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

Acads  -  acyl-Coenzyme A dehydrogenase, short chain

Mus musculus

Synonyms: AI196007, Bcd-1, Bcd1, Butyryl-CoA dehydrogenase, Hdlq8, ...
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 Acads

  • These mice have undetectable SCAD activity, severe organic aciduria; excreting ethylmalonic and methylsuccinic acids and N-butyrylglycine, and develop a fatty liver upon fasting or dietary fat challenge [1].
  • We have used recombinant adeno-associated virus (rAAV) vectors expressing short-chain acyl-CoA dehydrogenase (SCAD) to correct the accumulation of fatty acyl-CoA intermediates in deficient cell lines [2].
  • The rAAV-SCAD vector was then packaged into either rAAV serotype 1 or 2 capsids and injected intramuscularly into SCAD-deficient mice [2].
  • Hydrodynamic administration of naked DNA was investigated as a method for in vivo expression of variant proteins involved in metabolic diseases, using short-chain acyl-CoA dehydrogenase (SCAD) deficient mice (BALB/cByJ) as a model [3].
  • In summary, we conclude that BALB/cByJ mice with SCAD deficiency, but with a functional urea cycle, might have an adequate adaptive mechanism to adjust to an excessive acyl-CoA load without hyperammonemia at the cerebral level [4].

Psychiatry related information on Acads

  • Here we show that a deficiency in short-chain acyl-coenzyme A dehydrogenase (encoded by Acads) in mice causes a marked slowing in theta frequency during paradoxical sleep only [5].

High impact information on Acads

  • Microarray analysis of gene expression in mice with mutations in Acads indicates overexpression of Glo1 (encoding glyoxylase 1), a gene involved in the detoxification of metabolic by-products [5].
  • We found Acads expression in brain regions involved in theta generation, notably the hippocampus [5].
  • In three transgenic lines produced on the SCAD-deficient background, recombinant SCAD activity and antigen in liver mitochondria were found up to 7-fold of normal control values [6].
  • We report the therapeutic effects of liver-specific expression of a short-chain acyl-CoA dehydrogenase (SCAD) transgene in the SCAD-deficient mouse model [6].
  • As predicted, on either AIN76A or wheat bran diet, the Scad mutation almost completely eliminated apoptosis in the flat mucosa of the proximal colon and reduced apoptosis by 50% in the distal colon compared with littermates that were wild-type for Scad [7].

Biological context of Acads

  • The 5' region of the mouse Acads gene lacks a TATA box or a CAAT box, is GC rich, and also lacks any similarity to the related gene, medium-chain acyl-CoA dehydrogenase [8].
  • First, during 10-day exposure to a macronutrient self-selection diet, Acads -/- mice consumed proportionately less fat and more carbohydrate than Acads +/+ mice, yet total energy intake was similar between strains [9].
  • Acads gene deletion in BALB/cByJ mouse strain occurred after 1981 and is not present in BALB/cByJ-fld mutant mice [10].
  • Data from a three-point cross indicated that the null variant maps to the structural locus for the enzyme, Bcd-1, on chromosome 5 [11].
  • Genetics and ontogeny of butyryl CoA dehydrogenase in the mouse and linkage of Bcd-1 with Dao-1 [12].

Anatomical context of Acads

  • Scad+/+ mice maintained on a wheat bran-fiber-supplemented diet gained significantly more weight than mice maintained on AIN76A, but this was eliminated by the Scad mutation, demonstrating that uptake and metabolism of SCFAs in the gastrointestinal tract can be a significant energy source [7].
  • [9,10(n)-3H]- and [15,16(n)-3H]palmitate oxidations in J mouse fibroblasts were 96 and 35% of control, respectively, consistent with an isolated SCAD defect [13].
  • Acyl-CoA dehydrogenase activities were assayed in muscle and fibroblast mitochondria from BALB/cBy controls (Y) and SCAD-deficient J mice [13].
  • A tendency to a reduction in the level of butyrylcarnitine in blood was observed although only approximately 5% of the liver cells expressed the SCAD protein [3].

Associations of Acads with chemical compounds

  • It is postulated that the spf/Y (scad/scad) double-mutant may serve as a useful animal model to study the ammonia: fatty acyl CoA synergism [14].
  • In the present study we examined pathogen-free, SCAD deficient BALB/cByJ mice and control BALB/cBy mice for biochemical and tissue changes following fasting or salicylate challenge [15].

Other interactions of Acads

  • Breeding experiments were conducted to combine the X-linked sparse-fur (spf) mutation with ornithine transcarbamylase deficiency and the autosomal recessive deficiency of short-chain acyl CoA dehydrogenase (SCAD) in BALB/cByJ mice [14].

