity of cysteine proteinase inhibitor (cystatin β)b yg l u -tathione mediated covalent modification, glutathione centennial,”
  22. (1983). Selective cleavage of peptide bonds by cathepsins L and B from rat liver,”
  23. (1985). Structural studies on the carbohydrate moieties of rat liver cathepsins
  24. (1989). structure of rat cathepsin
  25. Structures and functions of lysosomal thiol proteinases and their endogenous inhibitor,” CurrentTopicsinCellularRegulation,vol.22,pp.71–101,1983.
  26. (1984). Three forms of thiol proteinase inhibitor from rat liver formed depending on the oxidation-reduction state of a sulfhydryl group,”
  27. Total synthesis of cystatin-α gene and its expression in E. Coli,”