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)
 

Links

 

Gene Review

Gcdh  -  glutaryl-Coenzyme A dehydrogenase

Mus musculus

Synonyms: 9030411L18, AI266902, D17825, GCD, Glutaryl-CoA dehydrogenase, mitochondrial
 
 
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 Gcdh

  • Subjecting the Gcdh-/- mice to a metabolic stress, which often precipitates an encephalopathic crisis and the development of dystonia in GA-I patients, failed to have any neurologic effect on the mice [1].
 

High impact information on Gcdh

 

Biological context of Gcdh

  • We hypothesize that the lack of similarity in regards to the neurologic phenotype and striatal pathology of GA-I patients, as compared with the Gcdh-/- mice, is due to intrinsic differences between the striata of mice and men [1].
  • Gcdh was mapped by backcross analysis to mouse chromosome 8 within a region that is homologous to a region of human chromosome 19, where the human gene was previously mapped [3].
  • The mouse Gcdh gene contains 11 exons and spans 7 kb of genomic DNA [3].
  • The mouse Gcdh cDNA is 1.75 kb long and contains an open reading frame of 438 amino acids [3].
  • Transfection studies mapped the mouse GCD promoter to a 500-bp region of DNA 5' of the translation start site [4].
 

Anatomical context of Gcdh

  • As cerebral concentrations of GA and 3-OH-GA have not yet been studied systematically, we investigated the tissue-specific distribution of these organic acids and glutarylcarnitine in brain, liver, skeletal and heart muscle of Gcdh-deficient mice as well as in hepatic Gcdh(-/-) mice and in C57Bl/6 mice following intraperitoneal loading [5].
  • In contrast, most 8-week-old Gcdh-/- mice survived on high lysine, but developed white matter lesions, reactive astrocytes and neuronal loss after 6 weeks [6].
  • High lysine alone resulted in vasogenic oedema and blood-brain barrier breakdown within the striatum, associated with serum and tissue GA accumulation, neuronal loss, haemorrhage, paralysis, seizures and death in 75% of 4-week-old Gcdh-/- mice after 3-12 days [6].
  • Statistical analyses of the gingival tissues in this region in both strains showed that, with age, the length of the junctional epithelium (JED) increased, the depth of the gingival sulcus (GSD) did not change, and the height of the gingival crest (GCD) decreased [7].
 

Associations of Gcdh with chemical compounds

  • Concentrations of GA, 3-OH-GA and glutarylcarnitine were significantly elevated in all tissues of Gcdh(-/-) mice [5].
  • Thus, the Gcdh-/- mouse exposed to high protein or lysine may be a useful model of human GA-1 including developmentally dependent striatal vulnerability [6].
 

Other interactions of Gcdh

  • The genomic locus of Mem3 has been mapped to Chromosome (Chr) 8 near the D8Mit78 marker and the glutaryl CoA dehydrogenase (Gcdh) locus [8].
 

Analytical, diagnostic and therapeutic context of Gcdh

  • In contrast, cerebral concentrations of these organic acids remained low in hepatic Gcdh(-/-) mice and after intraperitoneal injection of GA and 3-OH-GA [5].
  • Western blot and RT/PCR analyses of mouse tissues demonstrated that GCD is ubiquitously expressed, with the highest levels of expression in liver and kidney, consistent with its role in amino acid oxidation [4].

References

  1. Biochemical, pathologic and behavioral analysis of a mouse model of glutaric acidemia type I. Koeller, D.M., Woontner, M., Crnic, L.S., Kleinschmidt-DeMasters, B., Stephens, J., Hunt, E.L., Goodman, S.I. Hum. Mol. Genet. (2002) [Pubmed]
  2. Bioenergetics in glutaryl-coenzyme A dehydrogenase deficiency: a role for glutaryl-coenzyme A. Sauer, S.W., Okun, J.G., Schwab, M.A., Crnic, L.R., Hoffmann, G.F., Goodman, S.I., Koeller, D.M., Kölker, S. J. Biol. Chem. (2005) [Pubmed]
  3. Cloning, structure, and chromosome localization of the mouse glutaryl-CoA dehydrogenase gene. Koeller, D.M., DiGiulio, K.A., Angeloni, S.V., Dowler, L.L., Frerman, F.E., White, R.A., Goodman, S.I. Genomics (1995) [Pubmed]
  4. Analysis of the expression of murine glutaryl-CoA dehydrogenase: in vitro and in vivo studies. Woontner, M., Crnic, L.S., Koeller, D.M. Mol. Genet. Metab. (2000) [Pubmed]
  5. Intracerebral accumulation of glutaric and 3-hydroxyglutaric acids secondary to limited flux across the blood-brain barrier constitute a biochemical risk factor for neurodegeneration in glutaryl-CoA dehydrogenase deficiency. Sauer, S.W., Okun, J.G., Fricker, G., Mahringer, A., Müller, I., Crnic, L.R., Mühlhausen, C., Hoffmann, G.F., Hörster, F., Goodman, S.I., Harding, C.O., Koeller, D.M., Kölker, S. J. Neurochem. (2006) [Pubmed]
  6. A diet-induced mouse model for glutaric aciduria type I. Zinnanti, W.J., Lazovic, J., Wolpert, E.B., Antonetti, D.A., Smith, M.B., Connor, J.R., Woontner, M., Goodman, S.I., Cheng, K.C. Brain (2006) [Pubmed]
  7. Age-related development of the long-junctional epithelium in the senescence-accelerated mouse. Sashima, M., Satoh, M., Suzuki, A. J. Dent. Res. (1991) [Pubmed]
  8. Genetic mapping and embryonic expression of a novel, maternally transcribed gene Mem3. Hwang, S., Benjamin, L.E., Oh, B., Rothstein, J.L., Ackerman, S.L., Beddington, R.S., Solter, D., Knowles, B.B. Mamm. Genome (1996) [Pubmed]
 
WikiGenes - Universities