Inactivation of glyceraldehyde-3-phosphate dehydrogenase by the dopamine metabolite, 3,4-dihydroxyphenylacetaldehyde

Brigitte C. Vanle, Virginia R. Florang, Daryl J. Murry, Arturo L. Aguirre, Jonathan A. Doorn

Research output: Contribution to journalArticlepeer-review

21 Scopus citations


Background The aldehyde metabolite of dopamine, 3,4-dihydroxyphenylacetaldehyde (DOPAL) is an endogenous neurotoxin implicated in Parkinson's Disease. Elucidating protein targets of DOPAL is essential in understanding it's pathology. The enzyme, glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a target of DOPAL. Methods GAPDH activity was measured via reduction of NAD+ cofactor (340 nm). Protein aggregation was assessed with SDS-PAGE methods and specific modification via chemical probes. Results Low micromolar levels of DOPAL caused extensive GAPDH aggregation and irreversibly inhibited enzyme activity. The inactivation of GAPDH was dependent on both the catechol and aldehyde moieties of DOPAL. It is suggested that Cys are modified and oxidized by DOPAL. Conclusions The mechanism by which DOPAL modifies GAPDH can serve as a mechanistic explanation to the pathological events in Parkinson's Disease.

Original languageEnglish (US)
Pages (from-to)275-281
Number of pages7
JournalBiochemical and Biophysical Research Communications
Issue number2
StatePublished - Oct 14 2017
Externally publishedYes


  • 3,4-Dihydroxyphenylacetaldehyde
  • Biogenic aldehyde
  • Glyceraldehyde-3-phosphate dehydrogenase
  • Parkinson's disease

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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