Lipidomic Analysis of α-Synuclein Neurotoxicity Identifies Stearoyl CoA Desaturase as a Target for Parkinson Treatment
In Parkinson’s disease (PD), α-synuclein (αS) pathologically impacts the brain, a highly lipid-rich organ. We investigated how alterations in αS or lipid/fatty acid homeostasis affect each other. Lipidomic profiling of human αS-expressing yeast revealed increases in oleic acid (OA, 18:1), diglycerid...
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| Published in | Molecular cell Vol. 73; no. 5; pp. 1001 - 1014.e8 |
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| Main Authors | , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
United States
Elsevier Inc
07.03.2019
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| Subjects | |
| Online Access | Get full text |
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| Abstract | In Parkinson’s disease (PD), α-synuclein (αS) pathologically impacts the brain, a highly lipid-rich organ. We investigated how alterations in αS or lipid/fatty acid homeostasis affect each other. Lipidomic profiling of human αS-expressing yeast revealed increases in oleic acid (OA, 18:1), diglycerides, and triglycerides. These findings were recapitulated in rodent and human neuronal models of αS dyshomeostasis (overexpression; patient-derived triplication or E46K mutation; E46K mice). Preventing lipid droplet formation or augmenting OA increased αS yeast toxicity; suppressing the OA-generating enzyme stearoyl-CoA-desaturase (SCD) was protective. Genetic or pharmacological SCD inhibition ameliorated toxicity in αS-overexpressing rat neurons. In a C. elegans model, SCD knockout prevented αS-induced dopaminergic degeneration. Conversely, we observed detrimental effects of OA on αS homeostasis: in human neural cells, excess OA caused αS inclusion formation, which was reversed by SCD inhibition. Thus, monounsaturated fatty acid metabolism is pivotal for αS-induced neurotoxicity, and inhibiting SCD represents a novel PD therapeutic approach.
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•αS impacts lipid homeostasis, triggering excess oleic acid (OA) and diglycerides (DG)•Triglycerides and lipid droplets protect against toxicity by sequestering OA and DG•Stearoyl-CoA desaturase (SCD) inhibition rescues αS toxicity and neuron degeneration•SCD inhibition decreases αS inclusions and increases αS multimerization and solubility
α-synuclein is an abundant nerve cell component that forms abnormal aggregates in Parkinson’s disease and other fatal brain disorders. No disease-modifying drugs are available. Here, we identify new drug targets in lipid pathways and describe how cellular lipid alterations drive α-synuclein toxicity. |
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| AbstractList | In Parkinson's disease (PD), α-synuclein (αS) pathologically impacts the brain, a highly lipid-rich organ. We investigated how alterations in αS or lipid/fatty acid homeostasis affect each other. Lipidomic profiling of human αS-expressing yeast revealed increases in oleic acid (OA, 18:1), diglycerides, and triglycerides. These findings were recapitulated in rodent and human neuronal models of αS dyshomeostasis (overexpression; patient-derived triplication or E46K mutation; E46K mice). Preventing lipid droplet formation or augmenting OA increased αS yeast toxicity; suppressing the OA-generating enzyme stearoyl-CoA-desaturase (SCD) was protective. Genetic or pharmacological SCD inhibition ameliorated toxicity in αS-overexpressing rat neurons. In a C. elegans model, SCD knockout prevented αS-induced dopaminergic degeneration. Conversely, we observed detrimental effects of OA on αS homeostasis: in human neural cells, excess