Monoamine oxidase (MAO) metabolizes cytosolic dopamine (DA), thereby limiting auto-oxidation, but is also thought to generate cytosolic hydrogen peroxide (H2O2). We show that MAO metabolism of DA does not increase cytosolic H2O2 but leads to mitochondrial electron transport chain (ETC) activity. This is dependent upon MAO anchoring to the outer mitochondrial membrane and shuttling electrons through the intermembrane space to support the bioenergetic demands of phasic DA release.
Bibliographical noteFunding Information:
This study was supported by grants from the JPB Foundation, the IDP Foundation, the Michael J. Fox Foundation and the NIH (NS047085) to D.J.S.; an NIH grant (NS076054) to D.K.; an NIH grant (DA039253) and a Northwestern Memorial Foundation grant to S.M.G.; the Boyd and Elsi Welin Professorship and Tsai Family Fund to J.C.S.; and NIH grants U01NS103522, U01NS090604 and DPMH107056 to L.T. The authors thank the Northwestern Center for Advanced Microscopy (supported by National Cancer Center Support Grant P30 CA060553) for assistance.
PubMed: MeSH publication types
- Journal Article
- Research Support, N.I.H., Extramural
- Research Support, Non-U.S. Gov't