A potential role for neuronal connexin 36 in the pathogenesis of amyotrophic lateral sclerosis

•A role for neuronal connexin 36 in the pathogenesis of ALS is proposed.•The mechanism relies on contribution of connexin 36 to ALS-related neuronal death.•A perspective for the use of connexin 36 blockade for ALS therapy is discussed. Neuronal gap junctional protein connexin 36 (Cx36) contributes t...

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Published in:	Neuroscience letters Vol. 666; pp. 1 - 4
Main Authors:	Belousov, Andrei B., Nishimune, Hiroshi, Denisova, Janna V., Fontes, Joseph D.
Format:	Journal Article
Language:	English
Published:	Ireland Elsevier B.V 14.02.2018
Subjects:	Amyotrophic lateral sclerosis Amyotrophic Lateral Sclerosis - metabolism Amyotrophic Lateral Sclerosis - pathology Animals Connexin 36 Connexins - metabolism Disease Models, Animal Gap Junction delta-2 Protein Gap junctions Gap Junctions - metabolism Humans Mice Motor Neurons - metabolism Neurodegenerative diseases Spinal cord Spinal Cord - metabolism Superoxide Dismutase-1 - metabolism Amyotrophic lateral sclerosis Spinal cord Neurodegenerative diseases Gap junctions Connexin 36
ISSN:	0304-3940, 1872-7972, 1872-7972
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Abstract	•A role for neuronal connexin 36 in the pathogenesis of ALS is proposed.•The mechanism relies on contribution of connexin 36 to ALS-related neuronal death.•A perspective for the use of connexin 36 blockade for ALS therapy is discussed. Neuronal gap junctional protein connexin 36 (Cx36) contributes to neuronal death following a range of acute brain insults such as ischemia, traumatic brain injury and epilepsy. Whether Cx36 contributes to neuronal death and pathological outcomes in chronic neurodegenerative diseases, such as amyotrophic lateral sclerosis (ALS), is not known. We show here that the expression of Cx36 is significantly decreased in lumbar segments of the spinal cord of both human ALS subjects and SOD1G93A mice as compared to healthy human and wild-type mouse controls, respectively. In purified neuronal cultures prepared from the spinal cord of wild-type mice, knockdown of Cx36 reduces neuronal death caused by overexpression of the mutant human SOD1-G93A protein. Taken together, these data suggest a possible contribution of Cx36 to ALS pathogenesis. A perspective for the use of blockers of Cx36 gap junction channels for ALS therapy is discussed.
AbstractList	Neuronal gap junctional protein connexin 36 (Cx36) contributes to neuronal death following a range of acute brain insults such as ischemia, traumatic brain injury and epilepsy. Whether Cx36 contributes to neuronal death and pathological outcomes in chronic neurodegenerative diseases, such as amyotrophic lateral sclerosis (ALS), is not known. We show here that the expression of Cx36 is significantly decreased in lumbar segments of the spinal cord of both human ALS subjects and SOD1 mice as compared to healthy human and wild-type mouse controls, respectively. In purified neuronal cultures prepared from the spinal cord of wild-type mice, knockdown of Cx36 reduces neuronal death caused by overexpression of the mutant human SOD1-G93A protein. Taken together, these data suggest a possible contribution of Cx36 to ALS pathogenesis. A perspective for the use of blockers of Cx36 gap junction channels for ALS therapy is discussed. •A role for neuronal connexin 36 in the pathogenesis of ALS is proposed.•The mechanism relies on contribution of connexin 36 to ALS-related neuronal death.