Stem cell-derived cranial and spinal motor neurons reveal proteostatic differences between ALS resistant and sensitive motor neurons

Author:

An Disi1,Fujiki Ryosuke2345,Iannitelli Dylan E1ORCID,Smerdon John W6,Maity Shuvadeep17ORCID,Rose Matthew F23589ORCID,Gelber Alon2310,Wanaselja Elizabeth K1,Yagudayeva Ilona1,Lee Joun Y23,Vogel Christine17ORCID,Wichterle Hynek6ORCID,Engle Elizabeth C234510,Mazzoni Esteban Orlando111ORCID

Affiliation:

1. Department of Biology, New York University, New York, United States

2. Department of Neurology, Boston Children’s Hospital, Boston, United States

3. FM Kirby Neurobiology Center, Boston Children’s Hospital, Boston, United States

4. Department of Neurology, Harvard Medical School, Boston, United States

5. Medical Genetics Training Program, Harvard Medical School, Boston, United States

6. Department of Physiology and Cellular Biophysics, Columbia University Medical Center, New York, United States

7. Center for Genomics and Systems Biology, New York University, New York, United States

8. Department of Pathology, Brigham and Women’s Hospital, Boston, United States

9. Department of Pathology, Boston Children’s Hospital, Boston, United States

10. Broad Institute of MIT and Harvard, Cambridge, United States

11. NYU Neuroscience Institute, NYU Langone Medical Center, New York, United States

Abstract

In amyotrophic lateral sclerosis (ALS) spinal motor neurons (SpMN) progressively degenerate while a subset of cranial motor neurons (CrMN) are spared until late stages of the disease. Using a rapid and efficient protocol to differentiate mouse embryonic stem cells (ESC) to SpMNs and CrMNs, we now report that ESC-derived CrMNs accumulate less human (h)SOD1 and insoluble p62 than SpMNs over time. ESC-derived CrMNs have higher proteasome activity to degrade misfolded proteins and are intrinsically more resistant to chemically-induced proteostatic stress than SpMNs. Chemical and genetic activation of the proteasome rescues SpMN sensitivity to proteostatic stress. In agreement, the hSOD1 G93A mouse model reveals that ALS-resistant CrMNs accumulate less insoluble hSOD1 and p62-containing inclusions than SpMNs. Primary-derived ALS-resistant CrMNs are also more resistant than SpMNs to proteostatic stress. Thus, an ESC-based platform has identified a superior capacity to maintain a healthy proteome as a possible mechanism to resist ALS-induced neurodegeneration.

Funder

Project ALS

Eunice Kennedy Shriver National Institute of Child Health and Human Development

New York State Department of Health

March of Dimes

National Institute of Neurological Disorders and Stroke

New York University

Japan Heart Foundation/Bayer Yakuhin Research Grant Abroad

National Institutes of Health

National Institute of General Medical Sciences

National Heart, Lung, and Blood Institute

Howard Hughes Medical Institute

Zegar Family Foundation Fund for Genomics Research at New York University

Publisher

eLife Sciences Publications, Ltd

Subject

General Immunology and Microbiology,General Biochemistry, Genetics and Molecular Biology,General Medicine,General Neuroscience

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