Detection of Protein Aggregates in Brain and Cerebrospinal Fluid Derived from Multiple Sclerosis Patients
Studies of the properties of soluble oligomers species of amyloidogenic proteins, derived from different proteins with little sequence homology, have indicated that they share a common structure and may share similar pathogenic mechanisms. Amyloid β, tau protein as well as amyloid precursor protein...
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| Format: | Article |
| Language: | English |
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Frontiers Media S.A.
2014-12-01
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| Series: | Frontiers in Neurology |
| Subjects: | |
| Online Access: | http://journal.frontiersin.org/Journal/10.3389/fneur.2014.00251/full |
| _version_ | 1818202752190251008 |
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| author | Monique eDavid Mourad eTayebi |
| author_facet | Monique eDavid Mourad eTayebi |
| author_sort | Monique eDavid |
| collection | DOAJ |
| description | Studies of the properties of soluble oligomers species of amyloidogenic proteins, derived from different proteins with little sequence homology, have indicated that they share a common structure and may share similar pathogenic mechanisms. Amyloid β, tau protein as well as amyloid precursor protein normally associated with Alzheimer’s disease and Parkinson’s disease were found in lesions and plaques of Multiple Sclerosis patients. The Objective of the study is to investigate whether brain and CSF samples derived from Multiple Sclerosis patients demonstrate the presence of soluble oligomers normally associated with protein misfolding diseases such as Alzheimer’s disease.We have used anti-oligomer monoclonal antibodies to immunodetect soluble oligomers in CSF and brain tissues derived from Multiple Sclerosis patients. In this report, we describe the presence of soluble oligomers in the brain tissue and cerebral spinal fluid of Multiple Sclerosis patients detected with our monoclonal anti-oligomer antibodies with Western blot. These results might suggest that protein aggregation plays a role in Multiple Sclerosis pathogenesis although further and more refined studies are needed to confirm the role of soluble aggregates in Multiple Sclerosis. |
| first_indexed | 2024-12-12T03:14:26Z |
| format | Article |
| id | doaj.art-3cb4bc9801204ee196f3026e9c6cf911 |
| institution | Directory Open Access Journal |
| issn | 1664-2295 |
| language | English |
| last_indexed | 2024-12-12T03:14:26Z |
| publishDate | 2014-12-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Neurology |
| spelling | doaj.art-3cb4bc9801204ee196f3026e9c6cf9112022-12-22T00:40:20ZengFrontiers Media S.A.Frontiers in Neurology1664-22952014-12-01510.3389/fneur.2014.0025189415Detection of Protein Aggregates in Brain and Cerebrospinal Fluid Derived from Multiple Sclerosis PatientsMonique eDavid0Mourad eTayebi1PrioCam LLCThe University of SurreyStudies of the properties of soluble oligomers species of amyloidogenic proteins, derived from different proteins with little sequence homology, have indicated that they share a common structure and may share similar pathogenic mechanisms. Amyloid β, tau protein as well as amyloid precursor protein normally associated with Alzheimer’s disease and Parkinson’s disease were found in lesions and plaques of Multiple Sclerosis patients. The Objective of the study is to investigate whether brain and CSF samples derived from Multiple Sclerosis patients demonstrate the presence of soluble oligomers normally associated with protein misfolding diseases such as Alzheimer’s disease.We have used anti-oligomer monoclonal antibodies to immunodetect soluble oligomers in CSF and brain tissues derived from Multiple Sclerosis patients. In this report, we describe the presence of soluble oligomers in the brain tissue and cerebral spinal fluid of Multiple Sclerosis patients detected with our monoclonal anti-oligomer antibodies with Western blot. These results might suggest that protein aggregation plays a role in Multiple Sclerosis pathogenesis although further and more refined studies are needed to confirm the role of soluble aggregates in Multiple Sclerosis.http://journal.frontiersin.org/Journal/10.3389/fneur.2014.00251/fullMultiple Sclerosisprotein aggregationProtein Misfolding DiseaseSoluble Oligomersanti-oligomer antibodies |
| spellingShingle | Monique eDavid Mourad eTayebi Detection of Protein Aggregates in Brain and Cerebrospinal Fluid Derived from Multiple Sclerosis Patients Frontiers in Neurology Multiple Sclerosis protein aggregation Protein Misfolding Disease Soluble Oligomers anti-oligomer antibodies |
| title | Detection of Protein Aggregates in Brain and Cerebrospinal Fluid Derived from Multiple Sclerosis Patients |
| title_full | Detection of Protein Aggregates in Brain and Cerebrospinal Fluid Derived from Multiple Sclerosis Patients |
| title_fullStr | Detection of Protein Aggregates in Brain and Cerebrospinal Fluid Derived from Multiple Sclerosis Patients |
| title_full_unstemmed | Detection of Protein Aggregates in Brain and Cerebrospinal Fluid Derived from Multiple Sclerosis Patients |
| title_short | Detection of Protein Aggregates in Brain and Cerebrospinal Fluid Derived from Multiple Sclerosis Patients |
| title_sort | detection of protein aggregates in brain and cerebrospinal fluid derived from multiple sclerosis patients |
| topic | Multiple Sclerosis protein aggregation Protein Misfolding Disease Soluble Oligomers anti-oligomer antibodies |
| url | http://journal.frontiersin.org/Journal/10.3389/fneur.2014.00251/full |
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