The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

AATF  -  apoptosis antagonizing transcription factor

Homo sapiens

Synonyms: Apoptosis-antagonizing transcription factor, BFR2, CHE-1, CHE1, DED, ...
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of AATF

  • In primary renal tubule epithelial cells, overexpression of AATF mediated by recombinant adeno-associated virus (AAV) vectors resulted in significant antiapoptotic activity, whereas knockdown of AATF by small interference RNA led to exacerbated cell death after IRI [1].
  • The list includes 11 catalytically active caspases, 26 CARD (caspase associated recruitment domain)-, 32 DD (death domain)-, 12 DED (death effector domain)-, 8 BIR (baculovirus inhibitor of apoptosis protein region)-, 24 BH (Bcl-2 homology)-, and 34 PAAD/PYD (pyrin/PAAD)-containing sequences [2].
  • However, when human dermal fibroblasts were incorporated into DED, the number of epidermal cysts formed by wild-type ES cells increased dramatically, and small groups of keratin 14-positive cells differentiated from beta(1)-null ES cells [3].
  • Emerged epidermal cultures on dead de-epidermized dermis (DED) constitute an excellent model for in vitro reproduction of dermatoses linked to a keratinocyte defect [4].

High impact information on AATF

  • In search of novel interaction partners of AATF, we identified the tumor susceptibility gene product TSG101, which had also been recognized as a co-regulator of nuclear hormone receptors [5].
  • Moreover, AATF enhances steroid receptor-mediated transactivation in a hormone- and dose-dependent manner (Leister, P., Burgdorf, S., and Scheidtmann, K. H., (2003) Signal Transduction 3, 18-25) [5].
  • Mutagenesis studies revealed that the translocation of the DED of DEDD2 to the nucleus is essential for its pro-apoptotic activity [6].
  • It now is reported that AATF is expressed in human kidney proximal tubule (HK-2) cells and in mouse primary renal tubule epithelial cells [1].
  • Apoptosis antagonizing transcription factor (AATF) is a leucine zipper domain-containing protein that has antiapoptotic properties [1].

Biological context of AATF

  • Interestingly, AATF interfered with Dlk-induced apoptosis [7].
  • Indeed, a Gal4-BD-AATF fusion protein exhibited strong transactivation activity [7].
  • In transfected HK-2 cells, RNA interference-mediated silencing of AATF exacerbated whereas overexpression of the full-length AATF ameliorated mitochondrial dysfunction, accumulation of superoxide and peroxynitrite, lipid peroxidation, caspase-3 activation, and apoptotic death that were induced by IRI [1].
  • The present results suggest that the C5(+) phenotype is not associated with any genetic abnormality in the CHE1 locus, and BChE-specific activity is enhanced in the C5(+) variant [8].
  • Recently the demonstration that de-epidermized dermis (DED) has all the characteristics of an excellent dermal substitute into which various types of cells can be introduced and made to develop, opens exciting new possibilities of research in the field of wound healing and tissue engineering [9].

Anatomical context of AATF

  • By culturing embryoid bodies on dead, deepidermized human dermis (DED) we showed that epidermal basement membrane did not induce beta(1)-null ES cells to undergo keratinocyte differentiation and did not stimulate the differentiation of wild-type ES cells [3].
  • Contrary to this, both AGC and AC were found to be present in significant amounts in an air-exposed model using de-epidermized dermis (DED) as a substrate (in which, as judged from morphologic criteria, the extent of keratinocyte stratification is similar to that seen under the in vivo conditions) [10].
  • In fibroblast-free DED matrices normalization of epidermal differentiation was only achieved when the culture medium was supplemented by keratinocyte growth factor [11].
  • The epithelium was composed of gingival or vaginal keratinocytes seeded on a de-epidermized dermis (DED) and grown in submerged culture for 2 weeks [12].
  • These cells were expanded and applied to sterilized de-epidermized dermis (DED) to obtain a full-thickness TE oral mucosa [13].

Associations of AATF with chemical compounds

  • Irradiation of DED before incubation with glucose strongly enhanced induction of AGEs, corresponding to the effect of solar irradiation on AGEs observed in vivo [14].
  • Irrespective of the number of fibroblasts incorporated into DED, the expression of alpha(3), alpha(6), beta(1), and beta(4) integrin subunits was upregulated [11].
  • Horizontal migration of keratinocytes on the DED was assessed using a tetrazolium-blue (MTT) assay [13].
  • In the presence of reconstructed epidermis on top of DED the penetration rate of sucrose is about 100 times and that of NG 2 times lower, as compared to DED only, indicating that the stratum corneum of the cultured epidermis exhibits considerable barrier capacity [15].
  • They re-express them, however, when they are cultured in medium supplemented with delipidized [retinoic acid (RA)-depleted] serum or in air-exposed cultures using de-epidermized dermis (DED) as a substrate [16].