Analytical, diagnostic and therapeutic context of Acads

  • This study is the first to demonstrate the systemic correction of a fatty acid oxidation disorder with rAAV and the utility of MRS as a noninvasive method to monitor SCAD correction after in vivo gene therapy [2].
  • Radiolabeling and immunoprecipitation studies in J mouse fibroblasts revealed no SCAD synthesis, but normal MCAD synthesis [13].


  1. Short-chain acyl-coenzyme A dehydrogenase deficiency in mice. Wood, P.A., Amendt, B.A., Rhead, W.J., Millington, D.S., Inoue, F., Armstrong, D. Pediatr. Res. (1989) [Pubmed]
  2. Systemic correction of a fatty acid oxidation defect by intramuscular injection of a recombinant adeno-associated virus vector. Conlon, T.J., Walter, G., Owen, R., Cossette, T., Erger, K., Gutierrez, G., Goetzman, E., Matern, D., Vockley, J., Flotte, T.R. Hum. Gene Ther. (2006) [Pubmed]
  3. Expression of short-chain acyl-CoA dehydrogenase (SCAD) proteins in the liver of SCAD deficient mice after hydrodynamic gene transfer. Holm, D.A., Dagnaes-Hansen, F., Simonsen, H., Gregersen, N., Bolund, L., Jensen, T.G., Corydon, T.J. Mol. Genet. Metab. (2003) [Pubmed]
  4. Decompensation of hepatic and cerebral acyl-CoA metabolism in BALB/cByJ mice by chronic riboflavin deficiency: restoration by acetyl-L-carnitine. Rao, K.V., Qureshi, I.A. Can. J. Physiol. Pharmacol. (1997) [Pubmed]
  5. Deficiency in short-chain fatty acid beta-oxidation affects theta oscillations during sleep. Tafti, M., Petit, B., Chollet, D., Neidhart, E., de Bilbao, F., Kiss, J.Z., Wood, P.A., Franken, P. Nat. Genet. (2003) [Pubmed]
  6. Functional correction of short-chain acyl-CoA dehydrogenase deficiency in transgenic mice: implications for gene therapy of human mitochondrial enzyme deficiencies. Kelly, C.L., Rhead, W.J., Kutschke, W.K., Brix, A.E., Hamm, D.A., Pinkert, C.A., Lindsey, J.R., Wood, P.A. Hum. Mol. Genet. (1997) [Pubmed]
  7. Short-chain fatty acid metabolism, apoptosis, and Apc-initiated tumorigenesis in the mouse gastrointestinal mucosa. Augenlicht, L.H., Anthony, G.M., Church, T.L., Edelmann, W., Kucherlapati, R., Yang, K., Lipkin, M., Heerdt, B.G. Cancer Res. (1999) [Pubmed]
  8. Cloning and characterization of the mouse short-chain acyl-CoA dehydrogenase gene. Kelly, C.L., Wood, P.A. Mamm. Genome (1996) [Pubmed]
  9. Mice bearing Acads mutation display altered postingestive but not 5-s orosensory response to dietary fat. Smith Richards, B.K., Belton, B.N., York, B., Volaufova, J. Am. J. Physiol. Regul. Integr. Comp. Physiol. (2004) [Pubmed]
  10. Acads gene deletion in BALB/cByJ mouse strain occurred after 1981 and is not present in BALB/cByJ-fld mutant mice. Reue, K., Cohen, R.D. Mamm. Genome (1996) [Pubmed]
  11. Organic aciduria and butyryl CoA dehydrogenase deficiency in BALB/cByJ mice. Schiffer, S.P., Prochazka, M., Jezyk, P.F., Roderick, T.H., Yudkoff, M., Patterson, D.F. Biochem. Genet. (1989) [Pubmed]
  12. Genetics and ontogeny of butyryl CoA dehydrogenase in the mouse and linkage of Bcd-1 with Dao-1. Seeley, T.L., Holmes, R.S. Biochem. Genet. (1981) [Pubmed]
  13. Short-chain acyl-coenzyme A dehydrogenase activity, antigen, and biosynthesis are absent in the BALB/cByJ mouse. Amendt, B.A., Freneaux, E., Reece, C., Wood, P.A., Rhead, W.J. Pediatr. Res. (1992) [Pubmed]
  14. Breeding experiments to combine the X-linked sparse-fur (spf) mutation with the autosomal recessive BALB/cByJ strain: testing the biochemical phenotype of double-mutant mice as a model for ammonia: fatty acyl CoA synergism. Qureshi, I.A., Leblanc, D., Cyr, D., Giguère, R., Mitchell, G. Biochem. Biophys. Res. Commun. (1993) [Pubmed]
  15. Pathologic characterization of short-chain acyl-CoA dehydrogenase deficiency in BALB/cByJ mice. Armstrong, D.L., Masiowski, M.L., Wood, P.A. Am. J. Med. Genet. (1993) [Pubmed]
WikiGenes - Universities