Changes in mitochondrial complex I activity and coenzyme Q binding site in Leber's hereditary optic neuropathy (LHON)

Mol Aspects Med. 1997:18 Suppl:S263-7. doi: 10.1016/s0098-2997(97)00028-9.

Abstract

The complex I function in sub-mitochondrial particles was studied in platelets from patients and healthy carriers with 11778/ND4 or 3460/ND1 mtDNA point mutations associated with LHON. Both 11778/ND4 and 3460/ND1 mutations induced rotenone resistance and 11778/ND4 showed an increased K(m) for ubiquinol-2 with respect to the control group. It was concluded that even with different pathogenic mechanisms both mutations affect the quinone binding site of complex I.

Publication types

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

MeSH terms

  • Binding Sites
  • Blood Platelets / metabolism*
  • DNA, Mitochondrial / genetics*
  • Humans
  • Kinetics
  • Mitochondria / metabolism*
  • NAD(P)H Dehydrogenase (Quinone) / metabolism*
  • Optic Atrophies, Hereditary / metabolism*
  • Point Mutation
  • Rotenone / pharmacology
  • Ubiquinone / blood*
  • Uncoupling Agents / pharmacology

Substances

  • DNA, Mitochondrial
  • Uncoupling Agents
  • Rotenone
  • Ubiquinone
  • NAD(P)H Dehydrogenase (Quinone)
  • Ubiquinone Q2