Protease-resistant SOD1 aggregates in amyotrophic lateral sclerosis demonstrated by paraffin-embedded tissue (PET) blot
Objectives The paraffin-embedded tissue (PET) blot technique followed by limited protease digestion has been established to detect protein aggregates in prion diseases, alpha-synucleopathies, and tauopathies. We analyzed whether the scope of the method can be extended to analyze aggregates in mouse...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Steinacker, Petra [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2014 |
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| Schlagwörter: |
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| Anmerkung: |
© Steinacker et al.; licensee BioMed Central Ltd. 2014 |
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| Übergeordnetes Werk: |
Enthalten in: Acta Neuropathologica Communications - London : Biomed Central, 2013, 2(2014), 1 vom: 28. Aug. |
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| Übergeordnetes Werk: |
volume:2 ; year:2014 ; number:1 ; day:28 ; month:08 |
| Links: |
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| DOI / URN: |
10.1186/s40478-014-0130-x |
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SPR036508969 |
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| 520 | |a Objectives The paraffin-embedded tissue (PET) blot technique followed by limited protease digestion has been established to detect protein aggregates in prion diseases, alpha-synucleopathies, and tauopathies. We analyzed whether the scope of the method can be extended to analyze aggregates in mouse and human tissue with amyotrophic lateral sclerosis (ALS) associated with superoxide dismutase 1 (SOD1) mutation. Methods Formalin-fixed and paraffin-embedded brain and spinal cord tissue from $ SOD1^{G93A} $ mice was first analyzed for the expression of SOD1, aggregated SOD1, ubiquitin, and p62 by convential immunohistochemistry and then used to establish the PET blot technique, limited protease digest, and immunodetection of SOD1 aggregates. The method was then transferred to spinal cord from an ALS patient with $ SOD1^{E100G} $ mutation. Results Mouse and human paraffin-embedded brain and spinal cord tissue can be blotted to membranes and stained with anti-SOD1 antibodies. The SOD1 labelling is abolished after limited proteolytic digest in controls, whereas under identical conditions SOD1 aggregates are detected the $ SOD1^{G93A} $ mouse model of ALS and in human familial ALS. The most prominent areas where aggregates could be detected are the brainstem and the anterior horn of the spinal cord. Discussion Applicability of the PET blot technique to demonstrate SOD1 aggregates in ALS tissue associated with mutations in the SOD1 gene offers a new approach to examine potential spreading of aggregates in the course of ALS. | ||
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| 700 | 1 | |a Ludolph, Albert C |4 aut | |
| 700 | 1 | |a Otto, Markus |4 aut | |
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10.1186/s40478-014-0130-x doi (DE-627)SPR036508969 (SPR)s40478-014-0130-x-e DE-627 ger DE-627 rakwb eng Steinacker, Petra verfasserin aut Protease-resistant SOD1 aggregates in amyotrophic lateral sclerosis demonstrated by paraffin-embedded tissue (PET) blot 2014 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Steinacker et al.; licensee BioMed Central Ltd. 2014 Objectives The paraffin-embedded tissue (PET) blot technique followed by limited protease digestion has been established to detect protein aggregates in prion diseases, alpha-synucleopathies, and tauopathies. We analyzed whether the scope of the method can be extended to analyze aggregates in mouse and human tissue with amyotrophic lateral sclerosis (ALS) associated with superoxide dismutase 1 (SOD1) mutation. Methods Formalin-fixed and paraffin-embedded brain and spinal cord tissue from $ SOD1^{G93A} $ mice was first analyzed for the expression of SOD1, aggregated SOD1, ubiquitin, and p62 by convential immunohistochemistry and then used to establish the PET blot technique, limited protease digest, and immunodetection of SOD1 aggregates. The method was then transferred to spinal cord from an ALS patient