Human Molecular Genetics, Vol 6, 1215-1224, Copyright © 1997 by Oxford University Press
KE Orii, T Aoyama, K Wakui, Y Fukushima, H Miyajima, S Yamaguchi, T Orii, N Kondo and T Hashimoto
Mitochondrial trifunctional protein (TP), an enzyme of beta-oxidation, is a
multienzyme complex composed of four molecules of the alpha- subunit
(HADHA) containing the enoyl-CoA hydratase and 3-hydroxyacyl- CoA
dehydrogenase domains and four molecules of the beta-subunit (HADHB)
containing the 3-ketoacyl-CoA thiolase domain. An inborn error of this
enzyme complex can cause sudden infant death syndrome, acute hepatic
encephalopathy or liver failure, skeletal myopathy, or hypertrophic
cardiomyopathy. TP deficiency is classified into two different biochemical
phenotypes: one represents the existence of both subunits and the lack of
only the 3-hydroxyacyl-CoA dehydrogenase activity and the other represents
the absence of both subunits and the lack of all three TP activities,
although their clinical features are similar. We have identified two
Japanese patients with this disorder. Three enzyme activities of TP were
undetectable in fibroblasts from these two patients. We detected two
mutations in the HADHB gene from two Japanese patients, an exonic single T
insertion which created a new cryptic 5' splice site and a G1331A
transition (R411 K). Patient 1 was a compound heterozygote, while patient 2
was a homozygote of a G1331A transition.
ARTICLES
Genomic and mutational analysis of the mitochondrial trifunctional protein beta-subunit (HADHB) gene in patients with trifunctional protein deficiency
Department of Pediatrics, Gifu University School of Medicine, Tsukasa- machi, Japan. kenjior-gif@umin.u-tokyo.ac.jp
CiteULike 
Connotea 
Del.icio.us What's this?
This article has been cited by other articles:
|
|
 |
|
  H.-D. Park, S. R. Kim, C.-S. Ki, S.-Y. Lee, Y. S. Chang, D.-K. Jin, and W. S. Park Two Novel HADHB Gene Mutations in a Korean Patient with Mitochondrial Trifunctional Protein Deficiency Ann. Clin. Lab. Sci., January 1, 2009; 39(4): 399 - 404. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 H.-J. Kao, C.-F. Cheng, Y.-H. Chen, S.-I. Hung, C.-C. Huang, D. Millington, T. Kikuchi, J.-Y. Wu, and Y.-T. Chen ENU mutagenesis identifies mice with cardiac fibrosis and hepatic steatosis caused by a mutation in the mitochondrial trifunctional protein {beta}-subunit Hum. Mol. Genet., December 15, 2006; 15(24): 3569 - 3577. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 A. M. Das, S. Illsinger, T. Lucke, H. Hartmann, J. P.N. Ruiter, U. Steuerwald, H. R. Waterham, M. Duran, and R. J.A. Wanders Isolated Mitochondrial Long-Chain Ketoacyl-CoA Thiolase Deficiency Resulting from Mutations in the HADHB Gene Clin. Chem., March 1, 2006; 52(3): 530 - 534. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 J. Marin-Garcia and M. J. Goldenthal Fatty acid metabolism in cardiac failure: biochemical, genetic and cellular analysis Cardiovasc Res, June 1, 2002; 54(3): 516 - 527. [Full Text] [PDF]
|
|
|
|
 |
|
 K. E. Orii, K. O. Orii, M. Souri, T. Orii, N. Kondo, T. Hashimoto, and T. Aoyama Genes for the Human Mitochondrial Trifunctional Protein alpha - and beta -Subunits Are Divergently Transcribed from a Common Promoter Region J. Biol. Chem., March 19, 1999; 274(12): 8077 - 8084. [Abstract] [Full Text] [PDF]
|
|