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SOD1 Lysine 123 Acetylation in the Adult Central Nervous System
Superoxide dismutase 1 (SOD1) knockout (Sod1(−/−)) mice exhibit an accelerated aging phenotype. In humans, SOD1 mutations are linked to familial amyotrophic lateral sclerosis (ALS), and post-translational modification (PTM) of wild-type SOD1 has been associated with sporadic ALS. Reversible acetylat...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Frontiers Media S.A.
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5167747/ https://www.ncbi.nlm.nih.gov/pubmed/28066183 http://dx.doi.org/10.3389/fncel.2016.00287 |
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author | Kaliszewski, Michael Kennedy, Austin K. Blaes, Shelby L. Shaffer, Robert S. Knott, Andrew B. Song, Wenjun Hauser, Henry A. Bossy, Blaise Huang, Ting-Ting Bossy-Wetzel, Ella |
author_facet | Kaliszewski, Michael Kennedy, Austin K. Blaes, Shelby L. Shaffer, Robert S. Knott, Andrew B. Song, Wenjun Hauser, Henry A. Bossy, Blaise Huang, Ting-Ting Bossy-Wetzel, Ella |
author_sort | Kaliszewski, Michael |
collection | PubMed |
description | Superoxide dismutase 1 (SOD1) knockout (Sod1(−/−)) mice exhibit an accelerated aging phenotype. In humans, SOD1 mutations are linked to familial amyotrophic lateral sclerosis (ALS), and post-translational modification (PTM) of wild-type SOD1 has been associated with sporadic ALS. Reversible acetylation regulates many enzymes and proteomic studies have identified SOD1 acetylation at lysine 123 (K123). The function and distribution of K123-acetylated SOD1 (Ac-K123 SOD1) in the nervous system is unknown. Here, we generated polyclonal rabbit antibodies against Ac-K123 SOD1. Sod1 deletion in Sod1(−/−) mice, K123 mutation or preabsorption with Ac-K123 peptide all abolished antibody binding. Using immunohistochemistry, we assessed Ac-K123 SOD1 distribution in the normal adult mouse nervous system. In the cerebellum, Ac-K123 SOD1 staining was prominent in cell bodies of the granular cell layer (GCL) and Purkinje cell dendrites and interneurons of the molecular cell layer. In the hippocampus, Ac-K123 SOD1 staining was strong in the fimbria, subiculum, pyramidal cells and Schaffer collateral fibers of the cornus ammonis field 1 (CA1) region and granule and neuronal progenitor cells of the dentate gyrus. In addition, labeling was observed in the choroid plexus (CP) and the ependyma of the brain ventricles and central canal of the spinal cord. In the olfactory bulb, Ac-K123 SOD1 staining was prominent in axons of sensory neurons, in cell bodies of interneurons and neurites of the mitral and tufted cells. In the retina, labeling was strong in the retinal ganglion cell layer (RGCL) and axons of retinal ganglion cells (RGCs), the inner nuclear layer (INL) and cone photoreceptors of the outer nuclear layer (ONL). In summary, our findings describe Ac-K123 SOD1 distribution to distinct regions and cell types of the normal nervous system. |
format | Online Article Text |
id | pubmed-5167747 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-51677472017-01-06 SOD1 Lysine 123 Acetylation in the Adult Central Nervous System Kaliszewski, Michael Kennedy, Austin K. Blaes, Shelby L. Shaffer, Robert S. Knott, Andrew B. Song, Wenjun Hauser, Henry A. Bossy, Blaise Huang, Ting-Ting Bossy-Wetzel, Ella Front Cell Neurosci Neuroscience Superoxide dismutase 1 (SOD1) knockout (Sod1(−/−)) mice exhibit an accelerated aging phenotype. In humans, SOD1 mutations are linked to familial amyotrophic lateral sclerosis (ALS), and post-translational modification (PTM) of wild-type SOD1 has been associated with sporadic ALS. Reversible acetylation regulates many enzymes and proteomic studies have identified SOD1 acetylation at lysine 123 (K123). The function and distribution of K123-acetylated SOD1 (Ac-K123 SOD1) in the nervous system is unknown. Here, we generated polyclonal rabbit antibodies against Ac-K123 SOD1. Sod1 deletion in Sod1(−/−) mice, K123 mutation or preabsorption with Ac-K123 peptide all abolished antibody binding. Using immunohistochemistry, we assessed Ac-K123 SOD1 distribution in the normal adult mouse nervous system. In the cerebellum, Ac-K123 SOD1 staining was prominent in cell bodies of the granular cell layer (GCL) and Purkinje cell dendrites and interneurons of the molecular cell layer. In the hippocampus, Ac-K123 SOD1 staining was strong in the fimbria, subiculum, pyramidal cells and Schaffer collateral fibers of the cornus ammonis field 1 (CA1) region and granule and neuronal progenitor cells of the dentate gyrus. In addition, labeling was observed in the choroid plexus (CP) and the ependyma of the brain ventricles and central canal of the spinal cord. In the olfactory bulb, Ac-K123 SOD1 staining was prominent in axons of sensory neurons, in cell bodies of interneurons and neurites of the mitral and tufted cells. In the retina, labeling was strong in the retinal ganglion cell layer (RGCL) and axons of retinal ganglion cells (RGCs), the inner nuclear layer (INL) and cone photoreceptors of the outer nuclear layer (ONL). In summary, our findings describe Ac-K123 SOD1 distribution to distinct regions and cell types of the normal nervous system. Frontiers Media S.A. 2016-12-20 /pmc/articles/PMC5167747/ /pubmed/28066183 http://dx.doi.org/10.3389/fncel.2016.00287 Text en Copyright © 2016 Kaliszewski, Kennedy, Blaes, Shaffer, Knott, Song, Hauser, Bossy, Huang and Bossy-Wetzel. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution and reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Neuroscience Kaliszewski, Michael Kennedy, Austin K. Blaes, Shelby L. Shaffer, Robert S. Knott, Andrew B. Song, Wenjun Hauser, Henry A. Bossy, Blaise Huang, Ting-Ting Bossy-Wetzel, Ella SOD1 Lysine 123 Acetylation in the Adult Central Nervous System |
title | SOD1 Lysine 123 Acetylation in the Adult Central Nervous System |
title_full | SOD1 Lysine 123 Acetylation in the Adult Central Nervous System |
title_fullStr | SOD1 Lysine 123 Acetylation in the Adult Central Nervous System |
title_full_unstemmed | SOD1 Lysine 123 Acetylation in the Adult Central Nervous System |
title_short | SOD1 Lysine 123 Acetylation in the Adult Central Nervous System |
title_sort | sod1 lysine 123 acetylation in the adult central nervous system |
topic | Neuroscience |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5167747/ https://www.ncbi.nlm.nih.gov/pubmed/28066183 http://dx.doi.org/10.3389/fncel.2016.00287 |
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