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Inactivation of glyceraldehyde-3-phosphate dehydrogenase by the dopamine metabolite, 3,4-dihydroxyphenylacetaldehyde
| Content Provider | Scilit |
|---|---|
| Author | Vanle, Brigitte C. Florang, Virginia R. Murry, Daryl J. Aguirre, Arturo L. Doorn, Jonathan A. |
| Copyright Year | 2017 |
| Description | Journal: Biochemical and Biophysical Research Communications 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. 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. 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. The mechanism by which DOPAL modifies GAPDH can serve as a mechanistic explanation to the pathological events in Parkinson's Disease. |
| Related Links | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5746426/pdf |
| Ending Page | 281 |
| Page Count | 7 |
| Starting Page | 275 |
| ISSN | 0006291X |
| e-ISSN | 10902104 |
| DOI | 10.1016/j.bbrc.2017.08.067 |
| Journal | Biochemical and Biophysical Research Communications |
| Issue Number | 2 |
| Volume Number | 492 |
| Language | English |
| Publisher | Elsevier BV |
| Publisher Date | 2017-10-01 |
| Access Restriction | Open |
| Subject Keyword | Journal: Biochemical and Biophysical Research Communications Biochemistry and Molecular Biology 3,4-dihydroxyphenylacetaldehyde Biogenic Aldehyde Glyceraldehyde-3-phosphate Dehydrogenase Parkinson's Disease |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Molecular Biology Biochemistry Biophysics |
