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Gene Review

ALDH3A2  -  aldehyde dehydrogenase 3 family, member A2

Homo sapiens

Synonyms: ALDH10, Aldehyde dehydrogenase 10, Aldehyde dehydrogenase family 3 member A2, FALDH, Fatty aldehyde dehydrogenase, ...
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Disease relevance of ALDH3A2


Psychiatry related information on ALDH3A2


High impact information on ALDH3A2


Chemical compound and disease context of ALDH3A2


Biological context of ALDH3A2


Anatomical context of ALDH3A2

  • We performed mutation analysis in probands or fetuses from 13 unrelated SLS families and identified seven novel ALDH3A2 mutations [13].
  • Although this gene is expressed in a variety of human tissues, the expression level of ALDH10 in the liver and skeletal muscle appears to be higher than that in other tissues examined [14].
  • To assess the role of FALDH in the detoxification of oxidized lipid species, we evaluated the production of reactive oxygen species in normal versus FALDH-overexpressing adipocytes [15].
  • Upon insulin injection, FALDH mRNA expression increased in rat liver and white adipose tissue and was impaired in two models of insulin-resistant mice, db/db and high fat diet mice [15].
  • Moreover, insulin treatment increases FALDH activity in hepatocytes, and expression of FALDH was augmented during adipocyte differentiation [15].

Associations of ALDH3A2 with chemical compounds


Other interactions of ALDH3A2


Analytical, diagnostic and therapeutic context of ALDH3A2

  • Our results demonstrate that SLS is caused by a strikingly heterogeneous group of mutations in the FALDH gene and provide a framework for understanding the genetic basis of SLS and the development of DNA-based diagnostic tests [23].
  • Isoelectric focusing analysis indicated that ALDH3 is hardly expressed in normal as well as patients' fibroblast cells, while ALDH10 expressed in the normal cells is diminished in the three patients' cells [24].
  • Differential centrifugation studies in fibroblasts indicated that this FALDH enzyme was largely particulate; soluble FALDH activity was normal in SLS cells [18].
  • By site-directed mutagenesis we have prepared the T269I and the D267E mutants and the D267E/T269I double mutant of Saccharomyces cerevisiae FALDH with the aim of investigating the role of these residues in the kinetics [25].
  • The current lack of treatment is an impetus to develop gene therapy strategies by introducing functional FALDH into defective cells [3].