•A perspective for the use of connexin 36 blockade for ALS therapy is discussed. Neuronal gap junctional protein connexin 36 (Cx36) contributes to neuronal death following a range of acute brain insults such as ischemia, traumatic brain injury and epilepsy. Whether Cx36 contributes to neuronal death and pathological outcomes in chronic neurodegenerative diseases, such as amyotrophic lateral sclerosis (ALS), is not known. We show here that the expression of Cx36 is significantly decreased in lumbar segments of the spinal cord of both human ALS subjects and SOD1G93A mice as compared to healthy human and wild-type mouse controls, respectively. In purified neuronal cultures prepared from the spinal cord of wild-type mice, knockdown of Cx36 reduces neuronal death caused by overexpression of the mutant human SOD1-G93A protein. Taken together, these data suggest a possible contribution of Cx36 to ALS pathogenesis. A perspective for the use of blockers of Cx36 gap junction channels for ALS therapy is discussed. Neuronal gap junctional protein connexin 36 (Cx36) contributes to neuronal death following a range of acute brain insults such as ischemia, traumatic brain injury and epilepsy. Whether Cx36 contributes to neuronal death and pathological outcomes in chronic neurodegenerative diseases, such as amyotrophic lateral sclerosis (ALS), is not known. We show here that the expression of Cx36 is significantly decreased in lumbar segments of the spinal cord of both human ALS subjects and SOD1G93A mice as compared to healthy human and wild-type mouse controls, respectively. In purified neuronal cultures prepared from the spinal cord of wild-type mice, knockdown of Cx36 reduces neuronal death caused by overexpression of the mutant human SOD1-G93A protein. Taken together, these data suggest a possible contribution of Cx36 to ALS pathogenesis. A perspective for the use of blockers of Cx36 gap junction channels for ALS therapy is discussed. Neuronal gap junctional protein connexin 36 (Cx36) contributes to neuronal death following a range of acute brain insults such as ischemia, traumatic brain injury and epilepsy. Whether Cx36 contributes to neuronal death and pathological outcomes in chronic neurodegenerative diseases, such as amyotrophic lateral sclerosis (ALS), is not known. We show here that the expression of Cx36 is significantly decreased in lumbar segments of the spinal cord of both human ALS subjects and SOD1G93A mice as compared to healthy human and wild-type mouse controls, respectively. In purified neuronal cultures prepared from the spinal cord of wild-type mice, knockdown of Cx36 reduces neuronal death caused by overexpression of the mutant human SOD1-G93A protein. Taken together, these data suggest a possible contribution of Cx36 to ALS pathogenesis. A perspective for the use of blockers of Cx36 gap junction channels for ALS therapy is discussed.Neuronal gap junctional protein connexin 36 (Cx36) contributes to neuronal death following a range of acute brain insults such as ischemia, traumatic brain injury and epilepsy. Whether Cx36 contributes to neuronal death and pathological outcomes in chronic neurodegenerative diseases, such as amyotrophic lateral sclerosis (ALS), is not known. We show here that the expression of Cx36 is significantly decreased in lumbar segments of the spinal cord of both human ALS subjects and SOD1G93A mice as compared to healthy human and wild-type mouse controls, respectively. In purified neuronal cultures prepared from the spinal cord of wild-type mice, knockdown of Cx36 reduces neuronal death caused by overexpression of the mutant human SOD1-G93A protein. Taken together, these data suggest a possible contribution of Cx36 to ALS pathogenesis. A perspective for the use of blockers of Cx36 gap junction channels for ALS therapy is discussed.
Author	Nishimune, Hiroshi Denisova, Janna V. Belousov, Andrei B. Fontes, Joseph D.
AuthorAffiliation	3 Department of Biochemistry and Molecular Biology, University of Kansas Medical Center, Kansas City, Kansas, USA 1 Department of Molecular and Integrative Physiology, University of Kansas Medical Center, Kansas City, Kansas, USA 2 Department of Anatomy and Cell Biology, University of Kansas Medical Center, Kansas City, Kansas, USA
AuthorAffiliation_xml	– name: 3 Department of Biochemistry and Molecular Biology, University of Kansas Medical Center, Kansas City, Kansas, USA – name: 2 Department of Anatomy and Cell Biology, University of Kansas Medical Center, Kansas City, Kansas, USA – name: 1 Department of Molecular and Integrative Physiology, University of Kansas Medical Center, Kansas City, Kansas, USA