OA caused αS inclusion formation, which was reversed by SCD inhibition. Thus, monounsaturated fatty acid metabolism is pivotal for αS-induced neurotoxicity, and inhibiting SCD represents a novel PD therapeutic approach. In Parkinson’s disease (PD), α-synuclein (αS) pathologically impacts the brain, a highly lipid-rich organ. We investigated how alterations in αS or lipid/fatty acid homeostasis affect each other. Lipidomic profiling of human αS-expressing yeast revealed increases in oleic acid (OA, 18:1), diglycerides, and triglycerides. These findings were recapitulated in rodent and human neuronal models of αS dyshomeostasis (overexpression; patient-derived triplication or E46K mutation; E46K mice). Preventing lipid droplet formation or augmenting OA increased αS yeast toxicity; suppressing the OA-generating enzyme stearoyl-CoA-desaturase (SCD) was protective. Genetic or pharmacological SCD inhibition ameliorated toxicity in αS-overexpressing rat neurons. In a C. elegans model, SCD knockout prevented αS-induced dopaminergic degeneration. Conversely, we observed detrimental effects of OA on αS homeostasis: in human neural cells, excess OA caused αS inclusion formation, which was reversed by SCD inhibition. Thus, monounsaturated fatty acid metabolism is pivotal for αS-induced neurotoxicity, and inhibiting SCD represents a novel PD therapeutic approach. [Display omitted] •αS impacts lipid homeostasis, triggering excess oleic acid (OA) and diglycerides (DG)•Triglycerides and lipid droplets protect against toxicity by sequestering OA and DG•Stearoyl-CoA desaturase (SCD) inhibition rescues αS toxicity and neuron degeneration•SCD inhibition decreases αS inclusions and increases αS multimerization and solubility α-synuclein is an abundant nerve cell component that forms abnormal aggregates in Parkinson’s disease and other fatal brain disorders. No disease-modifying drugs are available. Here, we identify new drug targets in lipid pathways and describe how cellular lipid alterations drive α-synuclein toxicity. In Parkinson's disease (PD), α-synuclein (αS) pathologically impacts the brain, a highly lipid-rich organ. We investigated how alterations in αS or lipid/fatty acid homeostasis affect each other. Lipidomic profiling of human αS-expressing yeast revealed increases in oleic acid (OA, 18:1), diglycerides, and triglycerides. These findings were recapitulated in rodent and human neuronal models of αS dyshomeostasis (overexpression; patient-derived triplication or E46K mutation; E46K mice). Preventing lipid droplet formation or augmenting OA increased αS yeast toxicity; suppressing the OA-generating enzyme stearoyl-CoA-desaturase (SCD) was protective. Genetic or pharmacological SCD inhibition ameliorated toxicity in αS-overexpressing rat neurons. In a C. elegans model, SCD knockout prevented αS-induced dopaminergic degeneration. Conversely, we observed detrimental effects of OA on αS homeostasis: in human neural cells, excess OA caused αS inclusion formation, which was reversed by SCD inhibition. Thus, monounsaturated fatty acid metabolism is pivotal for αS-induced neurotoxicity, and inhibiting SCD represents a novel PD therapeutic approach.In Parkinson's disease (PD), α-synuclein (αS) pathologically impacts the brain, a highly lipid-rich organ. We investigated how alterations in αS or lipid/fatty acid homeostasis affect each other. Lipidomic profiling of human αS-expressing yeast revealed increases in oleic acid (OA, 18:1), diglycerides, and triglycerides. These findings were recapitulated in rodent and human neuronal models of αS dyshomeostasis (overexpression; patient-derived triplication or E46K mutation; E46K mice). Preventing lipid droplet formation or augmenting OA