Focused Cerebellar Laser Light Induced Hyperthermia Improves Symptoms and Pathology of Polyglutamine Disease SCA1 in a Mouse Model
Spinocerebellar ataxia 1 (SCA1) results from pathologic glutamine expansion in the ataxin-1 protein (ATXN1). This misfolded ATXN1 causes severe Purkinje cell (PC) loss and cerebellar ataxia in both humans and mice with the SCA1 disease. The molecular chaperone heat-shock proteins (HSPs) are known to...
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description | Spinocerebellar ataxia 1 (SCA1) results from pathologic glutamine expansion in the ataxin-1 protein (ATXN1). This misfolded ATXN1 causes severe Purkinje cell (PC) loss and cerebellar ataxia in both humans and mice with the SCA1 disease. The molecular chaperone heat-shock proteins (HSPs) are known to modulate polyglutamine protein aggregation and are neuroprotective. Since HSPs are induced under stress, we explored the effects of focused laser light induced hyperthermia (HT) on HSP-mediated protection against ATXN1 toxicity. We first tested the effects of HT in a cell culture model and found that HT induced Hsp70 and increased its localization to nuclear inclusions in HeLa cells expressing GFP-ATXN1[82Q]. HT treatment decreased ATXN1 aggregation by making GFP-ATXN1[82Q] inclusions smaller and more numerous compared to non-treated cells. Further, we tested our HT approach in vivo using a transgenic (Tg) mouse model of SCA1. We found that our laser method increased cerebellar temperature from 38 to 40 °C without causing any neuronal damage or inflammatory response. Interestingly, mild cerebellar HT stimulated the production of Hsp70 to a significant level. Furthermore, multiple exposure of focused cerebellar laser light induced HT to heterozygous SCA1 transgenic (Tg) mice significantly suppressed the SCA1 phenotype as compared to sham-treated control animals. Moreover, in treated SCA1 Tg mice, the levels of PC calcium signaling/buffering protein calbindin-D28k markedly increased followed by a reduction in PC neurodegenerative morphology. Taken together, our data suggest that laser light induced HT is a novel non-invasive approach to treat SCA1 and maybe other polyglutamine disorders. |
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S.</creator><creatorcontrib>Hearst, Scoty M. ; Shao, Qingmei ; Lopez, Mariper ; Raucher, Drazen ; Vig, Parminder J. S.</creatorcontrib><description>Spinocerebellar ataxia 1 (SCA1) results from pathologic glutamine expansion in the ataxin-1 protein (ATXN1). This misfolded ATXN1 causes severe Purkinje cell (PC) loss and cerebellar ataxia in both humans and mice with the SCA1 disease. The molecular chaperone heat-shock proteins (HSPs) are known to modulate polyglutamine protein aggregation and are neuroprotective. Since HSPs are induced under stress, we explored the effects of focused laser light induced hyperthermia (HT) on HSP-mediated protection against ATXN1 toxicity. We first tested the effects of HT in a cell culture model and found that HT induced Hsp70 and increased its localization to nuclear inclusions in HeLa cells expressing GFP-ATXN1[82Q]. HT treatment decreased ATXN1 aggregation by making GFP-ATXN1[82Q] inclusions smaller and more numerous compared to non-treated cells. Further, we tested our HT approach in vivo using a transgenic (Tg) mouse model of SCA1. We found that our laser method increased cerebellar temperature from 38 to 40 °C without causing any neuronal damage or inflammatory response. Interestingly, mild cerebellar HT stimulated the production of Hsp70 to a significant level. Furthermore, multiple exposure of focused cerebellar laser light induced HT to heterozygous SCA1 transgenic (Tg) mice significantly suppressed the SCA1 phenotype as compared to sham-treated control animals. Moreover, in treated SCA1 Tg mice, the levels of PC calcium signaling/buffering protein calbindin-D28k markedly increased followed by a reduction in PC neurodegenerative morphology. 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S.