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Chemical Compound Review

Ac-DEVD-CHO     (4S)-4-[[(2S)-2-acetamido-3- carboxy...

Synonyms: CHEMBL417149, CHEBI:59385, DNC009146, MF 191, AC1LD91U, ...
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Disease relevance of Ac-DEVD-CHO


High impact information on Ac-DEVD-CHO

  • Like PARP, cleavage of these substrates in apoptotic cell extracts is abolished by nanomolar concentrations of Ac-DEVD-CHO and micromolar amounts of Ac-YVAD-CHO, confirming the involvement of apopain or an apopain-like activity [5].
  • In addition, cells undergoing TRAIL-mediated apoptosis displayed cleavage of poly(ADP)-ribose polymerase (PARP) that was completely blocked by Ac-DEVD-CHO [6].
  • CPP32-like protease activity plays an essential role in this system, as the caspase inhibitor, Ac-DEVD-CHO, strongly inhibited fodrin and lamin B1 cleavage, as well as nuclear morphology changes [7].
  • This cleavage was inhibited by Ac-DEVD-CHO in a similar manner as that of poly(ADP)ribose polymerase, a known substrate of CPP32/caspase-3 [8].
  • We conclude that granzyme B activates an ICE-dependent cell death pathway in some cell types and requires a CPP32-like Ac-DEVD-CHO inhibitable protease acting upstream to initiate apoptosis [9].

Chemical compound and disease context of Ac-DEVD-CHO


Biological context of Ac-DEVD-CHO

  • Induction of s-Myc- and c-Myc-mediated apoptotic cell death was effectively prevented by caspase inhibitors such as Z-Asp-CH2-DCB and Ac-DEVD-CHO [11].
  • A specific caspase-3 inhibitor (Ac-DEVD-CHO) could reverse this phenotype [12].
  • The activation of CED-3-related caspases was further confirmed by an increase in the rate of Z-DEVD-7-amino-4-trifluoromethylcoumarin (Z-DEVD-AFC) hydrolysis that was sensitive to Ac-DEVD-CHO and was inhibited by pretreatment of the cells with TPCK but not by DCI [13].
  • Apoptosis, as demonstrated by oligonucleosomal DNA fragmentation and fluorescence microscopy, was induced 24 h after VVC treatment, which was also prevented by caspase-3 inhibitor, Ac-DEVD-CHO [14].
  • An inhibition of caspase enzyme activity by Ac-DEVD-CHO, a caspase-3 inhibitor, significantly increased cell viability in H(2)O(2)-treated cells [15].

Anatomical context of Ac-DEVD-CHO


Associations of Ac-DEVD-CHO with other chemical compounds


Gene context of Ac-DEVD-CHO

  • The apoptotic effects of fas agonists in IFN-gamma-treated human and murine FA-C cells were blocked when pretreated with inhibitors (ac-DEVD-cho, CP-DEVD-cho, Z-DEVD-FMK) of the caspase 3 protease [24].
  • However, DNA fragmentation induced by either allospecific FasL-defective CTL, or by perforin-deficient, TNP-modified, H-2b target cell-specific CTL was prevented in ICE -/- target cells loaded by electroporation with Ac-DEVD-CHO, an inhibitor of CPP32 and related ICE family proteases [25].
  • While lamin B is cleaved by caspase 6, the protease responsible for the cleavage of LAP2 and Nup153 was probably caspase 3, since (1) cleavage of both proteins was specifically prevented by in vivo addition of caspase 3 inhibitor Ac-DEVD-CHO and (2) consensus sites for these caspases are present in both proteins [26].
  • When A549 cells were pretreated with the caspase-inhibitory peptide N-acetyl-asp-Glu-Val-Asp-CHO (aldehyde) (Ac-DEVD-CHO), Adv/p16-mediated apoptosis and Rb cleavage were greatly inhibited [27].
  • In contrast, caspase 3-like activity was observed within minutes of E. histolytica contact and the caspase 3 inhibitor Ac-DEVD-CHO blocked Jurkat T cell death, as measured by both DNA fragmentation and 51Cr release [28].