increased αS yeast toxicity; suppressing the OA-generating enzyme stearoyl-CoA-desaturase (SCD) was protective. Genetic or pharmacological SCD inhibition ameliorated toxicity in αS-overexpressing rat neurons. In a C. elegans model, SCD knockout prevented αS-induced dopaminergic degeneration. Conversely, we observed detrimental effects of OA on αS homeostasis: in human neural cells, excess OA caused αS inclusion formation, which was reversed by SCD inhibition. Thus, monounsaturated fatty acid metabolism is pivotal for αS-induced neurotoxicity, and inhibiting SCD represents a novel PD therapeutic approach. In Parkinson’s disease (PD), α-Synuclein (αS) pathologically impacts the brain, a highly lipid-rich organ. We investigated how alterations in αS or lipid/fatty acid homeostasis affect each other. Lipidomic profiling of human αS-expressing yeast revealed increases in oleic acid (OA, 18:1), diglycerides and triglycerides. These findings were recapitulated in rodent and human neuronal models of αS dyshomeostasis (overexpression; patient-derived triplication or E46K mutation; E46K mice). Preventing lipid droplet formation or augmenting OA increased αS yeast toxicity; suppressing the OA-generating enzyme stearoyl-CoA-desaturase (SCD) was protective. Genetic or pharmacological SCD inhibition ameliorated toxicity in αS-overexpressing rat neurons. In a C. elegans model, SCD knockout prevented αS-induced dopaminergic degeneration. Conversely, we observed detrimental effects of OA on αS homeostasis: in human neural cells, excess OA caused αS inclusion formation, which was reversed by SCD inhibition. Thus, monounsaturated fatty acid metabolism is pivotal for αS-induced neurotoxicity, and inhibiting SCD represents a novel PD therapeutic approach. α-Synuclein is an abundant nerve cell component that forms abnormal aggregates in Parkinson’s disease and other fatal brain disorders. No disease-modifying drugs are available. Here, we identify new drug targets in lipid pathways and describe how cellular lipid alterations drive α-synuclein toxicity. |
| Author | Freyzon, Yelena Clish, Clary B. Barrasa, M. Inmaculada Lindquist, Susan Selkoe, Dennis Imberdis, Thibaut Baru, Valeriya Becuwe, Michel Srinivasan, Supriya Dettmer, Ulf Terry-Kantor, Elizabeth Landgraf, Dirk Newby, Gregory Ho, Gary P.H. Welte, Michael A. Jaenisch, Rudolf Walther, Tobias C. Kohlwein, Sepp D. Haque, Aftabul Farese, Robert V. Termine, Daniel Noble, Tallie Lou, Yali Soldner, Frank Sandoe, Jackson Hofbauer, Harald F. Nuber, Silke Ramalingam, Nagendran Pincus, David Kim, Tae-Eun Fanning, Saranna |
| AuthorAffiliation | 1 Ann Romney Center for Neurologic Diseases, Dept of Neurology, Brigham and Women’s Hospital and Harvard Medical School, Boston, MA 02115, USA 12 Mira Costa College, 1 Barnard Drive, Oceanside, California 92056, USA 7 Dept of Genetics, Harvard Medical School, 77 Avenue Louis Pasteur Boston, Massachusetts 02115, USA 5 Dept of Genetics and Complex Diseases, Harvard T. H. Chan School of Public Health, 655 Huntington Avenue, Boston, Massachusetts 02115, USA 8 HHMI, Dept of Genetics and Complex Diseases, Harvard T. H. Chan School of Public Health, 655 Huntington Avenue, Boston, Massachusetts 02115, USA 2 Whitehead Institute for Biomedical Research, Cambridge, MA 02142, USA 13 Dept of Biology, University of Rochester, Rochester, NY 14627, USA 11 The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California, USA 14 HHMI, Dept of Biology, MIT, Cambridge, MA 02139, USA 6 Dept of Cell Biology, Harvard Medical School, 240 Longwood Avenue Boston, Massachusetts 02115, USA 4 Broad Instit |