with $ SOD1^{E100G} $ mutation. Results Mouse and human paraffin-embedded brain and spinal cord tissue can be blotted to membranes and stained with anti-SOD1 antibodies. The SOD1 labelling is abolished after limited proteolytic digest in controls, whereas under identical conditions SOD1 aggregates are detected the $ SOD1^{G93A} $ mouse model of ALS and in human familial ALS. The most prominent areas where aggregates could be detected are the brainstem and the anterior horn of the spinal cord. Discussion Applicability of the PET blot technique to demonstrate SOD1 aggregates in ALS tissue associated with mutations in the SOD1 gene offers a new approach to examine potential spreading of aggregates in the course of ALS. Amyotrophic lateral sclerosis (dpeaa)DE-He213 Superoxide dismutase 1 (dpeaa)DE-He213 Protein aggregates (dpeaa)DE-He213 p62 (dpeaa)DE-He213 Ubiquitin (dpeaa)DE-He213 Berner, Christian aut Thal, Dietmar R aut Attems, Johannes aut Ludolph, Albert C aut Otto, Markus aut Enthalten in Acta Neuropathologica Communications London : Biomed Central, 2013 2(2014), 1 vom: 28. Aug. (DE-627)746066465 (DE-600)2715589-4 2051-5960 nnns volume:2 year:2014 number:1 day:28 month:08 https://dx.doi.org/10.1186/s40478-014-0130-x kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 2 2014 1 28 08 |
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10.1186/s40478-014-0130-x doi (DE-627)SPR036508969 (SPR)s40478-014-0130-x-e DE-627 ger DE-627 rakwb eng Steinacker, Petra verfasserin aut Protease-resistant SOD1 aggregates in amyotrophic lateral sclerosis demonstrated by paraffin-embedded tissue (PET) blot 2014 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Steinacker et al.; licensee BioMed Central Ltd. 2014 Objectives The paraffin-embedded tissue (PET) blot technique followed by limited protease digestion has been established to detect protein aggregates in prion diseases, alpha-synucleopathies, and tauopathies. We analyzed whether the scope of the method can be extended to analyze aggregates in mouse and human tissue with amyotrophic lateral sclerosis (ALS) associated with superoxide dismutase 1 (SOD1) mutation. Methods Formalin-fixed and paraffin-embedded brain and spinal cord tissue from $ SOD1^{G93A} $ mice was first analyzed for the expression of SOD1, aggregated SOD1, ubiquitin, and p62 by convential immunohistochemistry and then used to establish the PET blot technique, limited protease digest, and immunodetection of SOD1 aggregates. The method was then transferred to spinal cord from an ALS patient with $ SOD1^{E100G} $ mutation. Results Mouse and human paraffin-embedded brain and spinal cord tissue can be blotted to membranes and stained with anti-SOD1 antibodies. The SOD1 labelling is abolished after limited proteolytic digest in controls, whereas under identical conditions SOD1 aggregates are detected the $ SOD1^{G93A} $ mouse model of ALS and in human familial ALS. The most prominent areas where aggregates could be detected are the brainstem and the anterior horn of the spinal cord. Discussion Applicability of the PET blot technique to demonstrate SOD1 aggregates in ALS tissue associated with mutations in the SOD1 gene offers a new approach to examine potential spreading of aggregates in the course of ALS. Amyotrophic lateral sclerosis (dpeaa)DE-He213 Superoxide dismutase 1 (dpeaa)DE-He213 Protein aggregates (dpeaa)DE-He213 p62 (dpeaa)DE-He213 Ubiquitin (dpeaa)DE-He213 Berner, Christian aut Thal, Dietmar R aut Attems, Johannes aut Ludolph, Albert C aut Otto, Markus aut Enthalten in Acta Neuropathologica Communications London : Biomed Central, 2013 2(2014), 1 vom: 28. Aug. (DE-627)746066465 (DE-600)2715589-4 2051-5960 nnns volume:2 year:2014 number:1 day:28 month:08 https://dx.doi.org/10.1186/s40478-014-0130-x kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 2 2014 1 28 08 |
