SOD1 aggregation in ALS mice shows simplistic test tube behavior
A longstanding challenge in studies of neurodegenerative disease has been that the pathologic protein aggregates in live tissue are not amenable to structural and kinetic analysis by conventional methods. The situation is put in focus by the current progress in demarcating protein aggregation in vit...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Lisa Lang [verfasserIn] |
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| Format: |
Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2015 |
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| Rechteinformationen: |
Nutzungsrecht: © COPYRIGHT 2015 National Academy of Sciences |
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| Schlagwörter: |
Superoxide Dismutase - chemistry Superoxide Dismutase - metabolism Amyotrophic Lateral Sclerosis - enzymology Amyotrophic Lateral Sclerosis - pathology |
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| Übergeordnetes Werk: |
Enthalten in: Proceedings of the National Academy of Sciences of the United States of America - Washington, DC : NAS, 1877, 112(2015), 32, Seite 9878-9883 |
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| Übergeordnetes Werk: |
volume:112 ; year:2015 ; number:32 ; pages:9878-9883 |
| Links: |
Volltext |
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| DOI / URN: |
10.1073/pnas.1503328112 |
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| 520 | |a A longstanding challenge in studies of neurodegenerative disease has been that the pathologic protein aggregates in live tissue are not amenable to structural and kinetic analysis by conventional methods. The situation is put in focus by the current progress in demarcating protein aggregation in vitro, exposing new mechanistic details that are now calling for quantitative in vivo comparison. In this study, we bridge this gap by presenting a direct comparison of the aggregation kinetics of the ALS-associated protein superoxide dismutase 1 (SOD1) in vitro and in transgenic mice. The results based on tissue sampling by quantitative antibody assays show that the SOD1 fibrillation kinetics in vitro mirror with remarkable accuracy the spinal cord aggregate buildup and disease progression in transgenic mice. This similarity between in vitro and in vivo data suggests that, despite the complexity of live tissue, SOD1 aggregation follows robust and simplistic rules, providing new mechanistic insights into the ALS pathology and organism-level manifestation of protein aggregation phenomena in general. | ||
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| 650 | 4 | |a Apoproteins - metabolism | |
| 650 | 4 | |a Mutation - genetics | |
| 650 | 4 | |a Spinal Cord - metabolism | |
| 650 | 4 | |a Superoxide Dismutase - metabolism | |
| 650 | 4 | |a Amyotrophic Lateral Sclerosis - enzymology | |
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10.1073/pnas.1503328112 doi PQ20160617 (DE-627)OLC1961706156 (DE-599)GBVOLC1961706156 (PRQ)g2736-eaf97218e20c91e7df44b93c499d1077ccd30c20e8845e073c32ff901562a9d53 (KEY)0583363920150000112003209878sod1aggregationinalsmiceshowssimplistictesttubebeh DE-627 ger DE-627 rakwb eng 500 DNB 570 AVZ LING fid BIODIV fid Lisa Lang verfasserin aut SOD1 aggregation in ALS mice shows simplistic test tube behavior 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier A longstanding challenge in studies of neurodegenerative disease has been that the pathologic protein aggregates in live tissue are not amenable to structural and kinetic analysis by conventional methods. The situation is put in focus by the current progress in demarcating protein aggregation in vitro, exposing new mechanistic details that are now calling for quantitative in vivo comparison. In this study, we bridge this gap by presenting a direct comparison of the aggregation kinetics of the ALS-associated protein superoxide dismutase 1 (SOD1) in vitro and in transgenic mice. The results based on tissue sampling by quantitative antibody assays show that the SOD1 fibrillation kinetics in vitro mirror with remarkable accuracy the spinal cord aggregate buildup and disease progression in transgenic mice. This similarity between in vitro and in vivo data suggests that, despite the complexity of live tissue, SOD1 aggregation follows robust and simplistic rules, providing new mechanistic insights into the ALS pathology and organism-level manifestation of protein aggregation phenomena in general. Nutzungsrecht: © COPYRIGHT 2015 National Academy of Sciences Apoproteins - chemistry Superoxide Dismutase - chemistry Apoproteins - metabolism Mutation - genetics Spinal Cord - metabolism Superoxide Dismutase - metabolism Amyotrophic Lateral Sclerosis - enzymology Amyotrophic Lateral Sclerosis - pathology Superoxide Dismutase - genetics Amyotrophic lateral sclerosis Physiological aspects Tissue Neurological disorders Comparative analysis Proteins Rodents Kinetics aggregation superoxide dismutase 1 transgenic mice Biological Sciences aggregation kinetics Per Zetterström oth Thomas Brännström oth Stefan L. Marklund oth Jens Danielsson oth Mikael Oliveberg oth Enthalten in Proceedings of the National Academy of Sciences of the United States of America Washington, DC : NAS, 1877 112(2015), 32, Seite 9878-9883 (DE-627)129505269 (DE-600)209104-5 (DE-576)014909189 0027-8424 nnns volume:112 year:2015 number:32 pages:9878-9883 http://dx.doi.org/10.1073/pnas.1503328112 Volltext http://www.pnas.org/content/112/32/9878.abstract http://www.ncbi.nlm.nih.gov/pubmed/26221023 http://search.proquest.com/docview/1704124104 http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=4538623&tool=pmcentrez&rendertype=abstract http://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-120688 GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-LING FID-BIODIV SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-MAT SSG-OLC-FOR SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-MAT SSG-OPC-FOR GBV_ILN_40 GBV_ILN_59 AR 112 2015 32 9878-9883 |
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10.1073/pnas.1503328112 doi PQ20160617 (DE-627)OLC1961706156 (DE-599)GBVOLC1961706156 (PRQ)g2736-eaf97218e20c91e7df44b93c499d1077ccd30c20e8845e073c32ff901562a9d53 (KEY)0583363920150000112003209878sod1aggregationinalsmiceshowssimplistictesttubebeh DE-627 ger DE-627 rakwb eng 500 DNB 570 AVZ LING fid BIODIV fid Lisa Lang verfasserin aut SOD1 aggregation in ALS mice shows simplistic test tube behavior 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier A longstanding challenge in studies of neurodegenerative disease has been that the pathologic protein aggregates in live tissue are not amenable to structural and kinetic analysis by conventional methods. The situation is put in focus by the current progress in demarcating protein aggregation in vitro, exposing new mechanistic details that are now calling for quantitative in vivo comparison. In this study, we bridge this gap by presenting a direct comparison of the aggregation kinetics of the ALS-associated protein superoxide dismutase 1 (SOD1) in vitro and in transgenic mice. The results based on tissue sampling by quantitative antibody assays show that the SOD1 fibrillation kinetics in vitro mirror with remarkable accuracy the spinal cord aggregate buildup and disease progression in transgenic mice. This similarity between in vitro and in vivo data suggests that, despite the complexity of live tissue, SOD1 aggregation follows robust and simplistic rules, providing new mechanistic insights into the ALS pathology and organism-level manifestation of protein aggregation phenomena in general. Nutzungsrecht: © COPYRIGHT 2015 National Academy of Sciences Apoproteins - chemistry Superoxide Dismutase - chemistry Apoproteins - metabolism Mutation - genetics Spinal Cord - metabolism Superoxide Dismutase - metabolism Amyotrophic Lateral Sclerosis - enzymology Amyotrophic Lateral Sclerosis - pathology Superoxide Dismutase - genetics Amyotrophic lateral sclerosis Physiological aspects Tissue Neurological disorders Comparative analysis Proteins Rodents Kinetics aggregation superoxide dismutase 1 transgenic mice Biological Sciences aggregation kinetics Per Zetterström oth Thomas Brännström oth Stefan L. Marklund oth Jens Danielsson oth Mikael Oliveberg oth Enthalten in Proceedings of the National Academy of Sciences of the United States of America Washington, DC : NAS, 1877 112(2015), 32, Seite 9878-9883 (DE-627)129505269 (DE-600)209104-5 (DE-576)014909189 0027-8424 nnns volume:112 year:2015 number:32 pages:9878-9883 http://dx.doi.org/10.1073/pnas.1503328112 Volltext http://www.pnas.org/content/112/32/9878.abstract http://www.ncbi.nlm.nih.gov/pubmed/26221023 http://search.proquest.com/docview/1704124104 http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=4538623&tool=pmcentrez&rendertype=abstract http://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-120688 GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-LING FID-BIODIV SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-MAT SSG-OLC-FOR SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-MAT SSG-OPC-FOR GBV_ILN_40 GBV_ILN_59 AR 112 2015 32 9878-9883 |