  1. Polymorphisms of human aldehyde dehydrogenases. Consequences for drug metabolism and disease. Vasiliou, V., Pappa, A. Pharmacology (2000) [Pubmed]
  2. Mutations in a new cytochrome P450 gene in lamellar ichthyosis type 3. Lefèvre, C., Bouadjar, B., Ferrand, V., Tadini, G., Mégarbané, A., Lathrop, M., Prud'homme, J.F., Fischer, J. Hum. Mol. Genet. (2006) [Pubmed]
  3. Restoration of fatty aldehyde dehydrogenase deficiency in Sjögren-Larsson syndrome. Haug, S., Braun-Falco, M. Gene Ther. (2006) [Pubmed]
  4. A gene for familial juvenile nephronophthisis (recessive medullary cystic kidney disease) maps to chromosome 2p. Antignac, C., Arduy, C.H., Beckmann, J.S., Benessy, F., Gros, F., Medhioub, M., Hildebrandt, F., Dufier, J.L., Kleinknecht, C., Broyer, M. Nat. Genet. (1993) [Pubmed]
  5. Genomic organization and expression of the human fatty aldehyde dehydrogenase gene (FALDH). Rogers, G.R., Markova, N.G., De Laurenzi, V., Rizzo, W.B., Compton, J.G. Genomics (1997) [Pubmed]
  6. Mutational analysis of the NPHP4 gene in 250 patients with nephronophthisis. Hoefele, J., Sudbrak, R., Reinhardt, R., Lehrack, S., Hennig, S., Imm, A., Muerb, U., Utsch, B., Attanasio, M., O'Toole, J.F., Otto, E., Hildebrandt, F. Hum. Mutat. (2005) [Pubmed]
  7. Sjögren-Larsson syndrome is caused by mutations in the fatty aldehyde dehydrogenase gene. De Laurenzi, V., Rogers, G.R., Hamrock, D.J., Marekov, L.N., Steinert, P.M., Compton, J.G., Markova, N., Rizzo, W.B. Nat. Genet. (1996) [Pubmed]
  8. Sj??gren-Larsson syndrome: Molecular genetics and biochemical pathogenesis of fatty aldehyde dehydrogenase deficiency. Rizzo, W.B. Mol. Genet. Metab. (2007) [Pubmed]
  9. Effect of therapy on keratin polypeptide profiles of psoriatic epidermis. LeVine, M.J., McGilvray, N., Baden, H.P. Archives of dermatology. (1980) [Pubmed]
  10. High molecular compounds (polysaccharides and proanthocyanidins) from Hamamelis virginiana bark: influence on human skin keratinocyte proliferation and differentiation and influence on irritated skin. Deters, A., Dauer, A., Schnetz, E., Fartasch, M., Hensel, A. Phytochemistry (2001) [Pubmed]
  11. The hairless guinea-pig as a model for treatment of cumulative irritation in humans. Andersen, F., Hedegaard, K., Petersen, T.K., Bindslev-Jensen, C., Fullerton, A., Andersen, K.E. Skin research and technology : official journal of International Society for Bioengineering and the Skin (ISBS) [and] International Society for Digital Imaging of Skin (ISDIS) [and] International Society for Skin Imaging (ISSI). (2006) [Pubmed]
  12. Pre- and postnatal growth retardation, scaling skin, moderate mental retardation and quadrispasticity, hypospadias grade 2 and hydro-uretero nephrosis, postaxial polydactyly. A distinct MCA/MR syndrome? Fryns, J.P., Lagae, L., Rizzo, W.B. Clin. Dysmorphol. (1998) [Pubmed]
  13. Sjögren-Larsson syndrome: seven novel mutations in the fatty aldehyde dehydrogenase gene ALDH3A2. Carney, G., Wei, S., Rizzo, W.B. Hum. Mutat. (2004) [Pubmed]
  14. Human fatty aldehyde dehydrogenase gene (ALDH10): organization and tissue-dependent expression. Chang, C., Yoshida, A. Genomics (1997) [Pubmed]
  15. Fatty aldehyde dehydrogenase: potential role in oxidative stress protection and regulation of its gene expression by insulin. Demozay, D., Rocchi, S., Mas, J.C., Grillo, S., Pirola, L., Chavey, C., Van Obberghen, E. J. Biol. Chem. (2004) [Pubmed]
  16. Spectrum of mutations and sequence variants in the FALDH gene in patients with Sjögren-Larsson syndrome. Sillén, A., Anton-Lamprecht, I., Braun-Quentin, C., Kraus, C.S., Sayli, B.S., Ayuso, C., Jagell, S., Küster, W., Wadelius, C. Hum. Mutat. (1998) [Pubmed]
  17. Identification of fatty aldehyde dehydrogenase in the breakdown of phytol to phytanic acid. van den Brink, D.M., van Miert, J.N., Dacremont, G., Rontani, J.F., Jansen, G.A., Wanders, R.J. Mol. Genet. Metab. (2004) [Pubmed]
  18. Sjögren-Larsson syndrome. Deficient activity of the fatty aldehyde dehydrogenase component of fatty alcohol:NAD+ oxidoreductase in cultured fibroblasts. Rizzo, W.B., Craft, D.A. J. Clin. Invest. (1991) [Pubmed]
  19. Juvenile macular dystrophy associated with deficient activity of fatty aldehyde dehydrogenase in Sjögren-Larsson syndrome. Willemsen, M.A., Cruysberg, J.R., Rotteveel, J.J., Aandekerk, A.L., Van Domburg, P.H., Deutman, A.F. Am. J. Ophthalmol. (2000) [Pubmed]
  20. Adeno-associated virus vectors are able to restore fatty aldehyde dehydrogenase-deficiency. Implications for gene therapy in Sjogren-Larsson syndrome. Haug, S., Braun-Falco, M. Arch. Dermatol. Res. (2005) [Pubmed]
  21. Sjögren-Larsson syndrome. Gordon, N. Developmental medicine and child neurology (2007) [Pubmed]
  22. 5-Lipoxygenase inhibition: a new treatment strategy for Sjögren-Larsson syndrome. Willemsen, M.A., Rotteveel, J.J., Steijlen, P.M., Heerschap, A., Mayatepek, E. Neuropediatrics. (2000) [Pubmed]
  23. The molecular basis of Sjögren-Larsson syndrome: mutation analysis of the fatty aldehyde dehydrogenase gene. Rizzo, W.B., Carney, G., Lin, Z. Am. J. Hum. Genet. (1999) [Pubmed]
  24. Mutations associated with Sjögren-Larsson syndrome. Tsukamoto, N., Chang, C., Yoshida, A. Ann. Hum. Genet. (1997) [Pubmed]
  25. A double residue substitution in the coenzyme-binding site accounts for the different kinetic properties between yeast and human formaldehyde dehydrogenases. Fernández, M.R., Biosca, J.A., Torres, D., Crosas, B., Parés, X. J. Biol. Chem. (1999) [Pubmed]
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