TY - JOUR
T1 - Defective Mitochondrial Dynamics Underlie Manganese-Induced Neurotoxicity
AU - Morcillo, Patricia
AU - Cordero, Hector
AU - Ijomone, Omamuyovwi M.
AU - Ayodele, Akinyemi
AU - Bornhorst, Julia
AU - Gunther, Leslie
AU - Macaluso, Frank P.
AU - Bowman, Aaron B.
AU - Aschner, Michael
N1 - Funding Information:
We are grateful to Vera DesMarais, Peng Guo, Andrea Briceno, Hillary Guzik, Timothy Mendez and Xheni Nishku from the Analytical Imaging Facility, Albert Einstein College of Medicine, for the invaluable help acquiring the images, the technical assistance, and their critical comments. We thank Xueliang Du for the technical support with the Seahorse measurements. Lastly, we would like to acknowledge Dr. Estela Area Gomez (Columbia University, NY) for critical reading of the manuscript. Customized scripts generated for this study are available from the corresponding author on request.
Publisher Copyright:
© 2021, The Author(s), under exclusive licence to Springer Science+Business Media, LLC part of Springer Nature.
PY - 2021/7
Y1 - 2021/7
N2 - Perturbations in mitochondrial dynamics have been observed in most neurodegenerative diseases. Here, we focus on manganese (Mn)-induced Parkinsonism-like neurodegeneration, a disorder associated with the preferential of Mn in the basal ganglia where the mitochondria are considered an early target. Despite the extensive characterization of the clinical presentation of manganism, the mechanism by which Mn mediated mitochondrial toxicity is unclear. In this study we hypothesized whether Mn exposure alters mitochondrial activity, including axonal transport of mitochondria and mitochondrial dynamics, morphology, and network. Using primary neuron cultures exposed to 100 μM Mn (which is considered the threshold of Mn toxicity in vitro) and intraperitoneal injections of MnCl2 (25mg/kg) in rat, we observed that Mn increased mitochondrial fission mediated by phosphorylation of dynamin-related protein-1 at serine 616 (p-s616-DRP1) and decreased mitochondrial fusion proteins (MFN1 and MFN2) leading to mitochondrial fragmentation, defects in mitochondrial respiratory capacity, and mitochondrial ultrastructural damage in vivo and in vitro. Furthermore, Mn exposure impaired mitochondrial trafficking by decreasing dynactin (DCTN1) and kinesin-1 (KIF5B) motor proteins and increasing destabilization of the cytoskeleton at protein and gene levels. In addition, mitochondrial communication may also be altered by Mn exposure, increasing the length of nanotunnels to reach out distal mitochondria. These findings revealed an unrecognized role of Mn in dysregulation of mitochondrial dynamics providing a potential explanation of early hallmarks of the disorder, as well as a possible common pathway with neurological disorders arising upon chronic Mn exposure.
AB - Perturbations in mitochondrial dynamics have been observed in most neurodegenerative diseases. Here, we focus on manganese (Mn)-induced Parkinsonism-like neurodegeneration, a disorder associated with the preferential of Mn in the basal ganglia where the mitochondria are considered an early target. Despite the extensive characterization of the clinical presentation of manganism, the mechanism by which Mn mediated mitochondrial toxicity is unclear. In this study we hypothesized whether Mn exposure alters mitochondrial activity, including axonal transport of mitochondria and mitochondrial dynamics, morphology, and network. Using primary neuron cultures exposed to 100 μM Mn (which is considered the threshold of Mn toxicity in vitro) and intraperitoneal injections of MnCl2 (25mg/kg) in rat, we observed that Mn increased mitochondrial fission mediated by phosphorylation of dynamin-related protein-1 at serine 616 (p-s616-DRP1) and decreased mitochondrial fusion proteins (MFN1 and MFN2) leading to mitochondrial fragmentation, defects in mitochondrial respiratory capacity, and mitochondrial ultrastructural damage in vivo and in vitro. Furthermore, Mn exposure impaired mitochondrial trafficking by decreasing dynactin (DCTN1) and kinesin-1 (KIF5B) motor proteins and increasing destabilization of the cytoskeleton at protein and gene levels. In addition, mitochondrial communication may also be altered by Mn exposure, increasing the length of nanotunnels to reach out distal mitochondria. These findings revealed an unrecognized role of Mn in dysregulation of mitochondrial dynamics providing a potential explanation of early hallmarks of the disorder, as well as a possible common pathway with neurological disorders arising upon chronic Mn exposure.
KW - Cytoskeleton
KW - Manganese
KW - Mitochondrial dynamics
KW - Neuron
KW - Striatum
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U2 - 10.1007/s12035-021-02341-w
DO - 10.1007/s12035-021-02341-w
M3 - Article
C2 - 33666854
AN - SCOPUS:85102203500
SN - 0893-7648
VL - 58
SP - 3270
EP - 3289
JO - Molecular Neurobiology
JF - Molecular Neurobiology
IS - 7
ER -