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10.1073/pnas.1503328112 doi PQ20160617 (DE-627)OLC1961706156 (DE-599)GBVOLC1961706156 (PRQ)g2736-eaf97218e20c91e7df44b93c499d1077ccd30c20e8845e073c32ff901562a9d53 (KEY)0583363920150000112003209878sod1aggregationinalsmiceshowssimplistictesttubebeh DE-627 ger DE-627 rakwb eng 500 DNB 570 AVZ LING fid BIODIV fid Lisa Lang verfasserin aut SOD1 aggregation in ALS mice shows simplistic test tube behavior 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier A longstanding challenge in studies of neurodegenerative disease has been that the pathologic protein aggregates in live tissue are not amenable to structural and kinetic analysis by conventional methods. The situation is put in focus by the current progress in demarcating protein aggregation in vitro, exposing new mechanistic details that are now calling for quantitative in vivo comparison. In this study, we bridge this gap by presenting a direct comparison of the aggregation kinetics of the ALS-associated protein superoxide dismutase 1 (SOD1) in vitro and in transgenic mice. The results based on tissue sampling by quantitative antibody assays show that the SOD1 fibrillation kinetics in vitro mirror with remarkable accuracy the spinal cord aggregate buildup and disease progression in transgenic mice. This similarity between in vitro and in vivo data suggests that, despite the complexity of live tissue, SOD1 aggregation follows robust and simplistic rules, providing new mechanistic insights into the ALS pathology and organism-level manifestation of protein aggregation phenomena in general. Nutzungsrecht: © COPYRIGHT 2015 National Academy of Sciences Apoproteins - chemistry Superoxide Dismutase - chemistry Apoproteins - metabolism Mutation - genetics Spinal Cord - metabolism Superoxide Dismutase - metabolism Amyotrophic Lateral Sclerosis - enzymology Amyotrophic Lateral Sclerosis - pathology Superoxide Dismutase - genetics Amyotrophic lateral sclerosis Physiological aspects Tissue Neurological disorders Comparative analysis Proteins Rodents Kinetics aggregation superoxide dismutase 1 transgenic mice Biological Sciences aggregation kinetics Per Zetterström oth Thomas Brännström oth Stefan L. Marklund oth Jens Danielsson oth Mikael Oliveberg oth Enthalten in Proceedings of the National Academy of Sciences of the United States of America Washington, DC : NAS, 1877 112(2015), 32, Seite 9878-9883 (DE-627)129505269 (DE-600)209104-5 (DE-576)014909189 0027-8424 nnns volume:112 year:2015 number:32 pages:9878-9883 http://dx.doi.org/10.1073/pnas.1503328112 Volltext http://www.pnas.org/content/112/32/9878.abstract http://www.ncbi.nlm.nih.gov/pubmed/26221023 http://search.proquest.com/docview/1704124104 http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=4538623&tool=pmcentrez&rendertype=abstract http://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-120688 GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-LING FID-BIODIV SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-MAT SSG-OLC-FOR SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-MAT SSG-OPC-FOR GBV_ILN_40 GBV_ILN_59 AR 112 2015 32 9878-9883 |
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10.1073/pnas.1503328112 doi PQ20160617 (DE-627)OLC1961706156 (DE-599)GBVOLC1961706156 (PRQ)g2736-eaf97218e20c91e7df44b93c499d1077ccd30c20e8845e073c32ff901562a9d53 (KEY)0583363920150000112003209878sod1aggregationinalsmiceshowssimplistictesttubebeh DE-627 ger DE-627 rakwb eng 500 DNB 570 AVZ LING fid BIODIV fid Lisa Lang verfasserin aut SOD1 aggregation in ALS mice shows simplistic test tube behavior 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier A longstanding challenge in studies of neurodegenerative disease has been that the pathologic protein aggregates in live tissue are not amenable to structural and kinetic analysis by conventional methods. The situation is put in focus by the current progress in demarcating protein aggregation in vitro, exposing new mechanistic details that are now calling for quantitative in vivo comparison. In this study, we bridge this gap by presenting a direct comparison of the aggregation kinetics of the ALS-associated protein superoxide dismutase 1 (SOD1) in vitro and in transgenic mice. The results based on tissue sampling by quantitative antibody assays show that the SOD1 fibrillation kinetics in vitro mirror with remarkable accuracy the spinal cord aggregate buildup and disease progression in transgenic mice. This similarity between in vitro and in vivo data suggests that, despite the complexity of live tissue, SOD1 aggregation follows robust and simplistic rules, providing new mechanistic