Is prostaglandin E(2) a pathogenic factor in amyotrophic lateral sclerosis?

Ann Neurol. 2006 Jun;59(6):980-3. doi: 10.1002/ana.20847.

Abstract

Objective: To elucidate the role of cyclooxygenase-1 (Cox1) and prostaglandin E(2) in ALS neurodegeneration.

Methods: Mutation in superoxide dismutase-1 is a cause of the fatal paralytic disorder amyotrophic lateral sclerosis. Inhibition of cyclooxygenase-2 (Cox-2) in transgenic mice expressing an amyotrophic lateral sclerosis-linked superoxide dismutase-1 mutation led to the idea that prostaglandin E(2), the main synthetic product of Cox-2, is pathogenic in amyotrophic lateral sclerosis.

Results: Herein, we show by genetic intervention that prostaglandin E(2) in the spinal cord is mainly produced by Cox-1, and that ablation of Cox-1 fails to attenuate neurodegeneration.

Interpretation: The previously documented role of Cox-2 in ALS neurodegeneration in this particular mouse model occurs through a mechanism independent of prostaglandin E(2). Furthermore, plans to use selective Cox-1 inhibitors for neuroprotection in ALS are unlikely to be fruitful.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Amyotrophic Lateral Sclerosis / genetics
  • Amyotrophic Lateral Sclerosis / metabolism*
  • Animals
  • Cyclooxygenase 1 / genetics
  • Cyclooxygenase 1 / metabolism*
  • Cyclooxygenase 2 / metabolism
  • Dinoprostone / metabolism*
  • Disease Models, Animal
  • Mice
  • Mice, Knockout
  • Mice, Transgenic
  • Nerve Degeneration / metabolism*
  • Nerve Degeneration / pathology
  • Spinal Cord / metabolism*
  • Spinal Cord / pathology
  • Survival

Substances

  • Cyclooxygenase 1
  • Cyclooxygenase 2
  • Dinoprostone