Analytical, diagnostic and therapeutic context of Ac-DEVD-CHO

  • Ac-DEVD-CHO was similarly effective when given before reperfusion [2].
  • When the PN graft was implanted 2 weeks after injury, however, MNs failed to regenerate following Ac-DEVD-CHO treatment, whereas 53% of MNs regenerated their axons into the graft after treatment with Boc-D-FMK [29].
  • Western blotting and activity measurements showed that caspase-3 was indeed activated, but its peptide inhibitor (Ac-DEVD-CHO) neither suppressed nuclear fragmentation nor rescued the neurons from cell death. z-VAD-fmk, the general inhibitor of caspases, prevented nuclear fragmentation and delayed the cell death [30].
  • In MNU-treated rats, the TUNEL index 24 hr post-MNU was 79.5% in the peripheral and 83.7% in the central retina, while the Ac-DEVD-CHO injection significantly reduced it to 59.7 and 71.8%, respectively [31].
  • By using specific caspase inhibitors (Ac-DEVD-CHO, Ac-IETD-CHO and zVAD-fmk), we showed that caspase-3 and -7 (DEVDases) are major effector caspases during EV-induced apoptosis in permissive L929 and RK-13 cell cultures [32].


  1. Antiapoptotic role of endogenous nitric oxide in human melanoma cells. Salvucci, O., Carsana, M., Bersani, I., Tragni, G., Anichini, A. Cancer Res. (2001) [Pubmed]
  2. Inhibition of caspase-3 improves contractile recovery of stunned myocardium, independent of apoptosis-inhibitory effects. Ruetten, H., Badorff, C., Ihling, C., Zeiher, A.M., Dimmeler, S. J. Am. Coll. Cardiol. (2001) [Pubmed]
  3. V642I APP-inducible neuronal cells: a model system for investigating Alzheimer's disorders. Niikura, T., Murayama, N., Hashimoto, Y., Ito, Y., Yamagishi, Y., Matsuoka, M., Takeuchi, Y., Aiso, S., Nishimoto, I. Biochem. Biophys. Res. Commun. (2000) [Pubmed]
  4. Binding of tumour necrosis factor-alpha (TNF-alpha) to TNF-RI induces caspase(s)-dependent apoptosis in human cholangiocarcinoma cell lines. Utaisincharoen, P., Ubol, S., Tangthawornchaikul, N., Chaisuriya, P., Sirisinha, S. Clin. Exp. Immunol. (1999) [Pubmed]
  5. Apopain/CPP32 cleaves proteins that are essential for cellular repair: a fundamental principle of apoptotic death. Casciola-Rosen, L., Nicholson, D.W., Chong, T., Rowan, K.R., Thornberry, N.A., Miller, D.K., Rosen, A. J. Exp. Med. (1996) [Pubmed]
  6. Interleukin 1 beta-converting enzyme related proteases/caspases are involved in TRAIL-induced apoptosis of myeloma and leukemia cells. Mariani, S.M., Matiba, B., Armandola, E.A., Krammer, P.H. J. Cell Biol. (1997) [Pubmed]
  7. Cytochrome c activation of CPP32-like proteolysis plays a critical role in a Xenopus cell-free apoptosis system. Kluck, R.M., Martin, S.J., Hoffman, B.M., Zhou, J.S., Green, D.R., Newmeyer, D.D. EMBO J. (1997) [Pubmed]
  8. Involvement of caspase-dependent activation of cytosolic phospholipase A2 in tumor necrosis factor-induced apoptosis. Wissing, D., Mouritzen, H., Egeblad, M., Poirier, G.G., Jäättelä, M. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