</creatorcontrib><title>Focused Cerebellar Laser Light Induced Hyperthermia Improves Symptoms and Pathology of Polyglutamine Disease SCA1 in a Mouse Model</title><title>Cerebellum (London, England)</title><addtitle>Cerebellum</addtitle><addtitle>Cerebellum</addtitle><description>Spinocerebellar ataxia 1 (SCA1) results from pathologic glutamine expansion in the ataxin-1 protein (ATXN1). This misfolded ATXN1 causes severe Purkinje cell (PC) loss and cerebellar ataxia in both humans and mice with the SCA1 disease. The molecular chaperone heat-shock proteins (HSPs) are known to modulate polyglutamine protein aggregation and are neuroprotective. Since HSPs are induced under stress, we explored the effects of focused laser light induced hyperthermia (HT) on HSP-mediated protection against ATXN1 toxicity. We first tested the effects of HT in a cell culture model and found that HT induced Hsp70 and increased its localization to nuclear inclusions in HeLa cells expressing GFP-ATXN1[82Q]. HT treatment decreased ATXN1 aggregation by making GFP-ATXN1[82Q] inclusions smaller and more numerous compared to non-treated cells. Further, we tested our HT approach in vivo using a transgenic (Tg) mouse model of SCA1. We found that our laser method increased cerebellar temperature from 38 to 40 °C without causing any neuronal damage or inflammatory response. Interestingly, mild cerebellar HT stimulated the production of Hsp70 to a significant level. Furthermore, multiple exposure of focused cerebellar laser light induced HT to heterozygous SCA1 transgenic (Tg) mice significantly suppressed the SCA1 phenotype as compared to sham-treated control animals. Moreover, in treated SCA1 Tg mice, the levels of PC calcium signaling/buffering protein calbindin-D28k markedly increased followed by a reduction in PC neurodegenerative morphology. Taken together, our data suggest that laser light induced HT is a novel non-invasive approach to treat SCA1 and maybe other polyglutamine disorders.</description><subject>Animals</subject><subject>Ataxin-1</subject><subject>Ataxins</subject><subject>Biomedical and Life Sciences</subject><subject>Biomedicine</subject><subject>Cell Nucleus - metabolism</subject><subject>Cerebellum - pathology</subject><subject>Cerebellum - physiopathology</subject><subject>Disease Models, Animal</subject><subject>HeLa Cells</subject><subject>HSP70 Heat-Shock Proteins - metabolism</subject><subject>Humans</subject><subject>Hyperthermia, Induced - methods</subject><subject>Immunohistochemistry</subject><subject>Laser Therapy - methods</subject><subject>Mice, Transgenic</subject><subject>Motor Activity - physiology</subject><subject>Nerve Tissue Proteins - genetics</subject><subject>Nerve Tissue Proteins - metabolism</subject><subject>Neurobiology</subject><subject>Neuroimmunomodulation - physiology</subject><subject>Neurology</subject><subject>Neurosciences</subject><subject>Nuclear Proteins - genetics</subject><subject>Nuclear Proteins - metabolism</subject><subject>Original Paper</subject><subject>S100 Calcium Binding Protein beta Subunit - metabolism</subject><subject>Spinocerebellar Ataxias - pathology</subject><subject>Spinocerebellar Ataxias - physiopathology</subject><subject>Spinocerebellar Ataxias - therapy</subject><subject>Temperature</subject><subject>Treatment Outcome</subject><subject>Vacuoles - pathology</subject><subject>Vacuoles - physiology</subject><issn>1473-4222</issn><issn>1473-4230</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNqNkU9v1DAQxS0EoqXwAbggS1y4BMZ_EmeP1ULpSouo1N4txxnvpkrixU6QcuWTM8uWCiEhcRlbmt-8mafH2GsB7wWA-ZCFVEIUIHQBpakK8YSdC21UoaWCp49_Kc_Yi5zvAaQEbZ6zM6lXCkDBOftxFf2cseVrTNhg37vEty4j1W63n_hmbGdP7evlgGnaYxo6xzfDIcXvmPntMhymOGTuxpbfuGkf-7hbeAz8JvbLrp8nN3Qj8o9dRhLlt-tLwbuRO_4l0laqLfYv2bPg-oyvHt4Ldnf16W59XWy_ft6sL7eF16qeika1rVYm-CqAcz40NazQIAZTN5UOqKvQSCRXlfKl8SCMLHXZaDSaGFQX7N1Jlm7_NmOe7NBlf3Q8Ih1jRVlVtdKiXP0PCmWtNVSEvv0LvY9zGsnHL4qiMbUiSpwon2LOCYM9pG5wabEC7DFKe4rSEm-PUVpBM28elOdmwPZx4nd2BMgTkKk17jD9sfqfqj8BDSapJQ</recordid><startdate>20141001</startdate><enddate>20141001</enddate><creator>Hearst, Scoty M.</creator><creator>Shao, Qingmei</creator><creator>Lopez, Mariper</creator><creator>Raucher, Drazen</creator><creator>Vig, Parminder J. 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S.