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Chemical Compound Review

Chymostatin     (2S)-2-[[(S)-(2-amino- 3,4,5,6...

Synonyms: CHEMBL247767, CHEBI:510447, DNC007963, LS-187745, FT-0623815, ...
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Disease relevance of Chymostatin


Psychiatry related information on Chymostatin

  • When 3-week-old dystrophic mice received chymostatin (1 mg/kg, i.p.), the decrease in locomotor activity was retarded, serum enzyme levels decreased significantly, and muscle protein content increased significantly [6].

High impact information on Chymostatin

  • Chymostatin selectively inhibited the monocyte-derived plasminogen activators [7].
  • Detection and partial characterization of a chymostatin-sensitive endopeptidase in transformed fibroblasts [1].
  • Concurrent treatment with the protease inhibitor chymostatin completely prevents PrPc loss [8].
  • These results suggest that the apparent induction of intracellular transglutaminase activity is mediated by a chymostatin-sensitive protease, while both phorbol ester binding and the reduction by TPA of epidermal growth factor binding at the cell membrane were independent [9].
  • On the other hand, (30bp)DNA has little or no effect on the reversible inhibition of cat G by MPI or chymostatin or on the irreversible inhibition of cat G by carbobenzoxy-Gly-Leu-Phe-chloromethylketone [10].

Chemical compound and disease context of Chymostatin


Biological context of Chymostatin


Anatomical context of Chymostatin

  • Evidence that the enzyme being released in the peritoneal cavity of rats was chymase was provided both by its appearance after adding specific mast cell activators (ie, compound 48/80 and anti-IgE [gamma E immunoglobulin]) and by inhibition with chymostatin [21].
  • Chymostatin inhibited both the in vitro enzymatic activity and the processing of profilaggrin in a cultured rat keratinocyte cell line [22].
  • When monocytes were preincubated with drugs for 1 hr and washed, TLCK, TPCK, and PMSF inhibited cytolysis, whereas the less effective chymostatin and TAME and the inactive BPTI had no effect under these conditions [23].
  • The protease inhibitors leupeptin and chymostatin, which slowed overall proteolysis in nongrowing muscles and hepatocytes, reduced the degradation of the ACh receptor by 2--11-fold, but had no, or only slight, effects on the catabolism of average protein, even when overall proteolysis was accelerated by omitting serum and embryo extract [24].
  • The effect of synthetic analogues of chymostatin upon protein degradation in isolated skeletal muscle [25].

Associations of Chymostatin with other chemical compounds


Gene context of Chymostatin


Analytical, diagnostic and therapeutic context of Chymostatin

  • Chymostatin reversed ECP-mediated suppression of PHA-induced T-lymphocyte proliferation in separated cultures, but not in cocultures [35].
  • Crystallization of fiber purified in the presence of chymostatin provided crystals of a different structure under the electron microscope (crystals of type II), composed of 62-kDa fiber polypeptide units [36].
  • Affinity chromatography of chymotrypsin on a sepharose derivative coupled with a chymostatin analogue [37].
  • This may make some contribution to the regulation of tissue perfusion, as seen in the ischemic dog heart and the human leg; and (2) chymostatin-sensitive or the chymase type which only forms angiotensin II and may participate in structural remodelling of heart and vessels rather than in tissue perfusion [38].