  9. Activation of an interleukin 1 converting enzyme-dependent apoptosis pathway by granzyme B. Shi, L., Chen, G., MacDonald, G., Bergeron, L., Li, H., Miura, M., Rotello, R.J., Miller, D.K., Li, P., Seshadri, T., Yuan, J., Greenberg, A.H. Proc. Natl. Acad. Sci. U.S.A. (1996) [Pubmed]
  10. Calpain and caspase-3 inhibitors reduce infarct size and post-ischemic apoptosis in rat heart without modifying contractile recovery. Perrin, C., Ecarnot-Laubriet, A., Vergely, C., Rochette, L. Cell. Mol. Biol. (Noisy-le-grand) (2003) [Pubmed]
  11. A functional role for death proteases in s-Myc- and c-Myc-mediated apoptosis. Kagaya, S., Kitanaka, C., Noguchi, K., Mochizuki, T., Sugiyama, A., Asai, A., Yasuhara, N., Eguchi, Y., Tsujimoto, Y., Kuchino, Y. Mol. Cell. Biol. (1997) [Pubmed]
  12. Arsenic trioxide induces apoptosis in human T-cell leukemia virus type 1- and type 2-infected cells by a caspase-3-dependent mechanism involving Bcl-2 cleavage. Mahieux, R., Pise-Masison, C., Gessain, A., Brady, J.N., Olivier, R., Perret, E., Misteli, T., Nicot, C. Blood (2001) [Pubmed]
  13. Fas-mediated apoptosis in mouse hepatocytes involves the processing and activation of caspases. Jones, R.A., Johnson, V.L., Buck, N.R., Dobrota, M., Hinton, R.H., Chow, S.C., Kass, G.E. Hepatology (1998) [Pubmed]
  14. Vibrio vulnificus cytolysin induces superoxide anion-initiated apoptotic signaling pathway in human ECV304 cells. Kwon, K.B., Yang, J.Y., Ryu, D.G., Rho, H.W., Kim, J.S., Park, J.W., Kim, H.R., Park, B.H. J. Biol. Chem. (2001) [Pubmed]
  15. Melatonin protects against hydrogen peroxide-induced cell death signaling in SH-SY5Y cultured cells: involvement of nuclear factor kappa B, Bax and Bcl-2. Chetsawang, B., Putthaprasart, C., Phansuwan-Pujito, P., Govitrapong, P. J. Pineal Res. (2006) [Pubmed]
  16. Investigation of glucocorticoid-induced apoptotic pathway: processing of caspase-6 but not caspase-3. Miyashita, T., Nagao, K., Krajewski, S., Salvesen, G.S., Reed, J.C., Inoue, T., Yamada, M. Cell Death Differ. (1998) [Pubmed]
  17. Caspase activation of mammalian sterile 20-like kinase 3 (Mst3). Nuclear translocation and induction of apoptosis. Huang, C.Y., Wu, Y.M., Hsu, C.Y., Lee, W.S., Lai, M.D., Lu, T.J., Huang, C.L., Leu, T.H., Shih, H.M., Fang, H.I., Robinson, D.R., Kung, H.J., Yuan, C.J. J. Biol. Chem. (2002) [Pubmed]
  18. Expression of dominant-negative Fas-associated death domain blocks human keratinocyte apoptosis and vesication induced by sulfur mustard. Rosenthal, D.S., Velena, A., Chou, F.P., Schlegel, R., Ray, R., Benton, B., Anderson, D., Smith, W.J., Simbulan-Rosenthal, C.M. J. Biol. Chem. (2003) [Pubmed]
  19. Processing and activation of pro-interleukin-16 by caspase-3. Zhang, Y., Center, D.M., Wu, D.M., Cruikshank, W.W., Yuan, J., Andrews, D.W., Kornfeld, H. J. Biol. Chem. (1998) [Pubmed]
  20. Interruption of nuclear factor kappaB signaling by the androgen receptor facilitates 12-O-tetradecanoylphorbolacetate-induced apoptosis in androgen-sensitive prostate cancer LNCaP cells. Altuwaijri, S., Lin, H.K., Chuang, K.H., Lin, W.J., Yeh, S., Hanchett, L.A., Rahman, M.M., Kang, H.Y., Tsai, M.Y., Zhang, Y., Yang, L., Chang, C. Cancer Res. (2003) [Pubmed]