Analytical, diagnostic and therapeutic context of AATF

  • Biochemical dissection of the FADD death effector domain and functional replacement with a coiled-coil motif demonstrates that there is an obligatory FADD self-association via the DED during assembly of the death-inducing signaling complex [17].
  • CONCLUSIONS: Successful MDI/DED teaching followed by self-medication is feasible in the emergency setting, based on a simple protocol [18].
  • DESIGN: MDI arm within a single-center randomized clinical trial comparing bronchodilator administration by MDI with a delivery enhancement device (MDI/DED) vs delivery by wet nebulizer [18].
  • METHODS: By immunohistochemistry using a monoclonal antibody recognizing carboxymethyl lysine, an advanced glycation end-product (AGE) (first objective), and by incubating dead de-epidermized dermis (DED) with glucose to simulate ageing-induced glycation in a human dermal equivalent model (second objective) [14].
  • Keratinocytes of normal and pathological origin were expanded in submerged cell cultures and frozen keratinocytes from the resulting cell bank were subsequently used for seeding on DED [4].


  1. Apoptosis Antagonizing Transcription Factor Protects Renal Tubule Cells against Oxidative Damage and Apoptosis Induced by Ischemia-Reperfusion. Xie, J., Guo, Q. J. Am. Soc. Nephrol. (2006) [Pubmed]
  2. Life and death in paradise. Gozani, O., Boyce, M., Yoo, L., Karuman, P., Yuan, J. Nat. Cell Biol. (2002) [Pubmed]
  3. Dermal fibroblast-derived growth factors restore the ability of beta(1) integrin-deficient embryonal stem cells to differentiate into keratinocytes. Bagutti, C., Hutter, C., Chiquet-Ehrismann, R., Fässler, R., Watt, F.M. Dev. Biol. (2001) [Pubmed]
  4. Modified epidermal lipid composition in air-exposed culture of non-bullous congenital ichthyotic erythroderma (NBCIE) keratinocytes. Haftek, M., Berlioz, C., Amsellem, C., Martini, M.C., Thivolet, J., Schmitt, D. Arch. Dermatol. Res. (1993) [Pubmed]
  5. TSG101 interacts with apoptosis-antagonizing transcription factor and enhances androgen receptor-mediated transcription by promoting its monoubiquitination. Burgdorf, S., Leister, P., Scheidtmann, K.H. J. Biol. Chem. (2004) [Pubmed]
  6. Identification and characterization of DEDD2, a death effector domain-containing protein. Roth, W., Stenner-Liewen, F., Pawlowski, K., Godzik, A., Reed, J.C. J. Biol. Chem. (2002) [Pubmed]
  7. AATF, a novel transcription factor that interacts with Dlk/ZIP kinase and interferes with apoptosis. Page, G., Lödige, I., Kögel, D., Scheidtmann, K.H. FEBS Lett. (1999) [Pubmed]
  8. Genetic and immunological analyses of patients with increased serum butyrylcholinesterase activity and its C5 variant form. Akizuki, S., Ohnishi, A., Kotani, K., Sudo, K. Clin. Chem. Lab. Med. (2004) [Pubmed]
  9. Other uses of homologous skin grafts and skin bank bioproducts. Fimiani, M., Pianigiani, E., Di Simplicio, F.C., Sbano, P., Cuccia, A., Pompella, G., De Aloe, G., Petraglia, F. Clin. Dermatol. (2005) [Pubmed]
  10. Lipid composition of cultured human keratinocytes in relation to their differentiation. Ponec, M., Weerheim, A., Kempenaar, J., Mommaas, A.M., Nugteren, D.H. J. Lipid Res. (1988) [Pubmed]
  11. Crucial role of fibroblasts in regulating epidermal morphogenesis. El Ghalbzouri, A., Lamme, E., Ponec, M. Cell Tissue Res. (2002) [Pubmed]
  12. In vitro reconstructed mucosa-integrating Langerhans' cells. Sivard, P., Dezutter-Dambuyant, C., Kanitakis, J., Mosnier, J.F., Hamzeh, H., Bechetoille, N., Berthier, O., Sabido, O., Schmitt, D., Genin, C., Misery, L. Exp. Dermatol. (2003) [Pubmed]
  13. Tissue-engineered buccal mucosa for substitution urethroplasty. Bhargava, S., Chapple, C.R., Bullock, A.J., Layton, C., MacNeil, S. BJU international. (2004) [Pubmed]
  14. Glycation during human dermal intrinsic and actinic ageing: an in vivo and in vitro model study. Jeanmaire, C., Danoux, L., Pauly, G. Br. J. Dermatol. (2001) [Pubmed]
  15. Nitroglycerin and sucrose permeability as quality markers for reconstructed human epidermis. Ponec, M., Wauben-Penris, P.J., Burger, A., Kempenaar, J., Boddé, H.E. Skin Pharmacol. (1990) [Pubmed]
  16. Acylceramides and lanosterol-lipid markers of terminal differentiation in cultured human keratinocytes: modulating effect of retinoic acid. Brod, J., Bavelier, E., Justine, P., Weerheim, A., Ponec, M. In Vitro Cell. Dev. Biol. (1991) [Pubmed]
  17. FADD self-association is required for stable interaction with an activated death receptor. Sandu, C., Morisawa, G., Wegorzewska, I., Huang, T., Arechiga, A.F., Hill, J.M., Kim, T., Walsh, C.M., Werner, M.H. Cell Death Differ. (2006) [Pubmed]
  18. Teaching time for metered-dose inhalers in the emergency setting. Numata, Y., Bourbeau, J., Ernst, P., Duquette, G., Schwartzman, K. Chest (2002) [Pubmed]
WikiGenes - Universities