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Gene Review

CST5  -  cystatin D

Homo sapiens

Synonyms: Cystatin-5, Cystatin-D
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Disease relevance of CST5


High impact information on CST5

  • Crystal structure of human cystatin D, a cysteine peptidase inhibitor with restricted inhibition profile [4].
  • The structures reveal differences in the peptidase-interacting regions when compared with other cystatins, providing plausible explanations for the restricted inhibitory specificity of cystatin D for some papain-like peptidases and its lack of reactivity toward legumain-related enzymes [4].
  • Two alleles of the cystatin D gene (CST5), encoding protein variants with either Cys or Arg as residue 26 in their 122-residue polypeptide chains, are present in the population [5].
  • The inhibitory properties displayed by cystatin D suggest that it has a function in saliva as inhibitor of either endogenous or exogenous enzymes with cathepsin S- or H-like properties [5].
  • A cDNA coding for cystatin D, a human member of the cystatin protein family, has been cloned after specific amplification of reverse-transcribed parotid gland RNA [1].

Chemical compound and disease context of CST5


Biological context of CST5


Anatomical context of CST5

  • Expression of type 2 cystatin genes CST1-CST5 in adult human tissues and the developing submandibular gland [8].
  • On the basis of structural and functional properties, cystatin D represents a novel cysteine proteinase inhibitor possibly playing a protective role against proteinases present in the oral cavity [1].

Other interactions of CST5

  • Two members (CST4 and CST5) of the cystatin gene family have been characterized partially by DNA analysis [6].
  • The second cystatin pseudogene was elucidated in the clone, CST5, and it was assigned to the CSTP2 locus [6].
  • Such N-terminal truncation of cystatin C caused >300-fold lower inhibition of papain, cathepsin B, L and K, whereas the cathepsin H activity was compromised by a factor of ca. 10. Similarly, truncation of cystatin D caused alleviated inhibition of all endogenous target enzymes investigated [9].

Analytical, diagnostic and therapeutic context of CST5


  1. Human cystatin D. cDNA cloning, characterization of the Escherichia coli expressed inhibitor, and identification of the native protein in saliva. Freije, J.P., Balbín, M., Abrahamson, M., Velasco, G., Dalbøge, H., Grubb, A., López-Otín, C. J. Biol. Chem. (1993) [Pubmed]
  2. Different cysteine proteinases involved in bone resorption and osteoclast formation. Brage, M., Abrahamson, M., Lindström, V., Grubb, A., Lerner, U.H. Calcif. Tissue Int. (2005) [Pubmed]
  3. Cystatin D, a natural salivary cysteine protease inhibitor, inhibits coronavirus replication at its physiologic concentration. Collins, A.R., Grubb, A. Oral Microbiol. Immunol. (1998) [Pubmed]
  4. Crystal structure of human cystatin D, a cysteine peptidase inhibitor with restricted inhibition profile. Alvarez-Fernandez, M., Liang, Y.H., Abrahamson, M., Su, X.D. J. Biol. Chem. (2005) [Pubmed]
  5. Structural and functional characterization of two allelic variants of human cystatin D sharing a characteristic inhibition spectrum against mammalian cysteine proteinases. Balbín, M., Hall, A., Grubb, A., Mason, R.W., López-Otín, C., Abrahamson, M. J. Biol. Chem. (1994) [Pubmed]
  6. Characterization of two members (CST4 and CST5) of the cystatin gene family and molecular evolution of cystatin genes. Saitoh, E., Isemura, S., Sanada, K., Ohnishi, K. Agents Actions Suppl. (1992) [Pubmed]
  7. Localization of the human cystatin D gene (CST5) to chromosome 20p11.21 by in situ hybridization. Freije, J.P., Pendás, A.M., Velasco, G., Roca, A., Abrahamson, M., López-Otín, C. Cytogenet. Cell Genet. (1993) [Pubmed]
  8. Expression of type 2 cystatin genes CST1-CST5 in adult human tissues and the developing submandibular gland. Dickinson, D.P., Thiesse, M., Hicks, M.J. DNA Cell Biol. (2002) [Pubmed]
  9. Down-regulation of human extracellular cysteine protease inhibitors by the secreted staphylococcal cysteine proteases, staphopain A and B. Vincents, B., Onnerfjord, P., Gruca, M., Potempa, J., Abrahamson, M. Biol. Chem. (2007) [Pubmed]
  10. Structure and expression of the gene encoding cystatin D, a novel human cysteine proteinase inhibitor. Freije, J.P., Abrahamson, M., Olafsson, I., Velasco, G., Grubb, A., López-Otín, C. J. Biol. Chem. (1991) [Pubmed]
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