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Gene Review

ced-3  -  Protein CED-3

Caenorhabditis elegans

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Disease relevance of ced-3


High impact information on ced-3


Biological context of ced-3

  • The genes ced-3 and ced-4 define the first known step of a developmental pathway for programmed cell death, suggesting that these genes may be involved in determining which cells die during C. elegans development [7].
  • The ability of ced-3 and ced-4 alleles to restrict virus replication is correlated with their cell-killing activities [1].
  • This Pn.p cell death is suppressed by mutations in the caspase gene ced-3 and in the bcl-2 homolog ced-9, suggesting that the Pn.p cells are dying by PCD in pvl-5 mutants [8].
  • For example, lin-22 animals display transformations affecting entire postembryonic cell lineages, unc-86 animals are altered at an intermediate level of certain cell lineages, and ced-3 animals are affected only in the ultimate fates of cells produced by terminal cell divisions.(ABSTRACT TRUNCATED AT 400 WORDS)[9]
  • Silencing of the rad-51 gene also causes a reduction in fecundity, which is suppressed by mutation in the DNA damage checkpoint gene rad-5, but not in the cell death effector gene ced-3 [10].

Anatomical context of ced-3


Associations of ced-3 with chemical compounds

  • Vertebrate homologues of both ced-3 and ced-9 have been identified as the genes encoding the caspase cysteine proteases and the Bcl-2 family, respectively [14].

Regulatory relationships of ced-3


Other interactions of ced-3

  • To study the mechanism of lin-39 function, we isolated P. pacificus cell death mutants and identified mutations in ced-3 [12].

Analytical, diagnostic and therapeutic context of ced-3

  • Since molecular cloning of the C. elegans ced-3 gene revealed its homology with mammalian IL-1beta-converting enzyme,1 14 members of the caspase family have been identified, which have often been involved as mediators of one or more phases of the apoptotic process [16].


  1. Restriction of vaccinia virus replication by a ced-3 and ced-4-dependent pathway in Caenorhabditis elegans. Liu, W.H., Lin, Y.L., Wang, J.P., Liou, W., Hou, R.F., Wu, Y.C., Liao, C.L. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  2. Programmed cell death mediated by ced-3 and ced-4 protects Caenorhabditis elegans from Salmonella typhimurium-mediated killing. Aballay, A., Ausubel, F.M. Proc. Natl. Acad. Sci. U.S.A. (2001) [Pubmed]
  3. Retroviral transfer of CPP32beta gene into malignant gliomas in vitro and in vivo. Kondo, S., Tanaka, Y., Kondo, Y., Ishizaka, Y., Hitomi, M., Haqqi, T., Liu, J., Barnett, G.H., Alnemri, E.S., Barna, B.P. Cancer Res. (1998) [Pubmed]
  4. Involvement of interleukin-1beta-converting enzyme in apoptosis of irradiated retinoblastomas. Kondo, Y., Liu, J., Haqqi, T., Barna, B.P., Kondo, S. Invest. Ophthalmol. Vis. Sci. (1998) [Pubmed]
  5. Apoptosis: a process with a (beta)NAC for complexity. Shaham, S. Cell (2003) [Pubmed]
  6. The C. elegans cell death gene ced-3 encodes a protein similar to mammalian interleukin-1 beta-converting enzyme. Yuan, J., Shaham, S., Ledoux, S., Ellis, H.M., Horvitz, H.R. Cell (1993) [Pubmed]
  7. Genetic control of programmed cell death in the nematode C. elegans. Ellis, H.M., Horvitz, H.R. Cell (1986) [Pubmed]
  8. The Caenorhabditis elegans pvl-5 gene protects hypodermal cells from ced-3-dependent, ced-4-independent cell death. Joshi, P., Eisenmann, D.M. Genetics (2004) [Pubmed]
  9. Mutations that affect neural cell lineages and cell fates during the development of the nematode Caenorhabditis elegans. Horvitz, H.R., Sternberg, P.W., Greenwald, I.S., Fixsen, W., Ellis, H.M. Cold Spring Harb. Symp. Quant. Biol. (1983) [Pubmed]
  10. Roles for Caenorhabditis elegans rad-51 in meiosis and in resistance to ionizing radiation during development. Rinaldo, C., Bazzicalupo, P., Ederle, S., Hilliard, M., La Volpe, A. Genetics (2002) [Pubmed]
  11. Genetic control of programmed cell death in the Caenorhabditis elegans hermaphrodite germline. Gumienny, T.L., Lambie, E., Hartwieg, E., Horvitz, H.R., Hengartner, M.O. Development (1999) [Pubmed]
  12. The Pristionchus HOX gene Ppa-lin-39 inhibits programmed cell death to specify the vulva equivalence group and is not required during vulval induction. Sommer, R.J., Eizinger, A., Lee, K.Z., Jungblut, B., Bubeck, A., Schlak, I. Development (1998) [Pubmed]
  13. Accumulation of caspase-3 messenger ribonucleic acid and induction of caspase activity in the ovine corpus luteum following prostaglandin F2alpha treatment in vivo. Rueda, B.R., Hendry, I.R., Tilly, J.L., Hamernik, D.L. Biol. Reprod. (1999) [Pubmed]
  14. CED-4 induces chromatin condensation in Schizosaccharomyces pombe and is inhibited by direct physical association with CED-9. James, C., Gschmeissner, S., Fraser, A., Evan, G.I. Curr. Biol. (1997) [Pubmed]
  15. Bcl-2 overexpression blocks activation of the death protease CPP32/Yama/apopain. Monney, L., Otter, I., Olivier, R., Ravn, U., Mirzasaleh, H., Fellay, I., Poirier, G.G., Borner, C. Biochem. Biophys. Res. Commun. (1996) [Pubmed]
  16. Caspase activation without death. Zeuner, A., Eramo, A., Peschle, C., De Maria, R. Cell Death Differ. (1999) [Pubmed]
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