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Gene Review

Acadvl  -  acyl-Coenzyme A dehydrogenase, very long...

Mus musculus

Synonyms: MVLCAD, VLCAD, Very long-chain specific acyl-CoA dehydrogenase, mitochondrial, Vlcad
 
 
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Disease relevance of Acadvl

 

High impact information on Acadvl

  • Skin fibroblasts from 26 patients suspected of having a disorder of mitochondrial beta-oxidation were analyzed for VLCAD protein using immunoblotting, and 7 of them contained undetectable or trace levels of the enzyme [3].
  • The seven deficient fibroblast lines were characterized by measuring acyl-coenzyme A dehydrogenation activities, overall palmitic acid oxidation, and VLCAD protein synthesis using pulse-chase, further confirming the diagnosis of VLCAD deficiency [3].
  • Although many patients have been found to have very long-chain acyl-CoA dehydrogenase (VLCAD) deficiency, none have been documented with long-chain acyl-CoA dehydrogenase (LCAD) deficiency [4].
  • In order to understand the metabolic pathogenesis of long-chain fatty acid oxidation disorders, we generated mice with VLCAD deficiency (VLCAD(-/-)) and compared their pathologic and biochemical phenotypes of mice with LCAD deficiency (LCAD(-/-)) and wild-type mice [4].
  • Progeny with the combined LCAD(+/+)//VLCAD(+/-) genotype were over-represented in offspring from sires and dams heterozygous for both LCAD and VLCAD mutations [4].
 

Chemical compound and disease context of Acadvl

 

Biological context of Acadvl

 

Anatomical context of Acadvl

 

Associations of Acadvl with chemical compounds

  • Our results demonstrate different tissue-specific long-chain acylcarnitine profiles in response to various stressors, which may be of importance with respect to the heterogeneous clinical manifestations of VLCAD deficiency in humans [8].
  • In this paper we have used the VLCAD knockout mouse as a model to study changes in blood carnitine and acylcarnitine profiles under stress [2].
  • Palmitoyl-CoA dehydrogenase activity in skin fibroblasts from seven patients with unidentified defects of fatty acid oxidation was measured in the presence and absence of antibodies against medium-chain, long-chain, and very-long-chain acyl-CoA dehydrogenases (VLCAD) [9].
  • To study hepatic glucose production in FAO defects, we used the knockout mouse model of very long-chain acyl-CoA dehydrogenase (VLCAD) deficiency presenting with stress-induced hypoglycaemia [7].
 

Other interactions of Acadvl

  • In LCAD-/- and VLCAD-/- mice challenged with fasting and cold exposure, expression of fatty acid oxidation genes was elevated in liver, consistent with increased PPARalpha activity [10].
  • Mitochondrial beta-oxidation activity of fatty acids and expression of its related enzymes, including VLCAD, LCAD, and HCD, were down-regulated; on the other hand, peroxisomal beta-oxidation and its related enzymes, including AOX and BFE, were up-regulated [11].
  • It is a member of the acyl-CoA dehydrogenase (Acad or ACAD) gene family of enzymes, which also includes very-long-chain (VLCAD), medium-chain (MCAD), and short-chain (SCAD) acyl-CoA dehydrogenases [12].
  • We found that VLCAD-deficient hearts have microvesicular lipid accumulation, marked mitochondrial proliferation, and demonstrated facilitated induction of polymorphic ventricular tachycardia, without antecedent stress [13].
 

Analytical, diagnostic and therapeutic context of Acadvl

  • Altogether, these steps are important in the development of a durable gene therapy for VLCAD deficiency [5].
  • Transfected fibroblasts showed correction of the metabolic block as demonstrated by normalization of C14- and C16-acylcarnitine species in cell culture media and restoration of VLCAD activity in cells [5].

