The Physiological Roles of Amyloid-β Peptide Hint at New Ways to Treat Alzheimer's Disease
Amyloid-ß (Aß) is best known as the misfolded peptide that is involved in the pathogenesis of Alzheimer's disease (AD), and it is currently the primary therapeutic target in attempts to arrest the course of this disease. This notoriety has overshadowed evidence that Aß serves several important...
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| Format: | Article |
| Language: | English |
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Frontiers Media S.A.
2018-04-01
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| Series: | Frontiers in Aging Neuroscience |
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| Online Access: | http://journal.frontiersin.org/article/10.3389/fnagi.2018.00118/full |
| _version_ | 1817994517881552896 |
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| author | Holly M. Brothers Maya L. Gosztyla Stephen R. Robinson |
| author_facet | Holly M. Brothers Maya L. Gosztyla Stephen R. Robinson |
| author_sort | Holly M. Brothers |
| collection | DOAJ |
| description | Amyloid-ß (Aß) is best known as the misfolded peptide that is involved in the pathogenesis of Alzheimer's disease (AD), and it is currently the primary therapeutic target in attempts to arrest the course of this disease. This notoriety has overshadowed evidence that Aß serves several important physiological functions. Aß is present throughout the lifespan, it has been found in all vertebrates examined thus far, and its molecular sequence shows a high degree of conservation. These features are typical of a factor that contributes significantly to biological fitness, and this suggestion has been supported by evidence of functions that are beneficial for the brain. The putative roles of Aß include protecting the body from infections, repairing leaks in the blood-brain barrier, promoting recovery from injury, and regulating synaptic function. Evidence for these beneficial roles comes from in vitro and in vivo studies, which have shown that the cellular production of Aß rapidly increases in response to a physiological challenge and often diminishes upon recovery. These roles are further supported by the adverse outcomes of clinical trials that have attempted to deplete Aß in order to treat AD. We suggest that anti-Aß therapies will produce fewer adverse effects if the known triggers of Aß deposition (e.g., pathogens, hypertension, and diabetes) are addressed first. |
| first_indexed | 2024-04-14T01:53:57Z |
| format | Article |
| id | doaj.art-fb83d494a2614fecbafcfe343a6283da |
| institution | Directory Open Access Journal |
| issn | 1663-4365 |
| language | English |
| last_indexed | 2024-04-14T01:53:57Z |
| publishDate | 2018-04-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Aging Neuroscience |
| spelling | doaj.art-fb83d494a2614fecbafcfe343a6283da2022-12-22T02:19:13ZengFrontiers Media S.A.Frontiers in Aging Neuroscience1663-43652018-04-011010.3389/fnagi.2018.00118362212The Physiological Roles of Amyloid-β Peptide Hint at New Ways to Treat Alzheimer's DiseaseHolly M. Brothers0Maya L. Gosztyla1Stephen R. Robinson2Department of Psychology, The Ohio State University Columbus, Columbus, OH, United StatesDepartment of Neuroscience, The Ohio State University Columbus, Columbus, OH, United StatesDiscipline of Psychology, School of Health and Biomedical Sciences, RMIT University, Melbourne, VIC, AustraliaAmyloid-ß (Aß) is best known as the misfolded peptide that is involved in the pathogenesis of Alzheimer's disease (AD), and it is currently the primary therapeutic target in attempts to arrest the course of this disease. This notoriety has overshadowed evidence that Aß serves several important physiological functions. Aß is present throughout the lifespan, it has been found in all vertebrates examined thus far, and its molecular sequence shows a high degree of conservation. These features are typical of a factor that contributes significantly to biological fitness, and this suggestion has been supported by evidence of functions that are beneficial for the brain. The putative roles of Aß include protecting the body from infections, repairing leaks in the blood-brain barrier, promoting recovery from injury, and regulating synaptic function. Evidence for these beneficial roles comes from in vitro and in vivo studies, which have shown that the cellular production of Aß rapidly increases in response to a physiological challenge and often diminishes upon recovery. These roles are further supported by the adverse outcomes of clinical trials that have attempted to deplete Aß in order to treat AD. We suggest that anti-Aß therapies will produce fewer adverse effects if the known triggers of Aß deposition (e.g., pathogens, hypertension, and diabetes) are addressed first.http://journal.frontiersin.org/article/10.3389/fnagi.2018.00118/fullinfectionantimicrobialcancertraumatic injurycerebrovascularimmune system |
| spellingShingle | Holly M. Brothers Maya L. Gosztyla Stephen R. Robinson The Physiological Roles of Amyloid-β Peptide Hint at New Ways to Treat Alzheimer's Disease Frontiers in Aging Neuroscience infection antimicrobial cancer traumatic injury cerebrovascular immune system |
| title | The Physiological Roles of Amyloid-β Peptide Hint at New Ways to Treat Alzheimer's Disease |
| title_full | The Physiological Roles of Amyloid-β Peptide Hint at New Ways to Treat Alzheimer's Disease |
| title_fullStr | The Physiological Roles of Amyloid-β Peptide Hint at New Ways to Treat Alzheimer's Disease |
| title_full_unstemmed | The Physiological Roles of Amyloid-β Peptide Hint at New Ways to Treat Alzheimer's Disease |
| title_short | The Physiological Roles of Amyloid-β Peptide Hint at New Ways to Treat Alzheimer's Disease |
| title_sort | physiological roles of amyloid β peptide hint at new ways to treat alzheimer s disease |
| topic | infection antimicrobial cancer traumatic injury cerebrovascular immune system |
| url | http://journal.frontiersin.org/article/10.3389/fnagi.2018.00118/full |
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