Author_xml	– sequence: 1 givenname: Andrei B. surname: Belousov fullname: Belousov, Andrei B. email: abelousov@kumc.edu organization: Departments of Molecular and Integrative Physiology, University of Kansas Medical Center, Kansas City, KS, USA – sequence: 2 givenname: Hiroshi surname: Nishimune fullname: Nishimune, Hiroshi organization: Departments of Anatomy and Cell Biology, University of Kansas Medical Center, Kansas City, KS, USA – sequence: 3 givenname: Janna V. surname: Denisova fullname: Denisova, Janna V. organization: Departments of Molecular and Integrative Physiology, University of Kansas Medical Center, Kansas City, KS, USA – sequence: 4 givenname: Joseph D. surname: Fontes fullname: Fontes, Joseph D. organization: Departments of Biochemistry and Molecular Biology, University of Kansas Medical Center, Kansas City, KS, USA
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Cites_doi	10.1016/j.expneurol.2011.06.003 10.1073/pnas.051634298 10.1016/j.nbd.2013.04.012 10.1038/362059a0 10.1523/JNEUROSCI.2137-08.2008 10.1016/j.nbd.2012.07.004 10.1073/pnas.97.13.7573 10.1016/j.neulet.2012.06.065 10.2307/3579763 10.1371/journal.pone.0021108 10.1523/JNEUROSCI.1119-12.2013 10.1152/jn.00362.2007 10.1152/jn.00656.2010 10.1371/journal.pone.0125395 10.1523/JNEUROSCI.3872-11.2012 10.1073/pnas.0402044101 10.1016/j.tins.2012.11.001 10.1523/JNEUROSCI.6787-10.2011 10.1038/nm1205 10.1038/cdd.2008.196
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Keywords	Amyotrophic lateral sclerosis Spinal cord Neurodegenerative diseases Gap junctions Connexin 36
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References	Jouroukhin, Ostritsky, Assaf, Pelled, Giladi, Gozes (bib0060) 2013; 56 Wang, Song, Denisova, Park, Fontes, Belousov (bib0015) 2012; 32 Brooks, Sanjak, Belden, Juhasz-Poscine, Waclawik (bib0030) 2000 Ralph, Radcliffe, Day, Carthy, Leroux, Lee, Wong, Bilsland, Greensmith, Kingsman, Mitrophanous, Mazarakis, Azzouz (bib0055) 2005; 11 Cruikshank, Hopperstad, Younger, Connors, Spray, Srinivas (bib0105) 2004; 101 Belousov, Fontes (bib0025) 2013; 36 de Rivero Vaccari, Corriveau, Belousov (bib0090) 2007; 98 Rosen, Siddique, Patterson, Figlewicz, Sapp, Hentati, Donaldson, Goto, O'Regan, Deng (bib0035) 1993; 362 Yoo, Ko (bib0050) 2011; 231 Li, Kamasawa, Ciolofan, Olson, Lu, Davidson, Yasumura, Shigemoto, Rash, Nagy (bib0085) 2008; 28 Wang, Denisova, Kang, Fontes, Zhu, Belousov (bib0005) 2010; 104 Song, Song, Kincaid, Bossy, Bossy-Wetzel (bib0045) 2013; 51 Rash, Staines, Yasumura, Patel, Furman, Stelmack, Nagy (bib0075) 2000; 97 Fontes, Ramsey, Polk, Koop, Denisova, Belousov (bib0020) 2015; 10 Belousov, Wang, Song, Denisova, Berman, Fontes (bib0010) 2012; 524 Parone, Da Cruz, Han, McAlonis-Downes, Vetto, Lee, Tseng, Cleveland (bib0065) 2013; 33 Park, Wang, Park, Denisova, Fontes, Belousov (bib0070) 2011; 31 Takeuchi, Mizoguchi, Doi, Jin, Noda, Liang, Li, Zhou, Mori, Yasuoka, Li, Parajuli, Kawanokuchi, Sonobe, Sato, Yamanaka, Sobue, Mizuno, Suzumura (bib0095) 2011; 6 Liu, Narla, Kurinov, Li, Uckun (bib0040) 1999; 151 Eugenin, Eckardt, Theis, Willecke, Bennett, Saez (bib0080) 2001; 98 Decrock, Vinken, De Vuyst, Krysko, D'Herde, Vanhaecke, Vandenabeele, Rogiers, Leybaert (bib0100) 2009; 16 Belousov (10.1016/j.neulet.2017.12.027_bib0010) 2012; 524 Parone (10.1016/j.neulet.2017.12.027_bib0065) 2013; 33 Decrock (10.1016/j.neulet.2017.12.027_bib0100) 2009; 16 Takeuchi (10.1016/j.neulet.2017.12.027_bib0095) 2011; 6 de Rivero Vaccari (10.1016/j.neulet.2017.12.027_bib0090) 2007; 98 Wang (10.1016/j.neulet.2017.12.027_bib0005) 2010; 104 Yoo (10.1016/j.neulet.2017.12.027_bib0050) 2011; 231 Eugenin (10.1016/j.neulet.2017.12.027_bib0080) 2001; 98 Wang (10.1016/j.neulet.2017.12.027_bib0015) 2012; 32 Park (10.1016/j.neulet.2017.12.027_bib0070) 2011; 31 Belousov (10.1016/j.neulet.2017.12.027_bib0025) 2013; 36 Song (10.1016/j.neulet.2017.12.027_bib0045) 2013; 51 Fontes (10.1016/j.neulet.2017.12.027_bib0020) 2015; 10 Liu (10.1016/j.neulet.2017.12.027_bib0040) 1999; 151 Ralph (10.1016/j.neulet.2017.12.027_bib0055) 2005; 11 Jouroukhin (10.1016/j.neulet.2017.12.027_bib0060) 2013; 56 Rosen (10.1016/j.neulet.2017.12.027_bib0035) 1993; 362 Li (10.1016/j.neulet.2017.12.027_bib0085) 2008; 28 Cruikshank (10.1016/j.neulet.2017.12.027_bib0105) 2004; 101 Brooks (10.1016/j.neulet.2017.12.027_bib0030) 2000 Rash (10.1016/j.neulet.2017.12.027_bib0075) 2000; 97