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Nursing & Allied Health Database</collection><collection>Neurosciences Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Psychology Database (Alumni)</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>ProQuest Central</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Nursing & Allied Health Database (Alumni Edition)</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Psychology Database</collection><collection>Nursing & Allied Health Premium</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>ProQuest One Psychology</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><jtitle>Cerebellum (London, England)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hearst, Scoty M.</au><au>Shao, Qingmei</au><au>Lopez, Mariper</au><au>Raucher, Drazen</au><au>Vig, Parminder J. S.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Focused Cerebellar Laser Light Induced Hyperthermia Improves Symptoms and Pathology of Polyglutamine Disease SCA1 in a Mouse Model</atitle><jtitle>Cerebellum (London, England)</jtitle><stitle>Cerebellum</stitle><addtitle>Cerebellum</addtitle><date>2014-10-01</date><risdate>2014</risdate><volume>13</volume><issue>5</issue><spage>596</spage><epage>606</epage><pages>596-606</pages><issn>1473-4222</issn><eissn>1473-4230</eissn><abstract>Spinocerebellar ataxia 1 (SCA1) results from pathologic glutamine expansion in the ataxin-1 protein (ATXN1). This misfolded ATXN1 causes severe Purkinje cell (PC) loss and cerebellar ataxia in both humans and mice with the SCA1 disease. The molecular chaperone heat-shock proteins (HSPs) are known to modulate polyglutamine protein aggregation and are neuroprotective. Since HSPs are induced under stress, we explored the effects of focused laser light induced hyperthermia (HT) on HSP-mediated protection against ATXN1 toxicity. We first tested the effects of HT in a cell culture model and found that HT induced Hsp70 and increased its localization to nuclear inclusions in HeLa cells expressing GFP-ATXN1[82Q]. HT treatment decreased ATXN1 aggregation by making GFP-ATXN1[82Q] inclusions smaller and more numerous compared to non-treated cells. Further, we tested our HT approach in vivo using a transgenic (Tg) mouse model of SCA1. We found that our laser method increased cerebellar temperature from 38 to 40 °C without causing any neuronal damage or inflammatory response. Interestingly, mild cerebellar HT stimulated the production of Hsp70 to a significant level. Furthermore, multiple exposure of focused cerebellar laser light induced HT to heterozygous SCA1 transgenic (Tg) mice significantly suppressed the SCA1 phenotype as compared to sham-treated control animals. Moreover, in treated SCA1 Tg mice, the levels of PC calcium signaling/buffering protein calbindin-D28k markedly increased followed by a reduction in PC neurodegenerative morphology. Taken together, our data suggest that laser light induced HT is a novel non-invasive approach to treat SCA1 and maybe other polyglutamine disorders.</abstract><cop>Boston</cop><pub>Springer US</pub><pmid>24930030</pmid><doi>10.1007/s12311-014-0576-1</doi><tpages>11</tpages></addata></record> |
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subjects | Animals Ataxin-1 Ataxins Biomedical and Life Sciences Biomedicine Cell Nucleus - metabolism Cerebellum - pathology Cerebellum - physiopathology Disease Models, Animal HeLa Cells HSP70 Heat-Shock Proteins - metabolism Humans Hyperthermia, Induced - methods Immunohistochemistry Laser Therapy - methods Mice, Transgenic Motor Activity - physiology Nerve Tissue Proteins - genetics Nerve Tissue Proteins - metabolism Neurobiology Neuroimmunomodulation - physiology Neurology Neurosciences Nuclear Proteins - genetics Nuclear Proteins - metabolism Original Paper S100 Calcium Binding Protein beta Subunit - metabolism Spinocerebellar Ataxias - pathology Spinocerebellar Ataxias - physiopathology Spinocerebellar Ataxias - therapy Temperature Treatment Outcome Vacuoles - pathology Vacuoles - physiology |
title | Focused Cerebellar Laser Light Induced Hyperthermia Improves Symptoms and Pathology of Polyglutamine Disease SCA1 in a Mouse Model |
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