insights into the ALS pathology and organism-level manifestation of protein aggregation phenomena in general. Nutzungsrecht: © COPYRIGHT 2015 National Academy of Sciences Apoproteins - chemistry Superoxide Dismutase - chemistry Apoproteins - metabolism Mutation - genetics Spinal Cord - metabolism Superoxide Dismutase - metabolism Amyotrophic Lateral Sclerosis - enzymology Amyotrophic Lateral Sclerosis - pathology Superoxide Dismutase - genetics Amyotrophic lateral sclerosis Physiological aspects Tissue Neurological disorders Comparative analysis Proteins Rodents Kinetics aggregation superoxide dismutase 1 transgenic mice Biological Sciences aggregation kinetics Per Zetterström oth Thomas Brännström oth Stefan L. Marklund oth Jens Danielsson oth Mikael Oliveberg oth Enthalten in Proceedings of the National Academy of Sciences of the United States of America Washington, DC : NAS, 1877 112(2015), 32, Seite 9878-9883 (DE-627)129505269 (DE-600)209104-5 (DE-576)014909189 0027-8424 nnns volume:112 year:2015 number:32 pages:9878-9883 http://dx.doi.org/10.1073/pnas.1503328112 Volltext http://www.pnas.org/content/112/32/9878.abstract http://www.ncbi.nlm.nih.gov/pubmed/26221023 http://search.proquest.com/docview/1704124104 http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=4538623&tool=pmcentrez&rendertype=abstract http://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-120688 GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-LING FID-BIODIV SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-MAT SSG-OLC-FOR SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-MAT SSG-OPC-FOR GBV_ILN_40 GBV_ILN_59 AR 112 2015 32 9878-9883 |
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10.1073/pnas.1503328112 doi PQ20160617 (DE-627)OLC1961706156 (DE-599)GBVOLC1961706156 (PRQ)g2736-eaf97218e20c91e7df44b93c499d1077ccd30c20e8845e073c32ff901562a9d53 (KEY)0583363920150000112003209878sod1aggregationinalsmiceshowssimplistictesttubebeh DE-627 ger DE-627 rakwb eng 500 DNB 570 AVZ LING fid BIODIV fid Lisa Lang verfasserin aut SOD1 aggregation in ALS mice shows simplistic test tube behavior 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier A longstanding challenge in studies of neurodegenerative disease has been that the pathologic protein aggregates in live tissue are not amenable to structural and kinetic analysis by conventional methods. The situation is put in focus by the current progress in demarcating protein aggregation in vitro, exposing new mechanistic details that are now calling for quantitative in vivo comparison. In this study, we bridge this gap by presenting a direct comparison of the aggregation kinetics of the ALS-associated protein superoxide dismutase 1 (SOD1) in vitro and in transgenic mice. The results based on tissue sampling by quantitative antibody assays show that the SOD1 fibrillation kinetics in vitro mirror with remarkable accuracy the spinal cord aggregate buildup and disease progression in transgenic mice. This similarity between in vitro and in vivo data suggests that, despite the complexity of live tissue, SOD1 aggregation follows robust and simplistic rules, providing new mechanistic insights into the ALS pathology and organism-level manifestation of protein aggregation phenomena in general. Nutzungsrecht: © COPYRIGHT 2015 National Academy of Sciences Apoproteins - chemistry Superoxide Dismutase - chemistry Apoproteins - metabolism Mutation - genetics Spinal Cord - metabolism Superoxide Dismutase - metabolism Amyotrophic Lateral Sclerosis - enzymology Amyotrophic Lateral Sclerosis - pathology Superoxide Dismutase - genetics Amyotrophic lateral sclerosis Physiological aspects Tissue Neurological disorders Comparative analysis Proteins Rodents Kinetics aggregation superoxide dismutase 1 transgenic mice Biological Sciences aggregation kinetics Per Zetterström oth Thomas Brännström oth Stefan L. Marklund oth Jens Danielsson oth Mikael Oliveberg oth Enthalten in Proceedings of the National Academy of Sciences of the United States of America Washington, DC : NAS, 1877 112(2015), 32, Seite 9878-9883 (DE-627)129505269 (DE-600)209104-5 (DE-576)014909189 0027-8424 nnns volume:112 year:2015 number:32 pages:9878-9883 http://dx.doi.org/10.1073/pnas.1503328112 Volltext http://www.pnas.org/content/112/32/9878.abstract http://www.ncbi.nlm.nih.gov/pubmed/26221023 http://search.proquest.com/docview/1704124104 http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=4538623&tool=pmcentrez&rendertype=abstract http://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-120688 GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-LING FID-BIODIV SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-MAT SSG-OLC-FOR SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-MAT SSG-OPC-FOR GBV_ILN_40 GBV_ILN_59 AR 112 2015 32 9878-9883 |