References_xml	– volume: 33 start-page: 4657 year: 2013 end-page: 4671 ident: bib0065 article-title: Enhancing mitochondrial calcium buffering capacity reduces aggregation of misfolded SOD1 and motor neuron cell death without extending survival in mouse models of inherited amyotrophic lateral sclerosis publication-title: J. Neurosci. – volume: 31 start-page: 5909 year: 2011 end-page: 5920 ident: bib0070 article-title: Interplay of chemical neurotransmitters regulates developmental increase in electrical synapses publication-title: J. Neurosci. – volume: 231 start-page: 147 year: 2011 end-page: 159 ident: bib0050 article-title: Treatment with trichostatin A initiated after disease onset delays disease progression and increases survival in a mouse model of amyotrophic lateral sclerosis publication-title: Exp. Neurol. – volume: 11 start-page: 429 year: 2005 end-page: 433 ident: bib0055 article-title: Silencing mutant SOD1 using RNAi protects against neurodegeneration and extends survival in an ALS model publication-title: Nat. Med. – volume: 101 start-page: 12364 year: 2004 end-page: 12369 ident: bib0105 article-title: Potent block of Cx36 and Cx50 gap junction channels by mefloquine publication-title: Proc. Natl. Acad. Sci. U. S. A. – volume: 98 start-page: 4190 year: 2001 end-page: 4195 ident: bib0080 article-title: Microglia at brain stab wounds express connexin 43 and publication-title: Proc. Natl. Acad. Sci. U. S. A. – volume: 32 start-page: 713 year: 2012 end-page: 725 ident: bib0015 article-title: Neuronal gap junction coupling is regulated by glutamate and plays critical role in cell death during neuronal injury publication-title: J. Neurosci. – volume: 36 start-page: 227 year: 2013 end-page: 236 ident: bib0025 article-title: Neuronal gap junctions: making and breaking connections during development and injury publication-title: Trends Neurosci. – volume: 98 start-page: 2878 year: 2007 end-page: 2886 ident: bib0090 article-title: Gap junctions are required for NMDA receptor-dependent cell death in developing neurons publication-title: J. Neurophysiol. – volume: 51 start-page: 72 year: 2013 end-page: 81 ident: bib0045 article-title: Mutant SOD1G93A triggers mitochondrial fragmentation in spinal cord motor neurons: neuroprotection by SIRT3 and PGC-1α publication-title: Neurobiol. Dis. – volume: 10 start-page: e0125395 year: 2015 ident: bib0020 article-title: Death of neurons following injury requires conductive neuronal gap junction channels but not a specific connexin publication-title: PLoS One – volume: 362 start-page: 59 year: 1993 end-page: 62 ident: bib0035 article-title: Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis publication-title: Nature – volume: 56 start-page: 79 year: 2013 end-page: 94 ident: bib0060 article-title: NAP (davunetide) modifies disease progression in a mouse model of severe neurodegeneration: protection against impairments in axonal transport publication-title: Neurobiol. Dis. – volume: 16 start-page: 524 year: 2009 end-page: 536 ident: bib0100 article-title: Connexin-related signaling in cell death: to live or let die? publication-title: Cell Death Differ. – start-page: 31 year: 2000 end-page: 58 ident: bib0030 article-title: Natural history of amyotrophic lateral sclerosis – impairment, disability, handicap publication-title: Amyotrophic Lateral Sclerosis – volume: 524 start-page: 16 year: 2012 end-page: 19 ident: bib0010 article-title: Neuronal gap junctions play a role in the secondary neuronal death following controlled cortical impact publication-title: Neurosci. Lett. – volume: 6 start-page: e21108 year: 