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Protective properties of lysozyme on β-amyloid pathology : implications for Alzheimer disease

Helmfors, Linda (author)
Linköpings universitet,Molekylär Bioteknik,Tekniska fakulteten
Boman, Andrea (author)
Linköpings universitet,Avdelningen för cellbiologi,Medicinska fakulteten
Civitelli, Livia (author)
Linköpings universitet,Avdelningen för neuro- och inflammationsvetenskap,Medicinska fakulteten
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Nath, Sangeeta (author)
Linköpings universitet,Avdelningen för cellbiologi,Medicinska fakulteten
Sandin, Linnea (author)
Linköpings universitet,Avdelningen för cellbiologi,Medicinska fakulteten
Janefjord, Camilla (author)
Linköpings universitet,Avdelningen för neuro- och inflammationsvetenskap,Medicinska fakulteten
McCann, Heather (author)
Neuroscience Research Australia and University of New South Wales, Australia
Zetterberg, Henrik (author)
Clinical Neurochemistry Laboratory, Department of Neuroscience and Physiology, Sahlgrenska University Hospital, Mölndal, Sweden / UCL Institute of Neurology, Queen Square, London, United Kingdom
Blennow, Kaj (author)
Clinical Neurochemistry Laboratory, Department of Neuroscience and Physiology, Sahlgrenska University Hospital, Mölndal, Sweden
Halliday, Glenda (author)
UCL Institute of Neurology, Queen Square, London, United Kingdom
Brorsson, Ann-Christin (author)
Linköpings universitet,Molekylär Bioteknik,Tekniska fakulteten
Kågedal, Katarina (author)
Linköpings universitet,Avdelningen för cellbiologi,Medicinska fakulteten
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 (creator_code:org_t)
Elsevier, 2015
2015
English.
In: Neurobiology of Disease. - : Elsevier. - 0969-9961 .- 1095-953X. ; 83, s. 122-133
  • Journal article (peer-reviewed)
Abstract Subject headings
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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.

Subject headings

MEDICIN OCH HÄLSOVETENSKAP  -- Medicinska och farmaceutiska grundvetenskaper -- Cell- och molekylärbiologi (hsv//swe)
MEDICAL AND HEALTH SCIENCES  -- Basic Medicine -- Cell and Molecular Biology (hsv//eng)
NATURVETENSKAP  -- Kemi (hsv//swe)
NATURAL SCIENCES  -- Chemical Sciences (hsv//eng)

Keyword

Lysozyme
Biomarker
Alzheimer disease
Drosophila
Aβ aggregation

Publication and Content Type

ref (subject category)
art (subject category)

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