Reinvestigation of trihydroxycholestanoic acidemia reveals a peroxisome biogenesis disorder

Neurology. 2004 Jun 8;62(11):2077-81. doi: 10.1212/01.wnl.0000127576.26352.d1.

Abstract

Objective: To determine the enzymatic defect in a patient with ataxia, dysarthric speech, dry skin, hypotonia, and absent reflexes. The patient was previously diagnosed with a presumed deficiency of trihydroxycholestanoyl-CoA oxidase.

Background: Peroxisomes harbor a variety of metabolic functions, including fatty acid beta-oxidation, etherphospholipid biosynthesis, phytanic acid alpha-oxidation, and L-pipecolic acid oxidation. This patient was previously described with an isolated peroxisomal beta-oxidation defect caused by a deficiency of the enzyme trihydroxycholestanoyl-CoA oxidase. This was based on the pattern of accumulating metabolites.

Methods: Measurement of beta-oxidation enzymes, peroxisomal biochemical analysis in body fluids and cultured skin fibroblasts, and DNA analysis of the PEX12 gene were performed.

Results: An isolated beta-oxidation defect in this patient was excluded by measurement of the various beta-oxidation enzymes. The authors found that the patient had a peroxisome biogenesis disorder caused by mutations in the PEX12 gene, although all peroxisomal functions in cultured skin fibroblasts were normal.

Conclusions: The absence of clear peroxisomal abnormalities in the patient's fibroblasts, including a normal peroxisomal localization of catalase, implies that even when all peroxisomal functions in fibroblasts are normal, a peroxisome biogenesis disorder cannot be fully excluded, and further studies may be needed. In addition, the authors' findings imply that there is no longer evidence for the existence of trihydroxycholestanoyl-CoA oxidase deficiency as a distinct disease entity.

Publication types

  • Case Reports
  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Ataxia / enzymology
  • Ataxia / genetics
  • Catalase / analysis
  • Child, Preschool
  • Cholestanols / blood*
  • Consensus Sequence
  • DNA Mutational Analysis
  • Diagnostic Errors
  • Dysarthria / enzymology
  • Dysarthria / genetics
  • Erythrocytes / metabolism
  • Female
  • Fibroblasts / enzymology
  • Fibroblasts / metabolism
  • Fibroblasts / ultrastructure
  • Fungi / genetics
  • Humans
  • Intellectual Disability / enzymology
  • Intellectual Disability / genetics
  • Mammals / genetics
  • Membrane Proteins / deficiency*
  • Membrane Proteins / genetics
  • Molecular Sequence Data
  • Muscle Hypotonia / enzymology
  • Muscle Hypotonia / genetics
  • Oxidation-Reduction
  • Oxidoreductases / deficiency
  • Peroxisomes / metabolism*
  • Peroxisomes / physiology
  • Phytanic Acid / adverse effects
  • Phytanic Acid / blood
  • Sequence Alignment
  • Sequence Homology, Amino Acid

Substances

  • Cholestanols
  • Membrane Proteins
  • PEX12 protein, human
  • Phytanic Acid
  • 3,7,12-trihydroxycholestan-26-oic acid
  • Oxidoreductases
  • Catalase
  • trihydroxycholestanoyl-CoA oxidase