2011 ident: bib0095 article-title: Blockade of gap junction hemichannel suppresses disease progression in mouse models of amyotrophic lateral sclerosis and Alzheimer’s disease publication-title: PLoS One – volume: 151 start-page: 133 year: 1999 end-page: 141 ident: bib0040 article-title: Increased hydroxyl radical production and apoptosis in PC12 neuron cells expressing the gain-of-function mutant G93A SOD1 gene publication-title: Radiat. Res. – volume: 97 start-page: 7573 year: 2000 end-page: 7578 ident: bib0075 article-title: Immunogold evidence that neuronal gap junctions in adult rat brain and spinal cord contain connexin-36 but not connexin-32 or connexin-43 publication-title: Proc. Natl. Acad. Sci. U. S. A. – volume: 28 start-page: 9769 year: 2008 end-page: 9789 ident: bib0085 article-title: Connexin45-containing neuronal gap junctions in rodent retina also contain connexin36 in both apposing hemiplaques forming bihomotypic gap junctions, with scaffolding contributed by zonula occludens-1 publication-title: J. Neurosci. – volume: 104 start-page: 3551 year: 2010 end-page: 3556 ident: bib0005 article-title: Neuronal gap junctions are required for NMDA receptor-mediated excitotoxicity: implications in ischemic stroke publication-title: J. Neurophysiol. – volume: 231 start-page: 147 year: 2011 ident: 10.1016/j.neulet.2017.12.027_bib0050 article-title: Treatment with trichostatin A initiated after disease onset delays disease progression and increases survival in a mouse model of amyotrophic lateral sclerosis publication-title: Exp. Neurol. doi: 10.1016/j.expneurol.2011.06.003 – volume: 98 start-page: 4190 year: 2001 ident: 10.1016/j.neulet.2017.12.027_bib0080 article-title: Microglia at brain stab wounds express connexin 43 and in vitro form functional gap junctions after treatment with interferon-γ and tumor necrosis factor-α publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.051634298 – volume: 56 start-page: 79 year: 2013 ident: 10.1016/j.neulet.2017.12.027_bib0060 article-title: NAP (davunetide) modifies disease progression in a mouse model of severe neurodegeneration: protection against impairments in axonal transport publication-title: Neurobiol. Dis. doi: 10.1016/j.nbd.2013.04.012 – start-page: 31 year: 2000 ident: 10.1016/j.neulet.2017.12.027_bib0030 article-title: Natural history of amyotrophic lateral sclerosis – impairment, disability, handicap – volume: 362 start-page: 59 year: 1993 ident: 10.1016/j.neulet.2017.12.027_bib0035 article-title: Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis publication-title: Nature doi: 10.1038/362059a0 – volume: 28 start-page: 9769 year: 2008 ident: 10.1016/j.neulet.2017.12.027_bib0085 article-title: Connexin45-containing neuronal gap junctions in rodent retina also contain connexin36 in both apposing hemiplaques forming bihomotypic gap junctions, with scaffolding contributed by zonula occludens-1 publication-title: J. Neurosci. doi: 10.1523/JNEUROSCI.2137-08.2008 – volume: 51 start-page: 72 year: 2013 ident: 10.1016/j.neulet.2017.12.027_bib0045 article-title: Mutant SOD1G93A triggers mitochondrial fragmentation in spinal cord motor neurons: neuroprotection by SIRT3 and PGC-1α publication-title: Neurobiol. Dis. doi: 10.1016/j.nbd.2012.07.004 – volume: 97 start-page: 7573 year: 2000 ident: 10.1016/j.neulet.2017.12.027_bib0075 article-title: Immunogold evidence that neuronal gap junctions in adult rat brain and spinal cord contain connexin-36 but not connexin-32 or connexin-43 publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.97.13.7573 – volume: 524 start-page: 16 year: 2012 ident: 10.1016/j.neulet.2017.12.027_bib0010 article-title: Neuronal gap junctions play a role in the secondary neuronal death following controlled cortical impact publication-title: Neurosci. Lett. doi: 10.1016/j.neulet.2012.06.065 – volume: 151 start-page: 133 year: 1999 ident: 10.1016/j.neulet.2017.12.027_bib0040 article-title: Increased hydroxyl radical production and apoptosis in PC12 neuron cells expressing the gain-of-function mutant