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10.1186/s40478-014-0130-x doi (DE-627)SPR036508969 (SPR)s40478-014-0130-x-e DE-627 ger DE-627 rakwb eng Steinacker, Petra verfasserin aut Protease-resistant SOD1 aggregates in amyotrophic lateral sclerosis demonstrated by paraffin-embedded tissue (PET) blot 2014 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Steinacker et al.; licensee BioMed Central Ltd. 2014 Objectives The paraffin-embedded tissue (PET) blot technique followed by limited protease digestion has been established to detect protein aggregates in prion diseases, alpha-synucleopathies, and tauopathies. We analyzed whether the scope of the method can be extended to analyze aggregates in mouse and human tissue with amyotrophic lateral sclerosis (ALS) associated with superoxide dismutase 1 (SOD1) mutation. Methods Formalin-fixed and paraffin-embedded brain and spinal cord tissue from $ SOD1^{G93A} $ mice was first analyzed for the expression of SOD1, aggregated SOD1, ubiquitin, and p62 by convential immunohistochemistry and then used to establish the PET blot technique, limited protease digest, and immunodetection of SOD1 aggregates. The method was then transferred to spinal cord from an ALS patient with $ SOD1^{E100G} $ mutation. Results Mouse and human paraffin-embedded brain and spinal cord tissue can be blotted to membranes and stained with anti-SOD1 antibodies. The SOD1 labelling is abolished after limited proteolytic digest in controls, whereas under identical conditions SOD1 aggregates are detected the $ SOD1^{G93A} $ mouse model of ALS and in human familial ALS. The most prominent areas where aggregates could be detected are the brainstem and the anterior horn of the spinal cord. Discussion Applicability of the PET blot technique to demonstrate SOD1 aggregates in ALS tissue associated with mutations in the SOD1 gene offers a new approach to examine potential spreading of aggregates in the course of ALS. Amyotrophic lateral sclerosis (dpeaa)DE-He213 Superoxide dismutase 1 (dpeaa)DE-He213 Protein aggregates (dpeaa)DE-He213 p62 (dpeaa)DE-He213 Ubiquitin (dpeaa)DE-He213 Berner, Christian aut Thal, Dietmar R aut Attems, Johannes aut Ludolph, Albert C aut Otto, Markus aut Enthalten in Acta Neuropathologica Communications London : Biomed Central, 2013 2(2014), 1 vom: 28. Aug. (DE-627)746066465 (DE-600)2715589-4 2051-5960 nnns volume:2 year:2014 number:1 day:28 month:08 https://dx.doi.org/10.1186/s40478-014-0130-x kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 2 2014 1 28 08 |
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10.1186/s40478-014-0130-x doi (DE-627)SPR036508969 (SPR)s40478-014-0130-x-e DE-627 ger DE-627 rakwb eng Steinacker, Petra verfasserin aut Protease-resistant SOD1 aggregates in amyotrophic lateral sclerosis demonstrated by paraffin-embedded tissue (PET) blot 2014 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Steinacker et al.; licensee BioMed Central Ltd. 2014 Objectives The paraffin-embedded tissue (PET) blot technique followed by limited protease digestion has been established to detect protein aggregates in prion diseases, alpha-synucleopathies, and tauopathies. We analyzed whether the scope of the method can be extended to analyze aggregates in mouse and human tissue with amyotrophic lateral sclerosis (ALS) associated with superoxide dismutase 1 (SOD1) mutation. Methods Formalin-fixed and paraffin-embedded brain and spinal cord tissue from $ SOD1^{G93A} $ mice was first analyzed for the expression of SOD1, aggregated SOD1, ubiquitin, and p62 by convential immunohistochemistry and then used to establish the PET blot technique, limited protease digest, and immunodetection of SOD1 aggregates. The method was then transferred to spinal cord from an ALS patient with $ SOD1^{E100G} $ mutation. Results Mouse and human paraffin-embedded brain and spinal cord tissue can be blotted to membranes and stained with anti-SOD1 antibodies. The SOD1 labelling is abolished after limited proteolytic digest in controls, whereas under identical conditions SOD1 aggregates are detected the $ SOD1^{G93A} $ mouse model of ALS and in human familial ALS. The most prominent areas where aggregates could be detected are the brainstem and the anterior horn of the spinal cord. Discussion Applicability of the PET blot technique to demonstrate SOD1 aggregates in ALS tissue associated with mutations in the SOD1 gene offers a new approach to examine potential spreading of aggregates in the course of ALS. Amyotrophic lateral sclerosis (dpeaa)DE-He213 Superoxide dismutase 1 (dpeaa)DE-He213 Protein aggregates (dpeaa)DE-He213 p62 (dpeaa)DE-He213 Ubiquitin (dpeaa)DE-He213 Berner, Christian aut Thal, Dietmar R aut Attems, Johannes aut Ludolph, Albert C aut Otto, Markus aut Enthalten in Acta Neuropathologica Communications London : Biomed Central, 2013 2(2014), 1 vom: 28. Aug. (DE-627)746066465 (DE-600)2715589-4 2051-5960 nnns volume:2 year:2014 number:1 day:28 month:08 https://dx.doi.org/10.1186/s40478-014-0130-x kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 2 2014 1 28 08 |