| AuthorAffiliation_xml | – name: 2 Whitehead Institute for Biomedical Research, Cambridge, MA 02142, USA – name: 7 Dept of Genetics, Harvard Medical School, 77 Avenue Louis Pasteur Boston, Massachusetts 02115, USA – name: 3 Dept of Biology, MIT, Cambridge, MA 02139, USA – name: 14 HHMI, Dept of Biology, MIT, Cambridge, MA 02139, USA – name: 10 Dept of Chemical Physiology and The Dorris Neuroscience Center, 1 Barnard Drive, Oceanside, California 92056, USA – name: 4 Broad Institute of MIT and Harvard, Cambridge, MA 02142, USA – name: 13 Dept of Biology, University of Rochester, Rochester, NY 14627, USA – name: 1 Ann Romney Center for Neurologic Diseases, Dept of Neurology, Brigham and Women’s Hospital and Harvard Medical School, Boston, MA 02115, USA – name: 6 Dept of Cell Biology, Harvard Medical School, 240 Longwood Avenue Boston, Massachusetts 02115, USA – name: 12 Mira Costa College, 1 Barnard Drive, Oceanside, California 92056, USA – name: 9 Institute of Molecular Biosciences, BioTechMed-Graz, University of Graz, Austria – name: 11 The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California, USA – name: 8 HHMI, Dept of Genetics and Complex Diseases, Harvard T. H. Chan School of Public Health, 655 Huntington Avenue, Boston, Massachusetts 02115, USA – name: 5 Dept of Genetics and Complex Diseases, Harvard T. H. Chan School of Public Health, 655 Huntington Avenue, Boston, Massachusetts 02115, USA |
| Author_xml | – sequence: 1 givenname: Saranna surname: Fanning fullname: Fanning, Saranna organization: Ann Romney Center for Neurologic Diseases, Department of Neurology, Brigham and Women’s Hospital and Harvard Medical School, Boston, MA 02115, USA – sequence: 2 givenname: Aftabul surname: Haque fullname: Haque, Aftabul organization: Whitehead Institute for Biomedical Research, Cambridge, MA 02142, USA – sequence: 3 givenname: Thibaut surname: Imberdis fullname: Imberdis, Thibaut organization: Ann Romney Center for Neurologic Diseases, Department of Neurology, Brigham and Women’s Hospital and Harvard Medical School, Boston, MA 02115, USA – sequence: 4 givenname: Valeriya surname: Baru fullname: Baru, Valeriya organization: Whitehead Institute for Biomedical Research, Cambridge, MA 02142, USA – sequence: 5 givenname: M. Inmaculada surname: Barrasa fullname: Barrasa, M. Inmaculada organization: Whitehead Institute for Biomedical Research, Cambridge, MA 02142, USA – sequence: 6 givenname: Silke surname: Nuber fullname: Nuber, Silke organization: Ann Romney Center for Neurologic Diseases, Department of Neurology, Brigham and Women’s Hospital and Harvard Medical School, Boston, MA 02115, USA – sequence: 7 givenname: Daniel surname: Termine fullname: Termine, Daniel organization: Whitehead Institute for Biomedical Research, Cambridge, MA 02142, USA – sequence: 8 givenname: Nagendran surname: Ramalingam fullname: Ramalingam, Nagendran organization: Ann Romney Center for Neurologic Diseases, Department of Neurology, Brigham and Women’s Hospital and Harvard Medical School, Boston, MA 02115, USA – sequence: 9 givenname: Gary P.H. surname: Ho fullname: Ho, Gary P.H. organization: Ann Romney Center for Neurologic Diseases, Department of Neurology, Brigham and Women’s Hospital and Harvard Medical School, Boston, MA 02115, USA – sequence: 10 givenname: Tallie surname: Noble fullname: Noble, Tallie organization: Mira Costa College, 1 Barnard Drive, Oceanside, CA 92056, USA – sequence: 11 givenname: Jackson surname: Sandoe fullname: Sandoe, Jackson organization: Whitehead Institute for Biomedical Research, Cambridge, MA 02142, USA – sequence: 12 givenname: Yali surname: Lou fullname: Lou, Yali organization: Whitehead Institute for Biomedical Research, Cambridge, MA 02142, USA – sequence: 13 givenname: Dirk surname: Landgraf fullname: Landgraf, Dirk organization: Whitehead Institute for Biomedical