  1. Detection and partial characterization of a chymostatin-sensitive endopeptidase in transformed fibroblasts. O'Donnell-Tormey, J., Quigley, J.P. Proc. Natl. Acad. Sci. U.S.A. (1983) [Pubmed]
  2. Inhibition of experimental blood-borne lung metastasis by protease inhibitors. Saito, D., Sawamura, M., Umezawa, K., Kanai, Y., Furihata, C., Matsushima, T., Sugimura, T. Cancer Res. (1980) [Pubmed]
  3. Calpain inhibitor I reduces the activation of nuclear factor-kappaB and organ injury/dysfunction in hemorrhagic shock. McDonald, M.C., Mota-Filipe, H., Paul, A., Cuzzocrea, S., Abdelrahman, M., Harwood, S., Plevin, R., Chatterjee, P.K., Yaqoob, M.M., Thiemermann, C. FASEB J. (2001) [Pubmed]
  4. Chymase as a proangiogenic factor. A possible involvement of chymase-angiotensin-dependent pathway in the hamster sponge angiogenesis model. Muramatsu, M., Katada, J., Hayashi, I., Majima, M. J. Biol. Chem. (2000) [Pubmed]
  5. Structure of the complex formed between the bacterial-produced inhibitor chymostatin and the serine enzyme Streptomyces griseus protease A. Delbaere, L.T., Brayer, G.D. J. Mol. Biol. (1980) [Pubmed]
  6. Beneficial effect of chymostatin on dystrophic mice. Komatsu, K., Matsui, A., Satoh, S. Exp. Neurol. (1986) [Pubmed]
  7. Neutral protease secretion by human monocytes. Effect of surface-bound immune complexes. Ragsdale, C.G., Arend, W.P. J. Exp. Med. (1979) [Pubmed]
  8. Destabilization of the non-pathogenic, cellular prion-protein by a small molecular drug. Ochel, H.J., Gademann, G. Antivir. Ther. (Lond.) (2004) [Pubmed]
  9. Inhibition of 12-O-tetradecanoylphorbol-13-acetate induction of epidermal transglutaminase activity by protease inhibitors. Kawamura, H., Strickland, J.E., Yuspa, S.H. Cancer Res. (1983) [Pubmed]
  10. DNA strongly impairs the inhibition of cathepsin G by alpha(1)-antichymotrypsin and alpha(1)-proteinase inhibitor. Duranton, J., Boudier, C., Belorgey, D., Mellet, P., Bieth, J.G. J. Biol. Chem. (2000) [Pubmed]
  11. Leukocyte protease activities in myotonic dystrophy: studies on effects of protease inhibitors. Goto, I., Shinno, N., Kuroiwa, Y. Eur. Neurol. (1987) [Pubmed]
  12. Determination of the cytotoxic effect of Clostridium histolyticum culture supernatant on HeLa cells in the presence of protease inhibitors. Jóźwiak, J., Komar, A., Jankowska, E., Martirosian, G. FEMS Immunol. Med. Microbiol. (2005) [Pubmed]
  13. Involvement of malarial proteases in the interaction between the parasite and host erythrocyte in Plasmodium knowlesi infections. Banyal, H.S., Misra, G.C., Gupta, C.M., Dutta, G.P. J. Parasitol. (1981) [Pubmed]
  14. Differential effects of proteinase inhibitors and amines on the lysosomal and non-lysosomal pathways of protein degradation in isolated rat hepatocytes. Grinde, B., Seglen, P.O. Biochim. Biophys. Acta (1980) [Pubmed]
  15. Inhibitors and pathways of hepatocytic protein degradation. Seglen, P.O., Gordon, P.B., Grinde, B., Solheim, A., Kovács, A.L., Poli, A. Acta Biol. Med. Ger. (1981) [Pubmed]
  16. Mast cell chymase. A potent secretagogue for airway gland serous cells. Sommerhoff, C.P., Caughey, G.H., Finkbeiner, W.E., Lazarus, S.C., Basbaum, C.B., Nadel, J.A. J. Immunol. (1989) [Pubmed]
  17. Peptide aldehyde complexes with wheat serine carboxypeptidase II: implications for the catalytic mechanism and substrate specificity. Bullock, T.L., Breddam, K., Remington, S.J. J. Mol. Biol. (1996) [Pubmed]
  18. Slow-binding inhibition of chymotrypsin and cathepsin G by the peptide aldehyde chymostatin. Stein, R.L., Strimpler, A.M. Biochemistry (1987) [Pubmed]
  19. Isolation and characterization of an extracellular proteinase of Coccidioides immitis. Yuan, L., Cole, G.T. Infect. Immun. (1987) [Pubmed]
  20. A novel member of the subtilisin-like protease family from Streptomyces albogriseolus. Suzuki, M., Taguchi, S., Yamada, S., Kojima, S., Miura, K.I., Momose, H. J. Bacteriol. (1997) [Pubmed]
