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Iron and Lactoferrin Levels Remain Unchanged in Parkin Deficient Mouse Brains: Implications for Parkinson’s Disease Etiology

  • Author(s): Baker, Hanan
  • Advisor(s): Torres, Jorge
  • et al.
Abstract

Parkinson’s disease is a devastating neurodegenerative disease in which loss of dopaminergic neurons in the substantia nigra pars compacta leads to a variety of motor and non-motor deficits. Mutations in the Park2 or parkin gene have been implicated in familial forms of Parkinson’s disease. Parkin is an E3 ubiquitin ligase that plays a role in mitophagy, the degradation of damaged mitochondria. Defects in parkin are thought to impair mitophagy, leading to mitochondrial dysfunction and an increase in oxidative stress. Although best known for its participation in the regulation of mitochondrial dynamics, parkin has also been known to play a role in cell cycle progression. We had previously found that parkin binds to and selectively ubiquitinates lactoferrin in human cells. Lactoferrin is an iron binding protein predominantly found in milk and implicated in several beneficial processes. In this study I further evaluated this novel interaction in a parkin knockout mouse model. I found that parkin does indeed bind lactoferrin in mouse brains, however, knockout of parkin does not cause any change in lactoferrin or iron levels.

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