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Gene Review

CASP7  -  caspase 7, apoptosis-related cysteine...

Homo sapiens

Synonyms: Apoptotic protease Mch-3, CASP-7, CMH-1, Caspase-7, ICE-LAP3, ...
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High impact information on CASP7

  • These observations suggest that CPP32 and Mch3 are targets of mature Mch4 protease in apoptotic cells [1].
  • We call this enzyme Mch3/SCA-2 [2].
  • We have purified from hamster liver a second cysteine protease that cleaves and activates sterol regulatory element binding proteins (SREBPs). cDNA cloning revealed that this enzyme is the hamster equivalent of Mch3, a human enzyme that is related to the interleukin 1beta converting enzyme [2].
  • Mch3, a novel human apoptotic cysteine protease highly related to CPP32 [3].
  • Here we report the cloning of a new Ced-3/interleukin 1 beta-converting enzyme-related gene, designated Mch3, that encodes a protein with the highest degree of homology to CPP32 compared to other family members [3].

Biological context of CASP7


Anatomical context of CASP7


Associations of CASP7 with chemical compounds

  • CMH-1 shares conserved amino acid residues that form the core structure of ICE as well as those residues involved in catalysis and in the P1 aspartate binding [5].
  • In Jurkat T cells, Fas ligation or addition of exogenous C2-ceramide induced activations of caspase-3/CPP32 and caspase-7/Mch3 followed by PARP cleavage, effects that can be blocked either by SPP or TPA [9].

Enzymatic interactions of CASP7


Regulatory relationships of CASP7


Other interactions of CASP7


Analytical, diagnostic and therapeutic context of CASP7


  1. In vitro activation of CPP32 and Mch3 by Mch4, a novel human apoptotic cysteine protease containing two FADD-like domains. Fernandes-Alnemri, T., Armstrong, R.C., Krebs, J., Srinivasula, S.M., Wang, L., Bullrich, F., Fritz, L.C., Trapani, J.A., Tomaselli, K.J., Litwack, G., Alnemri, E.S. Proc. Natl. Acad. Sci. U.S.A. (1996) [Pubmed]
  2. Purification and cDNA cloning of a second apoptosis-related cysteine protease that cleaves and activates sterol regulatory element binding proteins. Pai, J.T., Brown, M.S., Goldstein, J.L. Proc. Natl. Acad. Sci. U.S.A. (1996) [Pubmed]
  3. Mch3, a novel human apoptotic cysteine protease highly related to CPP32. Fernandes-Alnemri, T., Takahashi, A., Armstrong, R., Krebs, J., Fritz, L., Tomaselli, K.J., Wang, L., Yu, Z., Croce, C.M., Salveson, G. Cancer Res. (1995) [Pubmed]
  4. ICE-LAP3, a novel mammalian homologue of the Caenorhabditis elegans cell death protein Ced-3 is activated during Fas- and tumor necrosis factor-induced apoptosis. Duan, H., Chinnaiyan, A.M., Hudson, P.L., Wing, J.P., He, W.W., Dixit, V.M. J. Biol. Chem. (1996) [Pubmed]
  5. Identification and characterization of CPP32/Mch2 homolog 1, a novel cysteine protease similar to CPP32. Lippke, J.A., Gu, Y., Sarnecki, C., Caron, P.R., Su, M.S. J. Biol. Chem. (1996) [Pubmed]
  6. Caspase 7 is a positional candidate gene for IDDM 17 in a Bedouin Arab family. Babu, S.R., Bao, F., Roberts, C.M., Martin, A.K., Gowan, K., Eisenbarth, G.S., Fain, P.R. Ann. N. Y. Acad. Sci. (2003) [Pubmed]
  7. Chromosomal localization of the human genes, CPP32, Mch2, Mch3, and Ich-1, involved in cellular apoptosis. Tiso, N., Pallavicini, A., Muraro, T., Zimbello, R., Apolloni, E., Valle, G., Lanfranchi, G., Danieli, G.A. Biochem. Biophys. Res. Commun. (1996) [Pubmed]
  8. Cytotoxic T-cell-derived granzyme B activates the apoptotic protease ICE-LAP3. Chinnaiyan, A.M., Hanna, W.L., Orth, K., Duan, H., Poirier, G.G., Froelich, C.J., Dixit, V.M. Curr. Biol. (1996) [Pubmed]
  9. Sphingosine 1-phosphate inhibits activation of caspases that cleave poly(ADP-ribose) polymerase and lamins during Fas- and ceramide-mediated apoptosis in Jurkat T lymphocytes. Cuvillier, O., Rosenthal, D.S., Smulson, M.E., Spiegel, S. J. Biol. Chem. (1998) [Pubmed]
  10. Chromosomal mapping of cell death proteases CPP32, MCH2, and MCH3. Bullrich, F., Fernandes-Alnemri, T., Litwack, G., Alnemri, E.S., Croce, C.M. Genomics (1996) [Pubmed]
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