KEGG   DISEASE: Mitochondrial trifunctional protein deficiency
Entry
H01352                      Disease                                

Name
Mitochondrial trifunctional protein deficiency
  Subgroup
LCHAD deficiency [DS:H00489]
LCKAT deficiency
  Supergrp
Disorders of mitochondrial fatty-acid oxidation [DS:H00525]
Secondary hyperammonemia [DS:H01400]
Mitochondrial disease [DS:H01427]
Description
Mitochondrial trifunctional protein (TFP) deficiency is a rare autosomal recessive disorder that is caused by mutations in HADHA and HADHB. TFP is a multienzyme complex of the fatty acid beta-oxidation cycle. Human TFP is an octamer composed of four alpha-subunits harboring long-chain enoyl-CoA hydratase and long-chain L-3-hydroxyacyl-CoA dehydrogenase (LCHAD) and four beta-subunits encoding long-chain 3-ketoacyl-CoA thiolase (LCKAT). This disease includes a lethal neonatal phenotype with cardiomyopathy and Reye-like syndrome, an infantile hepatic phenotype with recurrent hypoketotic hypoglycemia, and a childhood or adolescent-onset neuromyopathic phenotype with peripheral neuropathy and recurrent rhabdomyolysis.
Category
Inherited metabolic disease; Mitochondrial disease
Brite
Human diseases [BR:br08402]
 Congenital disorders of metabolism
  Mitochondrial diseases
   H01352  Mitochondrial trifunctional protein deficiency
Human diseases in ICD-11 classification [BR:br08403]
 05 Endocrine, nutritional or metabolic diseases
  Metabolic disorders
   Inborn errors of metabolism
    5C52  Inborn errors of lipid metabolism
     H01352  Mitochondrial trifunctional protein deficiency
Pathway
hsa00071  Fatty acid degradation
hsa01212  Fatty acid metabolism
Network
  Element
N00766  HADHB deficiency in beta-oxidation
N00775  HADHA deficiency in beta-oxidation
Gene
HADHA [HSA:3030] [KO:K07515]
HADHB [HSA:3032] [KO:K07509]
Other DBs
ICD-11: 5C52.01
ICD-10: E71.3
MeSH: C566945
OMIM: 609015 609016
Reference
  Authors
Spiekerkoetter U, Khuchua Z, Yue Z, Bennett MJ, Strauss AW
  Title
General mitochondrial trifunctional protein (TFP) deficiency as a result of either alpha- or beta-subunit mutations exhibits similar phenotypes because mutations in either subunit alter TFP complex expression and subunit turnover.
  Journal
Pediatr Res 55:190-6 (2004)
DOI:10.1203/01.PDR.0000103931.80055.06
Reference
  Authors
Jones PM, Butt Y, Bennett MJ
  Title
Accumulation of 3-hydroxy-fatty acids in the culture medium of long-chain L-3-hydroxyacyl CoA dehydrogenase (LCHAD) and mitochondrial trifunctional protein-deficient skin fibroblasts: implications for medium chain triglyceride dietary treatment of LCHAD deficiency.
  Journal
Pediatr Res 53:783-7 (2003)
DOI:10.1203/01.PDR.0000059748.67987.1F
Reference
  Authors
Liewluck T, Mundi MS, Mauermann ML
  Title
Mitochondrial trifunctional protein deficiency: a rare cause of adult-onset rhabdomyolysis.
  Journal
Muscle Nerve 48:989-91 (2013)
DOI:10.1002/mus.23959
Reference
PMID:9739053
  Authors
Ibdah JA, Tein I, Dionisi-Vici C, Bennett MJ, IJlst L, Gibson B, Wanders RJ, Strauss AW
  Title
Mild trifunctional protein deficiency is associated with progressive neuropathy and myopathy and suggests a novel genotype-phenotype correlation.
  Journal
J Clin Invest 102:1193-9 (1998)
DOI:10.1172/JCI2091
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