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Noxa

Introduction

Phorbol-12-myristate-13-acetate-induced protein 1, also known as PMAIP1 and Noxa, is a human gene.[1]

Noxa (Latin for damage) is a pro-apoptotic member of the Bcl-2 protein family.[2] Bcl-2 family members can form hetero- or homodimers, and they act as anti- or pro-apoptotic regulators that are involved in a wide variety of cellular activities. The expression of Noxa is regulated by the tumor suppressor p53, and Noxa has been shown to be involved in p53-mediated apoptosis.

See also

See also

References

References

  1. ↑ “Entrez Gene: PMAIP1 phorbol-12-myristate-13-acetate-induced protein 1”.
  2. ↑ Oda, E. (2000). “Noxa, a BH3-only member of the Bcl-2 family and candidate mediator of p53-induced apoptosis”. Science. 288: 1053–1058. Unknown parameter |month= ignored (help); Unknown parameter |coauthors= ignored (help)
Further reading

Further reading

  • Hijikata M, Kato N, Sato T; et al. (1990). “Molecular cloning and characterization of a cDNA for a novel phorbol-12-myristate-13-acetate-responsive gene that is highly expressed in an adult T-cell leukemia cell line”. J. Virol. 64 (10): 4632–9. PMID 2398525.
  • Oda E, Ohki R, Murasawa H; et al. (2000). “Noxa, a BH3-only member of the Bcl-2 family and candidate mediator of p53-induced apoptosis”. Science. 288 (5468): 1053–8. PMID 10807576.
  • Venter JC, Adams MD, Myers EW; et al. (2001). “The sequence of the human genome”. Science. 291 (5507): 1304–51. doi:10.1126/science.1058040. PMID 11181995.
  • Strausberg RL, Feingold EA, Grouse LH; et al. (2003). “Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences”. Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
  • Jansson AK, Emterling AM, Arbman G, Sun XF (2003). “Noxa in colorectal cancer: a study on DNA, mRNA and protein expression”. Oncogene. 22 (30): 4675–8. doi:10.1038/sj.onc.1206655. PMID 12879012.
  • Seo YW, Shin JN, Ko KH; et al. (2004). “The molecular mechanism of Noxa-induced mitochondrial dysfunction in p53-mediated cell death”. J. Biol. Chem. 278 (48): 48292–9. doi:10.1074/jbc.M308785200. PMID 14500711.
  • Kim JY, Ahn HJ, Ryu JH; et al. (2004). “BH3-only protein Noxa is a mediator of hypoxic cell death induced by hypoxia-inducible factor 1alpha”. J. Exp. Med. 199 (1): 113–24. doi:10.1084/jem.20030613. PMID 14699081.
  • Yakovlev AG, Di Giovanni S, Wang G; et al. (2004). “BOK and NOXA are essential mediators of p53-dependent apoptosis”. J. Biol. Chem. 279 (27): 28367–74. doi:10.1074/jbc.M313526200. PMID 15102863.
  • Qin JZ, Stennett L, Bacon P; et al. (2005). “p53-independent NOXA induction overcomes apoptotic resistance of malignant melanomas”. Mol. Cancer Ther. 3 (8): 895–902. PMID 15299072.
  • Gerhard DS, Wagner L, Feingold EA; et al. (2004). “The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)”. Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.
  • Flinterman M, Guelen L, Ezzati-Nik S; et al. (2005). “E1A activates transcription of p73 and Noxa to induce apoptosis”. J. Biol. Chem. 280 (7): 5945–59. doi:10.1074/jbc.M406661200. PMID 15572378.
  • Chen L, Willis SN, Wei A; et al. (2005). “Differential targeting of prosurvival Bcl-2 proteins by their BH3-only ligands allows complementary apoptotic function”. Mol. Cell. 17 (3): 393–403. doi:10.1016/j.molcel.2004.12.030. PMID 15694340.
  • Sun Y, Leaman DW (2005). “Involvement of Noxa in cellular apoptotic responses to interferon, double-stranded RNA, and virus infection”. J. Biol. Chem. 280 (16): 15561–8. doi:10.1074/jbc.M412630200. PMID 15705586.
  • Ceballos E, Muñoz-Alonso MJ, Berwanger B; et al. (2005). “Inhibitory effect of c-Myc on p53-induced apoptosis in leukemia cells. Microarray analysis reveals defective induction of p53 target genes and upregulation of chaperone genes”. Oncogene. 24 (28): 4559–71. doi:10.1038/sj.onc.1208652. PMID 15856024.
  • Willis SN, Chen L, Dewson G; et al. (2005). “Proapoptotic Bak is sequestered by Mcl-1 and Bcl-xL, but not Bcl-2, until displaced by BH3-only proteins”. Genes Dev. 19 (11): 1294–305. doi:10.1101/gad.1304105. PMID 15901672.
  • Alves NL, Derks IA, Berk E; et al. (2006). “The Noxa/Mcl-1 axis regulates susceptibility to apoptosis under glucose limitation in dividing T cells”. Immunity. 24 (6): 703–16. doi:10.1016/j.immuni.2006.03.018. PMID 16782027.
  • Obexer P, Geiger K, Ambros PF; et al. (2007). “FKHRL1-mediated expression of Noxa and Bim induces apoptosis via the mitochondria in neuroblastoma cells”. Cell Death Differ. 14 (3): 534–47. doi:10.1038/sj.cdd.4402017. PMID 16888645.
  • Fribley AM, Evenchik B, Zeng Q; et al. (2006). “Proteasome inhibitor PS-341 induces apoptosis in cisplatin-resistant squamous cell carcinoma cells by induction of Noxa”. J. Biol. Chem. 281 (42): 31440–7. doi:10.1074/jbc.M604356200. PMID 16928686.
  • Smit LA, Hallaert DY, Spijker R; et al. (2007). “Differential Noxa/Mcl-1 balance in peripheral versus lymph node chronic lymphocytic leukemia cells correlates with survival capacity”. Blood. 109 (4): 1660–8. doi:10.1182/blood-2006-05-021683. PMID 17038534.
  • Armstrong JL, Veal GJ, Redfern CP, Lovat PE (2007). “Role of Noxa in p53-independent fenretinide-induced apoptosis of neuroectodermal tumours”. Apoptosis. 12 (3): 613–22. doi:10.1007/s10495-006-0020-1. PMID 17216584.
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