References

  1. Abnormal mitochondrial bioenergetics and heart rate dysfunction in mice lacking very-long-chain acyl-CoA dehydrogenase. Exil, V.J., Gardner, C.D., Rottman, J.N., Sims, H., Bartelds, B., Khuchua, Z., Sindhal, R., Ni, G., Strauss, A.W. Am. J. Physiol. Heart Circ. Physiol. (2006) [Pubmed]
  2. Changes in blood carnitine and acylcarnitine profiles of very long-chain acyl-CoA dehydrogenase-deficient mice subjected to stress. Spiekerkoetter, U., Tokunaga, C., Wendel, U., Mayatepek, E., Exil, V., Duran, M., Wijburg, F.A., Wanders, R.J., Strauss, A.W. Eur. J. Clin. Invest. (2004) [Pubmed]
  3. Purification of human very-long-chain acyl-coenzyme A dehydrogenase and characterization of its deficiency in seven patients. Aoyama, T., Souri, M., Ushikubo, S., Kamijo, T., Yamaguchi, S., Kelley, R.I., Rhead, W.J., Uetake, K., Tanaka, K., Hashimoto, T. J. Clin. Invest. (1995) [Pubmed]
  4. Gestational, pathologic and biochemical differences between very long-chain acyl-CoA dehydrogenase deficiency and long-chain acyl-CoA dehydrogenase deficiency in the mouse. Cox, K.B., Hamm, D.A., Millington, D.S., Matern, D., Vockley, J., Rinaldo, P., Pinkert, C.A., Rhead, W.J., Lindsey, J.R., Wood, P.A. Hum. Mol. Genet. (2001) [Pubmed]
  5. In vitro characterization and in vivo expression of human very-long chain acyl-CoA dehydrogenase. Merritt, J.L., Matern, D., Vockley, J., Daniels, J., Nguyen, T.V., Schowalter, D.B. Mol. Genet. Metab. (2006) [Pubmed]
  6. Assignment of the gene for very-long-chain acyl-CoA dehydrogenase (Acadvl) to mouse chromosome band 11B2-B5 by in situ hybridization. Orii, K.O., Saito-Ohara, F., Ikeuchi, T., Orii, T., Kondo, N., Aoyama, T., Hashimoto, T. Cytogenet. Cell Genet. (1997) [Pubmed]
  7. Evidence for Impaired Gluconeogenesis in Very Long-chain Acyl-CoA Dehydrogenase-deficient Mice. Spiekerkoetter, U., Ruiter, J., Tokunaga, C., Wendel, U., Mayatepek, E., Wijburg, F.A., Strauss, A.W., Wanders, R.J. Horm. Metab. Res. (2006) [Pubmed]
  8. Tissue carnitine homeostasis in very-long-chain acyl-CoA dehydrogenase-deficient mice. Spiekerkoetter, U., Tokunaga, C., Wendel, U., Mayatepek, E., Ijlst, L., Vaz, F.M., van Vlies, N., Overmars, H., Duran, M., Wijburg, F.A., Wanders, R.J., Strauss, A.W. Pediatr. Res. (2005) [Pubmed]
  9. A novel disease with deficiency of mitochondrial very-long-chain acyl-CoA dehydrogenase. Aoyama, T., Uchida, Y., Kelley, R.I., Marble, M., Hofman, K., Tonsgard, J.H., Rhead, W.J., Hashimoto, T. Biochem. Biophys. Res. Commun. (1993) [Pubmed]
  10. Differential induction of genes in liver and brown adipose tissue regulated by peroxisome proliferator-activated receptor-alpha during fasting and cold exposure in acyl-CoA dehydrogenase-deficient mice. Goetzman, E.S., Tian, L., Wood, P.A. Mol. Genet. Metab. (2005) [Pubmed]
  11. Retinoic acid receptor alpha dominant negative form causes steatohepatitis and liver tumors in transgenic mice. Yanagitani, A., Yamada, S., Yasui, S., Shimomura, T., Murai, R., Murawaki, Y., Hashiguchi, K., Kanbe, T., Saeki, T., Ichiba, M., Tanabe, Y., Yoshida, Y., Morino, S., Kurimasa, A., Usuda, N., Yamazaki, H., Kunisada, T., Ito, H., Murawaki, Y., Shiota, G. Hepatology (2004) [Pubmed]
  12. Structural characterization of the mouse long-chain acyl-CoA dehydrogenase gene and 5' regulatory region. Kurtz, D.M., Tolwani, R.J., Wood, P.A. Mamm. Genome (1998) [Pubmed]
  13. Very-long-chain acyl-coenzyme a dehydrogenase deficiency in mice. Exil, V.J., Roberts, R.L., Sims, H., McLaughlin, J.E., Malkin, R.A., Gardner, C.D., Ni, G., Rottman, J.N., Strauss, A.W. Circ. Res. (2003) [Pubmed]
 
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