  21. Evidence for in vivo degradation of C3a anaphylatoxin by mast cell chymase. I. Nonspecific activation of rat peritoneal mast cells by C3ades Arg. Kajita, T., Hugli, T.E. Am. J. Pathol. (1991) [Pubmed]
  22. Identification of proteolytic cleavage sites in the conversion of profilaggrin to filaggrin in mammalian epidermis. Resing, K.A., Walsh, K.A., Haugen-Scofield, J., Dale, B.A. J. Biol. Chem. (1989) [Pubmed]
  23. Rapid killing of actinomycin D-treated tumor cells by human monocytes. II. Cytotoxicity is independent of secretion of reactive oxygen intermediates and is suppressed by protease inhibitors. Colotta, F., Bersani, L., Lazzarin, A., Poli, G., Mantovani, A. J. Immunol. (1985) [Pubmed]
  24. Comparison of the control and pathways for degradation of the acetylcholine receptor and average protein in cultured muscle cells. Libby, P., Goldberg, A.L. J. Cell. Physiol. (1981) [Pubmed]
  25. The effect of synthetic analogues of chymostatin upon protein degradation in isolated skeletal muscle. Mulligan, M.T., Galpin, I.J., Wilby, A.H., Beynon, R.J. Biochem. J. (1985) [Pubmed]
  26. Plasmodium falciparum antigens synthesized by schizonts and stabilized at the merozoite surface when schizonts mature in the presence of protease inhibitors. Lyon, J.A., Haynes, J.D. J. Immunol. (1986) [Pubmed]
  27. Angiotensin converting enzyme (ACE) and non-ACE dependent angiotensin II generation in resistance arteries from patients with heart failure and coronary heart disease. Petrie, M.C., Padmanabhan, N., McDonald, J.E., Hillier, C., Connell, J.M., McMurray, J.J. J. Am. Coll. Cardiol. (2001) [Pubmed]
  28. Activation of matrix-degrading metalloproteinases by mast cell proteases in atherosclerotic plaques. Johnson, J.L., Jackson, C.L., Angelini, G.D., George, S.J. Arterioscler. Thromb. Vasc. Biol. (1998) [Pubmed]
  29. Purification and characterization of a multicatalytic high-molecular-mass proteinase from rat skeletal muscle. Dahlmann, B., Kuehn, L., Rutschmann, M., Reinauer, H. Biochem. J. (1985) [Pubmed]
  30. Effects of metabolites present during growth of Tetrahymena pyriformis on the subsequent secretion of lysosomal hydrolases. Blum, J.J. J. Cell. Physiol. (1975) [Pubmed]
  31. Oral treponemes and their outer membrane extracts activate human gingival epithelial cells through toll-like receptor 2. Asai, Y., Jinno, T., Ogawa, T. Infect. Immun. (2003) [Pubmed]
  32. Interleukin-1alpha-induced proteolytic activation of metalloproteinase-9 by human skin. Han, Y.P., Downey, S., Garner, W.L. Surgery (2005) [Pubmed]
  33. Alternative pathway to endothelin-converting enzyme for the synthesis of endothelin in human blood vessels. Maguire, J., Davenport, A.P. J. Cardiovasc. Pharmacol. (2004) [Pubmed]
  34. Biochemical analysis of prostate specific antigen-proteolyzed insulin-like growth factor binding protein-3. Fielder, P.J., Rosenfeld, R.G., Graves, H.C., Grandbois, K., Maack, C.A., Sawamura, S., Ogawa, Y., Sommer, A., Cohen, P. Growth Regul. (1994) [Pubmed]
  35. Regulation of lymphocyte proliferation by eosinophils via chymotrypsin-like protease activity and adhesion molecule interaction. Matsunaga, Y., Shono, M., Takahashi, M., Tsuboi, Y., Ogawa, K., Yamada, T. Br. J. Pharmacol. (2000) [Pubmed]
  36. Crystallization, enzymatic cleavage, and the polarity of the adenovirus type 2 fiber. Devaux, C., Caillet-Boudin, M.L., Jacrot, B., Boulanger, P. Virology (1987) [Pubmed]
  37. Affinity chromatography of chymotrypsin on a sepharose derivative coupled with a chymostatin analogue. Nishikata, M. J. Biochem. (1983) [Pubmed]
  38. Serine protease angiotensin II systems. Arakawa, K. Journal of hypertension. Supplement : official journal of the International Society of Hypertension. (1996) [Pubmed]
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