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Protective properti...
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Helmfors, LindaLinköpings universitet,Molekylär Bioteknik,Tekniska fakulteten
(author)
Protective properties of lysozyme on β-amyloid pathology : implications for Alzheimer disease
- Article/chapterEnglish2015
Publisher, publication year, extent ...
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Elsevier,2015
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electronicrdacarrier
Numbers
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LIBRIS-ID:oai:DiVA.org:liu-122341
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https://urn.kb.se/resolve?urn=urn:nbn:se:liu:diva-122341URI
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https://doi.org/10.1016/j.nbd.2015.08.024DOI
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Language:English
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Summary in:English
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Subject category:ref swepub-contenttype
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Subject category:art swepub-publicationtype
Notes
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The hallmarks of Alzheimer disease are amyloid-β plaques and neurofibrillary tangles accompanied by signs of neuroinflammation. Lysozyme is a major player in the innate immune system and has recently been shown to prevent the aggregation of amyloid-β1-40 in vitro. In this study we found that patients with Alzheimer disease have increased lysozyme levels in the cerebrospinal fluid and lysozyme co-localized with amyloid-β in plaques. In Drosophila neuronal co-expression of lysozyme and amyloid-β1-42 reduced the formation of soluble and insoluble amyloid-β species, prolonged survival and improved the activity of amyloid-β1-42 transgenic flies. This suggests that lysozyme levels rise in Alzheimer disease as a compensatory response to amyloid-β increases and aggregation. In support of this, in vitro aggregation assays revealed that lysozyme associates with amyloid-β1-42 and alters its aggregation pathway to counteract the formation of toxic amyloid-β species. Overall, these studies establish a protective role for lysozyme against amyloid-β associated toxicities and identify increased lysozyme in patients with Alzheimer disease. Therefore, lysozyme has potential as a new biomarker as well as a therapeutic target for Alzheimer disease.
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Boman, AndreaLinköpings universitet,Avdelningen för cellbiologi,Medicinska fakulteten(Swepub:liu)andar41
(author)
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Civitelli, LiviaLinköpings universitet,Avdelningen för neuro- och inflammationsvetenskap,Medicinska fakulteten(Swepub:liu)livci24
(author)
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Nath, SangeetaLinköpings universitet,Avdelningen för cellbiologi,Medicinska fakulteten(Swepub:liu)sanna47
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Sandin, LinneaLinköpings universitet,Avdelningen för cellbiologi,Medicinska fakulteten(Swepub:liu)linsa35
(author)
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Janefjord, CamillaLinköpings universitet,Avdelningen för neuro- och inflammationsvetenskap,Medicinska fakulteten(Swepub:liu)camja19
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McCann, HeatherNeuroscience Research Australia and University of New South Wales, Australia
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Zetterberg, HenrikClinical Neurochemistry Laboratory, Department of Neuroscience and Physiology, Sahlgrenska University Hospital, Mölndal, Sweden / UCL Institute of Neurology, Queen Square, London, United Kingdom
(author)
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Blennow, KajClinical Neurochemistry Laboratory, Department of Neuroscience and Physiology, Sahlgrenska University Hospital, Mölndal, Sweden
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Halliday, GlendaUCL Institute of Neurology, Queen Square, London, United Kingdom
(author)
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Brorsson, Ann-ChristinLinköpings universitet,Molekylär Bioteknik,Tekniska fakulteten(Swepub:liu)annbr05
(author)
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Kågedal, KatarinaLinköpings universitet,Avdelningen för cellbiologi,Medicinska fakulteten(Swepub:liu)katka10
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Linköpings universitetMolekylär Bioteknik
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In:Neurobiology of Disease: Elsevier83, s. 122-1330969-99611095-953X
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Helmfors, Linda
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Boman, Andrea
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Civitelli, Livia
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Nath, Sangeeta
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Sandin, Linnea
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McCann, Heather
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Zetterberg, Henr ...
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Blennow, Kaj
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Linköping University