Research, Cambridge, MA 02142, USA – sequence: 14 givenname: Yelena surname: Freyzon fullname: Freyzon, Yelena organization: Whitehead Institute for Biomedical Research, Cambridge, MA 02142, USA – sequence: 15 givenname: Gregory surname: Newby fullname: Newby, Gregory organization: Whitehead Institute for Biomedical Research, Cambridge, MA 02142, USA – sequence: 16 givenname: Frank surname: Soldner fullname: Soldner, Frank organization: Whitehead Institute for Biomedical Research, Cambridge, MA 02142, USA – sequence: 17 givenname: Elizabeth surname: Terry-Kantor fullname: Terry-Kantor, Elizabeth organization: Ann Romney Center for Neurologic Diseases, Department of Neurology, Brigham and Women’s Hospital and Harvard Medical School, Boston, MA 02115, USA – sequence: 18 givenname: Tae-Eun surname: Kim fullname: Kim, Tae-Eun organization: Ann Romney Center for Neurologic Diseases, Department of Neurology, Brigham and Women’s Hospital and Harvard Medical School, Boston, MA 02115, USA – sequence: 19 givenname: Harald F. surname: Hofbauer fullname: Hofbauer, Harald F. organization: Institute of Molecular Biosciences, BioTechMed-Graz, University of Graz, 8010 Graz, Austria – sequence: 20 givenname: Michel surname: Becuwe fullname: Becuwe, Michel organization: Department of Genetics and Complex Diseases, Harvard T.H. Chan School of Public Health, 655 Huntington Avenue, Boston, MA 02115, USA – sequence: 21 givenname: Rudolf surname: Jaenisch fullname: Jaenisch, Rudolf organization: Whitehead Institute for Biomedical Research, Cambridge, MA 02142, USA – sequence: 22 givenname: David surname: Pincus fullname: Pincus, David organization: Whitehead Institute for Biomedical Research, Cambridge, MA 02142, USA – sequence: 23 givenname: Clary B. surname: Clish fullname: Clish, Clary B. organization: Broad Institute of MIT and Harvard, Cambridge, MA 02142, USA – sequence: 24 givenname: Tobias C. surname: Walther fullname: Walther, Tobias C. organization: Department of Genetics and Complex Diseases, Harvard T.H. Chan School of Public Health, 655 Huntington Avenue, Boston, MA 02115, USA – sequence: 25 givenname: Robert V. surname: Farese fullname: Farese, Robert V. organization: Department of Genetics and Complex Diseases, Harvard T.H. Chan School of Public Health, 655 Huntington Avenue, Boston, MA 02115, USA – sequence: 26 givenname: Supriya surname: Srinivasan fullname: Srinivasan, Supriya organization: Department of Chemical Physiology and The Dorris Neuroscience Center, 1 Barnard Drive, Oceanside, CA 92056, USA – sequence: 27 givenname: Michael A. surname: Welte fullname: Welte, Michael A. organization: Department of Biology, University of Rochester, Rochester, NY 14627, USA – sequence: 28 givenname: Sepp D. surname: Kohlwein fullname: Kohlwein, Sepp D. organization: Institute of Molecular Biosciences, BioTechMed-Graz, University of Graz, 8010 Graz, Austria – sequence: 29 givenname: Ulf surname: Dettmer fullname: Dettmer, Ulf email: udettmer@bwh.harvard.edu organization: Ann Romney Center for Neurologic Diseases, Department of Neurology, Brigham and Women’s Hospital and Harvard Medical School, Boston, MA 02115, USA – sequence: 30 givenname: Susan surname: Lindquist fullname: Lindquist, Susan organization: Whitehead Institute for Biomedical Research, Cambridge, MA 02142, USA – sequence: 31 givenname: Dennis surname: Selkoe fullname: Selkoe, Dennis email: dselkoe@bwh.harvard.edu organization: Ann Romney Center for Neurologic Diseases, Department of Neurology, Brigham and Women’s Hospital and Harvard Medical School, Boston, MA 02115, USA |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/30527540$$D View this record in MEDLINE/PubMed |