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SOD1 aggregation in ALS mice shows simplistic test tube behavior |
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A longstanding challenge in studies of neurodegenerative disease has been that the pathologic protein aggregates in live tissue are not amenable to structural and kinetic analysis by conventional methods. The situation is put in focus by the current progress in demarcating protein aggregation in vitro, exposing new mechanistic details that are now calling for quantitative in vivo comparison. In this study, we bridge this gap by presenting a direct comparison of the aggregation kinetics of the ALS-associated protein superoxide dismutase 1 (SOD1) in vitro and in transgenic mice. The results based on tissue sampling by quantitative antibody assays show that the SOD1 fibrillation kinetics in vitro mirror with remarkable accuracy the spinal cord aggregate buildup and disease progression in transgenic mice. This similarity between in vitro and in vivo data suggests that, despite the complexity of live tissue, SOD1 aggregation follows robust and simplistic rules, providing new mechanistic insights into the ALS pathology and organism-level manifestation of protein aggregation phenomena in general. |
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A longstanding challenge in studies of neurodegenerative disease has been that the pathologic protein aggregates in live tissue are not amenable to structural and kinetic analysis by conventional methods. The situation is put in focus by the current progress in demarcating protein aggregation in vitro, exposing new mechanistic details that are now calling for quantitative in vivo comparison. In this study, we bridge this gap by presenting a direct comparison of the aggregation kinetics of the ALS-associated protein superoxide dismutase 1 (SOD1) in vitro and in transgenic mice. The results based on tissue sampling by quantitative antibody assays show that the SOD1 fibrillation kinetics in vitro mirror with remarkable accuracy the spinal cord aggregate buildup and disease progression in transgenic mice. This similarity between in vitro and in vivo data suggests that, despite the complexity of live tissue, SOD1 aggregation follows robust and simplistic rules, providing new mechanistic insights into the ALS pathology and organism-level manifestation of protein aggregation phenomena in general. |
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A longstanding challenge in studies of neurodegenerative disease has been that the pathologic protein aggregates in live tissue are not amenable to structural and kinetic analysis by conventional methods. The situation is put in focus by the current progress in demarcating protein aggregation in vitro, exposing new mechanistic details that are now calling for quantitative in vivo comparison. In this study, we bridge this gap by presenting a direct comparison of the aggregation kinetics of the ALS-associated protein superoxide dismutase 1 (SOD1) in vitro and in transgenic mice. The results based on tissue sampling by quantitative antibody assays show that the SOD1 fibrillation kinetics in vitro mirror with remarkable accuracy the spinal cord aggregate buildup and disease progression in transgenic mice. This similarity between in vitro and in vivo data suggests that, despite the complexity of live tissue, SOD1 aggregation follows robust and simplistic rules, providing new mechanistic insights into the ALS pathology and organism-level manifestation of protein aggregation phenomena in general. |
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SOD1 aggregation in ALS mice shows simplistic test tube behavior |
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The situation is put in focus by the current progress in demarcating protein aggregation in vitro, exposing new mechanistic details that are now calling for quantitative in vivo comparison. In this study, we bridge this gap by presenting a direct comparison of the aggregation kinetics of the ALS-associated protein superoxide dismutase 1 (SOD1) in vitro and in transgenic mice. The results based on tissue sampling by quantitative antibody assays show that the SOD1 fibrillation kinetics in vitro mirror with remarkable accuracy the spinal cord aggregate buildup and disease progression in transgenic mice. 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