  21. Inhibition of CPP32-like proteases prevents granzyme B- and Fas-, but not granzyme A-based cytotoxicity exerted by CTL clones. Anel, A., Gamen, S., Alava, M.A., Schmitt-Verhulst, A.M., Piñeiro, A., Naval, J. J. Immunol. (1997) [Pubmed]
  22. DNA fragmentation induced by protease activation in p53-null human leukemia HL60 cells undergoing apoptosis following treatment with the topoisomerase I inhibitor camptothecin: cell-free system studies. Shimizu, T., Pommier, Y. Exp. Cell Res. (1996) [Pubmed]
  23. Transforming growth factor beta1 attenuates ceramide-induced CPP32/Yama activation and apoptosis in human leukaemic HL-60 cells. Kuo, M.L., Chen, C.W., Jee, S.H., Chuang, S.E., Cheng, A.L. Biochem. J. (1997) [Pubmed]
  24. Interferon-gamma-induced apoptotic responses of Fanconi anemia group C hematopoietic progenitor cells involve caspase 8-dependent activation of caspase 3 family members. Rathbun, R.K., Christianson, T.A., Faulkner, G.R., Jones, G., Keeble, W., O'Dwyer, M., Bagby, G.C. Blood (2000) [Pubmed]
  25. IL-1 beta convertase (ICE) does not play a requisite role in apoptosis induced in T lymphoblasts by Fas-dependent or Fas-independent CTL effector mechanisms. Smith, D.J., McGuire, M.J., Tocci, M.J., Thiele, D.L. J. Immunol. (1997) [Pubmed]
  26. Caspase-dependent proteolysis of integral and peripheral proteins of nuclear membranes and nuclear pore complex proteins during apoptosis. Buendia, B., Santa-Maria, A., Courvalin, J.C. J. Cell. Sci. (1999) [Pubmed]
  27. Activation of caspase-3 and cleavage of Rb are associated with p16-mediated apoptosis in human non-small cell lung cancer cells. Katsuda, K., Kataoka, M., Uno, F., Murakami, T., Kondo, T., Roth, J.A., Tanaka, N., Fujiwara, T. Oncogene (2002) [Pubmed]
  28. Caspase 3-dependent killing of host cells by the parasite Entamoeba histolytica. Huston, C.D., Houpt, E.R., Mann, B.J., Hahn, C.S., Petri, W.A. Cell. Microbiol. (2000) [Pubmed]
  29. Inhibition of caspases promotes long-term survival and reinnervation by axotomized spinal motoneurons of denervated muscle in newborn rats. Chan, Y.M., Yick, L.W., Yip, H.K., So, K.F., Oppenheim, R.W., Wu, W. Exp. Neurol. (2003) [Pubmed]
  30. Involvement of TLCK-sensitive serine protease in colchicine-induced cell death of sympathetic neurons in culture. Mitsui, C., Sakai, K., Ninomiya, T., Koike, T. J. Neurosci. Res. (2001) [Pubmed]
  31. Caspase-3 inhibitor rescues N -methyl- N -nitrosourea-induced retinal degeneration in Sprague-Dawley rats. Yoshizawa, K., Yang, J., Senzaki, H., Uemura, Y., Kiyozuka, Y., Shikata, N., Oishi, Y., Miki, H., Tsubura, A. Exp. Eye Res. (2000) [Pubmed]
  32. Apoptosis during ectromelia orthopoxvirus infection is DEVDase dependent: in vitro and in vivo studies. Krzyzowska, M., Schollenberger, A., Skierski, J., Niemialtowski, M. Microbes Infect. (2002) [Pubmed]
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