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| Copyright | 2018 Elsevier Inc. Copyright © 2018 Elsevier Inc. All rights reserved. |
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| Keywords | synucleinopathy triglyceride unsaturated fatty acid oleic acid diglyceride alpha-synuclein lipid droplets tetramer Parkinson’s disease stearoyl-CoA-desaturase inclusions |
| Language | English |
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| Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 Author Contributions Conceptualization: SF,UD,SL,DS,SK,DT,MAW,AH; Methodology: SF,AH,UD,SL,DS,CC,DS; Formal Analysis: SF,AH,UD,SL,DS,IB,TN,SS,GN,TI; Investigation: SF,AH,UD,TI,GN,TN,DL,DT,VB, JS, YF, YL, TEK,ETK,MB,SN,LC,GH,NR; Resources: VB,AH,UD,TI,YF,IB,TN,SS,CC,DP,HH,SK,RJ,SL,FS,DS; Writing Original Draft: SF,UD,DS,SK; Writing Review and Editing: SF,UD,DS,SK,MAW,AH,IB; Visualization: SF,UD,IB,DS,SK; Supervision: UD,DS,SL,SK,MAW,BF,TW,SS. |
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| PublicationTitle | Molecular cell |
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| Snippet | In Parkinson’s disease (PD), α-synuclein (αS) pathologically impacts the brain, a highly lipid-rich organ. We investigated how alterations in αS or... In Parkinson's disease (PD), α-synuclein (αS) pathologically impacts the brain, a highly lipid-rich organ. We investigated how alterations in αS or... In Parkinson's disease (PD), α-synuclein (αS) pathologically impacts the brain, a highly lipid-rich organ. We investigated how alterations in αS or lipid/fatty... In Parkinson’s disease (PD), α-Synuclein (αS) pathologically impacts the brain, a highly lipid-rich organ. We investigated how alterations in αS or lipid/fatty... |
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| SubjectTerms | alpha-synuclein alpha-Synuclein - genetics alpha-Synuclein - toxicity Animals Antiparkinson Agents - pharmacology Caenorhabditis elegans - drug effects Caenorhabditis elegans - enzymology Caenorhabditis elegans - genetics Cell Line Cerebral Cortex - drug effects Cerebral Cortex - enzymology Cerebral Cortex - pathology diglyceride Diglycerides - metabolism Disease Models, Animal Dopaminergic Neurons - drug effects Dopaminergic Neurons - enzymology Dopaminergic Neurons - pathology Drug Discovery - methods Enzyme Inhibitors - pharmacology Humans inclusions Induced Pluripotent Stem Cells - drug effects Induced Pluripotent Stem Cells - enzymology Induced Pluripotent Stem Cells - pathology lipid droplets Lipid Droplets - drug effects Lipid Droplets - enzymology Lipid Metabolism - drug effects Metabolomics - methods Mice, Inbred C57BL Mice, Transgenic Molecular Targeted Therapy Nerve Degeneration Neural Stem Cells - drug effects Neural Stem Cells - enzymology Neural Stem Cells - pathology Neurons - drug effects Neurons - enzymology Neurons - pathology oleic acid Oleic Acid - metabolism Parkinson Disease - drug therapy Parkinson Disease - enzymology Parkinson Disease - genetics Parkinson Disease - pathology Parkinson’s disease Rats, Sprague-Dawley Saccharomyces cerevisiae - drug effects Saccharomyces cerevisiae - enzymology Saccharomyces cerevisiae - genetics Stearoyl-CoA Desaturase - antagonists & inhibitors Stearoyl-CoA Desaturase - metabolism stearoyl-CoA-desaturase synucleinopathy tetramer triglyceride Triglycerides - metabolism unsaturated fatty acid |
| Title | Lipidomic Analysis of α-Synuclein Neurotoxicity Identifies Stearoyl CoA Desaturase as a Target for Parkinson Treatment |
| URI | https://dx.doi.org/10.1016/j.molcel.2018.11.028 https://www.ncbi.nlm.nih.gov/pubmed/30527540 https://www.proquest.com/docview/2155157241/abstract/ https://pubmed.ncbi.nlm.nih.gov/PMC6408259 |
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