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Thymidine phosphorylase gene mutations in MNGIE, a human mitochondrial disorder

I Nishino1, A Spinazzola, M Hirano

  • 1Columbia University College of Physicians and Surgeons, Department of Neurology, 630 West 168 Street, P & S 4-443, New York, NY 10032, USA.

Science (New York, N.Y.)
|January 29, 1999
PubMed

Insights

Mitochondrial neurogastrointestinal encephalomyopathy (MNGIE) is caused by thymidine phosphorylase (TP) gene mutations, leading to mitochondrial DNA deletions. This research identifies loss-of-function TP mutations as the cause of MNGIE.

Area of Science:

  • Genetics
  • Molecular Biology
  • Neuroscience

Background:

  • Mitochondrial neurogastrointestinal encephalomyopathy (MNGIE) is a rare, autosomal recessive disorder.
  • It is characterized by multiple deletions in skeletal muscle mitochondrial DNA (mtDNA).
  • The underlying cause was previously thought to be a defect in nuclear-mitochondrial genome communication.

Purpose of the Study:

  • To investigate the genetic basis of MNGIE.
  • To identify the specific gene mutations responsible for the disease.
  • To elucidate the pathogenic mechanism linking nuclear gene defects to mtDNA instability.

Main Methods:

  • Genetic analysis of 12 MNGIE probands.
  • Mutation screening of the thymidine phosphorylase (TP) gene.
  • Assay of TP enzyme activity in patient leukocytes.

Main Results:

  • Identified homozygous or compound-heterozygous mutations in the thymidine phosphorylase (TP) gene in all MNGIE patients.
  • TP gene mutations were located on chromosome 22q13.32-qter.
  • Leukocyte TP activity in MNGIE patients was significantly reduced (less than 5% of controls).

Conclusions:

  • Loss-of-function mutations in the thymidine phosphorylase (TP) gene cause MNGIE.
  • The disease mechanism likely involves impaired thymidine metabolism, affecting mtDNA replication or maintenance.
  • This finding establishes a direct link between nuclear gene defects and mitochondrial DNA integrity in MNGIE.

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