G93A SOD1 gene publication-title: Radiat. Res. doi: 10.2307/3579763 – volume: 6 start-page: e21108 year: 2011 ident: 10.1016/j.neulet.2017.12.027_bib0095 article-title: Blockade of gap junction hemichannel suppresses disease progression in mouse models of amyotrophic lateral sclerosis and Alzheimer’s disease publication-title: PLoS One doi: 10.1371/journal.pone.0021108 – volume: 33 start-page: 4657 year: 2013 ident: 10.1016/j.neulet.2017.12.027_bib0065 article-title: Enhancing mitochondrial calcium buffering capacity reduces aggregation of misfolded SOD1 and motor neuron cell death without extending survival in mouse models of inherited amyotrophic lateral sclerosis publication-title: J. Neurosci. doi: 10.1523/JNEUROSCI.1119-12.2013 – volume: 98 start-page: 2878 year: 2007 ident: 10.1016/j.neulet.2017.12.027_bib0090 article-title: Gap junctions are required for NMDA receptor-dependent cell death in developing neurons publication-title: J. Neurophysiol. doi: 10.1152/jn.00362.2007 – volume: 104 start-page: 3551 year: 2010 ident: 10.1016/j.neulet.2017.12.027_bib0005 article-title: Neuronal gap junctions are required for NMDA receptor-mediated excitotoxicity: implications in ischemic stroke publication-title: J. Neurophysiol. doi: 10.1152/jn.00656.2010 – volume: 10 start-page: e0125395 year: 2015 ident: 10.1016/j.neulet.2017.12.027_bib0020 article-title: Death of neurons following injury requires conductive neuronal gap junction channels but not a specific connexin publication-title: PLoS One doi: 10.1371/journal.pone.0125395 – volume: 32 start-page: 713 year: 2012 ident: 10.1016/j.neulet.2017.12.027_bib0015 article-title: Neuronal gap junction coupling is regulated by glutamate and plays critical role in cell death during neuronal injury publication-title: J. Neurosci. doi: 10.1523/JNEUROSCI.3872-11.2012 – volume: 101 start-page: 12364 year: 2004 ident: 10.1016/j.neulet.2017.12.027_bib0105 article-title: Potent block of Cx36 and Cx50 gap junction channels by mefloquine publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.0402044101 – volume: 36 start-page: 227 year: 2013 ident: 10.1016/j.neulet.2017.12.027_bib0025 article-title: Neuronal gap junctions: making and breaking connections during development and injury publication-title: Trends Neurosci. doi: 10.1016/j.tins.2012.11.001 – volume: 31 start-page: 5909 year: 2011 ident: 10.1016/j.neulet.2017.12.027_bib0070 article-title: Interplay of chemical neurotransmitters regulates developmental increase in electrical synapses publication-title: J. Neurosci. doi: 10.1523/JNEUROSCI.6787-10.2011 – volume: 11 start-page: 429 year: 2005 ident: 10.1016/j.neulet.2017.12.027_bib0055 article-title: Silencing mutant SOD1 using RNAi protects against neurodegeneration and extends survival in an ALS model publication-title: Nat. Med. doi: 10.1038/nm1205 – volume: 16 start-page: 524 year: 2009 ident: 10.1016/j.neulet.2017.12.027_bib0100 article-title: Connexin-related signaling in cell death: to live or let die? publication-title: Cell Death Differ. doi: 10.1038/cdd.2008.196
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Snippet	•A role for neuronal connexin 36 in the pathogenesis of ALS is proposed.•The mechanism relies on contribution of connexin 36 to ALS-related neuronal death.•A... Neuronal gap junctional protein connexin 36 (Cx36) contributes to neuronal death following a range of acute brain insults such as ischemia, traumatic brain...
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SubjectTerms	Amyotrophic lateral sclerosis Amyotrophic Lateral Sclerosis - metabolism Amyotrophic Lateral Sclerosis - pathology Animals Connexin 36 Connexins - metabolism Disease Models, Animal Gap Junction delta-2 Protein Gap junctions Gap Junctions - metabolism Humans Mice Motor Neurons - metabolism Neurodegenerative diseases Spinal cord Spinal Cord - metabolism Superoxide Dismutase-1 - metabolism
Title	A potential role for neuronal connexin 36 in the pathogenesis of amyotrophic lateral sclerosis
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