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10.1186/s40478-014-0130-x doi (DE-627)SPR036508969 (SPR)s40478-014-0130-x-e DE-627 ger DE-627 rakwb eng Steinacker, Petra verfasserin aut Protease-resistant SOD1 aggregates in amyotrophic lateral sclerosis demonstrated by paraffin-embedded tissue (PET) blot 2014 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Steinacker et al.; licensee BioMed Central Ltd. 2014 Objectives The paraffin-embedded tissue (PET) blot technique followed by limited protease digestion has been established to detect protein aggregates in prion diseases, alpha-synucleopathies, and tauopathies. We analyzed whether the scope of the method can be extended to analyze aggregates in mouse and human tissue with amyotrophic lateral sclerosis (ALS) associated with superoxide dismutase 1 (SOD1) mutation. Methods Formalin-fixed and paraffin-embedded brain and spinal cord tissue from $ SOD1^{G93A} $ mice was first analyzed for the expression of SOD1, aggregated SOD1, ubiquitin, and p62 by convential immunohistochemistry and then used to establish the PET blot technique, limited protease digest, and immunodetection of SOD1 aggregates. The method was then transferred to spinal cord from an ALS patient with $ SOD1^{E100G} $ mutation. Results Mouse and human paraffin-embedded brain and spinal cord tissue can be blotted to membranes and stained with anti-SOD1 antibodies. The SOD1 labelling is abolished after limited proteolytic digest in controls, whereas under identical conditions SOD1 aggregates are detected the $ SOD1^{G93A} $ mouse model of ALS and in human familial ALS. The most prominent areas where aggregates could be detected are the brainstem and the anterior horn of the spinal cord. Discussion Applicability of the PET blot technique to demonstrate SOD1 aggregates in ALS tissue associated with mutations in the SOD1 gene offers a new approach to examine potential spreading of aggregates in the course of ALS. Amyotrophic lateral sclerosis (dpeaa)DE-He213 Superoxide dismutase 1 (dpeaa)DE-He213 Protein aggregates (dpeaa)DE-He213 p62 (dpeaa)DE-He213 Ubiquitin (dpeaa)DE-He213 Berner, Christian aut Thal, Dietmar R aut Attems, Johannes aut Ludolph, Albert C aut Otto, Markus aut Enthalten in Acta Neuropathologica Communications London : Biomed Central, 2013 2(2014), 1 vom: 28. Aug. (DE-627)746066465 (DE-600)2715589-4 2051-5960 nnns volume:2 year:2014 number:1 day:28 month:08 https://dx.doi.org/10.1186/s40478-014-0130-x kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 2 2014 1 28 08 |
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protease-resistant sod1 aggregates in amyotrophic lateral sclerosis demonstrated by paraffin-embedded tissue (pet) blot |
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Protease-resistant SOD1 aggregates in amyotrophic lateral sclerosis demonstrated by paraffin-embedded tissue (PET) blot |
| abstract |
Objectives The paraffin-embedded tissue (PET) blot technique followed by limited protease digestion has been established to detect protein aggregates in prion diseases, alpha-synucleopathies, and tauopathies. We analyzed whether the scope of the method can be extended to analyze aggregates in mouse and human tissue with amyotrophic lateral sclerosis (ALS) associated with superoxide dismutase 1 (SOD1) mutation. Methods Formalin-fixed and paraffin-embedded brain and spinal cord tissue from $ SOD1^{G93A} $ mice was first analyzed for the expression of SOD1, aggregated SOD1, ubiquitin, and p62 by convential immunohistochemistry and then used to establish the PET blot technique, limited protease digest, and immunodetection of SOD1 aggregates. The method was then transferred to spinal cord from an ALS patient with $ SOD1^{E100G} $ mutation. Results Mouse and human paraffin-embedded brain and spinal cord tissue can be blotted to membranes and stained with anti-SOD1 antibodies. The SOD1 labelling is abolished after limited proteolytic digest in controls, whereas under identical conditions SOD1 aggregates are detected the $ SOD1^{G93A} $ mouse model of ALS and in human familial ALS. The most prominent areas where aggregates could be detected are the brainstem and the anterior horn of the spinal cord. Discussion Applicability of the PET blot technique to demonstrate SOD1 aggregates in ALS tissue associated with mutations in the SOD1 gene offers a new approach to examine potential spreading of aggregates in the course of ALS. © Steinacker et al.; licensee BioMed Central Ltd. 2014 |
| abstractGer |
Objectives The paraffin-embedded tissue (PET) blot technique followed by limited protease digestion has been established to detect protein aggregates in prion diseases, alpha-synucleopathies, and tauopathies. We analyzed whether the scope of the method can be extended to analyze aggregates in mouse and human tissue with amyotrophic lateral sclerosis (ALS) associated with superoxide dismutase 1 (SOD1) mutation. Methods Formalin-fixed and paraffin-embedded brain and spinal cord tissue from $ SOD1^{G93A} $ mice was first analyzed for the expression of SOD1, aggregated SOD1, ubiquitin, and p62 by convential immunohistochemistry and then used to establish the PET blot technique, limited protease digest, and immunodetection of SOD1 aggregates. The method was then transferred to spinal cord from an ALS patient with $ SOD1^{E100G} $ mutation. Results Mouse and human paraffin-embedded brain and spinal cord tissue can be blotted to membranes and stained with anti-SOD1 antibodies. The SOD1 labelling is abolished after limited proteolytic digest in controls, whereas under identical conditions SOD1 aggregates are detected the $ SOD1^{G93A} $ mouse model of ALS and in human familial ALS. The most prominent areas where aggregates could be detected are the brainstem and the anterior horn of the spinal cord. Discussion Applicability of the PET blot technique to demonstrate SOD1 aggregates in ALS tissue associated with mutations in the SOD1 gene offers a new approach to examine potential spreading of aggregates in the course of ALS. © Steinacker et al.; licensee BioMed Central Ltd. 2014 |
| abstract_unstemmed |
Objectives The paraffin-embedded tissue (PET) blot technique followed by limited protease digestion has been established to detect protein aggregates in prion diseases, alpha-synucleopathies, and tauopathies. We analyzed whether the scope of the method can be extended to analyze aggregates in mouse and human tissue with amyotrophic lateral sclerosis (ALS) associated with superoxide dismutase 1 (SOD1) mutation. Methods Formalin-fixed and paraffin-embedded brain and spinal cord tissue from $ SOD1^{G93A} $ mice was first analyzed for the expression of SOD1, aggregated SOD1, ubiquitin, and p62 by convential immunohistochemistry and then used to establish the PET blot technique, limited protease digest, and immunodetection of SOD1 aggregates. The method was then transferred to spinal cord from an ALS patient with $ SOD1^{E100G} $ mutation. Results Mouse and human paraffin-embedded brain and spinal cord tissue can be blotted to membranes and stained with anti-SOD1 antibodies. The SOD1 labelling is abolished after limited proteolytic digest in controls, whereas under identical conditions SOD1 aggregates are detected the $ SOD1^{G93A} $ mouse model of ALS and in human familial ALS. The most prominent areas where aggregates could be detected are the brainstem and the anterior horn of the spinal cord. Discussion Applicability of the PET blot technique to demonstrate SOD1 aggregates in ALS tissue associated with mutations in the SOD1 gene offers a new approach to examine potential spreading of aggregates in the course of ALS. © Steinacker et al.; licensee BioMed Central Ltd. 2014 |
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The most prominent areas where aggregates could be detected are the brainstem and the anterior horn of the spinal cord. 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