Amyloid proteins and their role in multiple sclerosis. Considerations in the use of amyloid-PET imaging
Thioflavin T derivatives are used in positron-emission tomography (PET) studies to detect amyloid protein deposits in patients with Alzheimer disease. These tracers bind extensively to white matter, which suggests that they may be useful in studies of multiple sclerosis (MS), and that proteins resul...
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| Format: | Article |
| Language: | English |
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Frontiers Media S.A.
2016-03-01
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| Series: | Frontiers in Neurology |
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| Online Access: | http://journal.frontiersin.org/Journal/10.3389/fneur.2016.00053/full |
| _version_ | 1818085333967831040 |
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| author | Jordi A. eMatias-Guiu Celia eOreja-Guevara Maria Nieves eCabrera-Martin Teresa eMoreno-Ramos José Luis eCarreras Jorge eMatias-Guiu |
| author_facet | Jordi A. eMatias-Guiu Celia eOreja-Guevara Maria Nieves eCabrera-Martin Teresa eMoreno-Ramos José Luis eCarreras Jorge eMatias-Guiu |
| author_sort | Jordi A. eMatias-Guiu |
| collection | DOAJ |
| description | Thioflavin T derivatives are used in positron-emission tomography (PET) studies to detect amyloid protein deposits in patients with Alzheimer disease. These tracers bind extensively to white matter, which suggests that they may be useful in studies of multiple sclerosis (MS), and that proteins resulting from proteolytic processing of the amyloid precursor protein (APP) may contribute to MS. This article reviews data from both clinical and preclinical studies addressing the role of these proteins, whether they are detected in CSF studies or using PET imaging. APP is widely expressed in demyelinated axons and may have a protective effect in MS and in experimental allergic encephalomyelitis in animals. Several mechanisms associated with this increased expression may affect the degree of remyelination in MS. Amyloid-PET imaging may help determine the degree of demyelination and provide information on the molecular changes linked to APP proteolytic processing experienced by patients with MS. |
| first_indexed | 2024-12-10T20:08:08Z |
| format | Article |
| id | doaj.art-eae3538cee5a43b8baa7e6d1f465abcd |
| institution | Directory Open Access Journal |
| issn | 1664-2295 |
| language | English |
| last_indexed | 2024-12-10T20:08:08Z |
| publishDate | 2016-03-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Neurology |
| spelling | doaj.art-eae3538cee5a43b8baa7e6d1f465abcd2022-12-22T01:35:20ZengFrontiers Media S.A.Frontiers in Neurology1664-22952016-03-01710.3389/fneur.2016.00053159494Amyloid proteins and their role in multiple sclerosis. Considerations in the use of amyloid-PET imagingJordi A. eMatias-Guiu0Celia eOreja-Guevara1Maria Nieves eCabrera-Martin2Teresa eMoreno-Ramos3José Luis eCarreras4Jorge eMatias-Guiu5Hospital Clinico San Carlos. Universidad Complutense. Madrid, SpainHospital Clinico San Carlos. Universidad Complutense. Madrid, SpainHospital Clinico San Carlos, Universidad ComplutenseHospital Clinico San Carlos. Universidad Complutense. Madrid, SpainHospital Clinico San Carlos, Universidad ComplutenseHospital Clinico San Carlos. Universidad Complutense. Madrid, SpainThioflavin T derivatives are used in positron-emission tomography (PET) studies to detect amyloid protein deposits in patients with Alzheimer disease. These tracers bind extensively to white matter, which suggests that they may be useful in studies of multiple sclerosis (MS), and that proteins resulting from proteolytic processing of the amyloid precursor protein (APP) may contribute to MS. This article reviews data from both clinical and preclinical studies addressing the role of these proteins, whether they are detected in CSF studies or using PET imaging. APP is widely expressed in demyelinated axons and may have a protective effect in MS and in experimental allergic encephalomyelitis in animals. Several mechanisms associated with this increased expression may affect the degree of remyelination in MS. Amyloid-PET imaging may help determine the degree of demyelination and provide information on the molecular changes linked to APP proteolytic processing experienced by patients with MS.http://journal.frontiersin.org/Journal/10.3389/fneur.2016.00053/fullAmyloidMultiple Sclerosisbiomarkersamyloid precursor proteinwhite matterpositron emission tomography |
| spellingShingle | Jordi A. eMatias-Guiu Celia eOreja-Guevara Maria Nieves eCabrera-Martin Teresa eMoreno-Ramos José Luis eCarreras Jorge eMatias-Guiu Amyloid proteins and their role in multiple sclerosis. Considerations in the use of amyloid-PET imaging Frontiers in Neurology Amyloid Multiple Sclerosis biomarkers amyloid precursor protein white matter positron emission tomography |
| title | Amyloid proteins and their role in multiple sclerosis. Considerations in the use of amyloid-PET imaging |
| title_full | Amyloid proteins and their role in multiple sclerosis. Considerations in the use of amyloid-PET imaging |
| title_fullStr | Amyloid proteins and their role in multiple sclerosis. Considerations in the use of amyloid-PET imaging |
| title_full_unstemmed | Amyloid proteins and their role in multiple sclerosis. Considerations in the use of amyloid-PET imaging |
| title_short | Amyloid proteins and their role in multiple sclerosis. Considerations in the use of amyloid-PET imaging |
| title_sort | amyloid proteins and their role in multiple sclerosis considerations in the use of amyloid pet imaging |
| topic | Amyloid Multiple Sclerosis biomarkers amyloid precursor protein white matter positron emission tomography |
| url | http://journal.frontiersin.org/Journal/10.3389/fneur.2016.00053/full |
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