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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 ...

  • Elsevier,2015
  • electronicrdacarrier

Numbers

  • LIBRIS-ID:oai:DiVA.org:liu-122341
  • https://urn.kb.se/resolve?urn=urn:nbn:se:liu:diva-122341URI
  • https://doi.org/10.1016/j.nbd.2015.08.024DOI

Supplementary language notes

  • Language:English
  • Summary in:English

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  • Subject category:ref swepub-contenttype
  • Subject category:art swepub-publicationtype

Notes

  • 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)
  • Civitelli, LiviaLinköpings universitet,Avdelningen för neuro- och inflammationsvetenskap,Medicinska fakulteten(Swepub:liu)livci24 (author)
  • Nath, SangeetaLinköpings universitet,Avdelningen för cellbiologi,Medicinska fakulteten(Swepub:liu)sanna47 (author)
  • Sandin, LinneaLinköpings universitet,Avdelningen för cellbiologi,Medicinska fakulteten(Swepub:liu)linsa35 (author)
  • Janefjord, CamillaLinköpings universitet,Avdelningen för neuro- och inflammationsvetenskap,Medicinska fakulteten(Swepub:liu)camja19 (author)
  • McCann, HeatherNeuroscience Research Australia and University of New South Wales, Australia (author)
  • Zetterberg, HenrikClinical Neurochemistry Laboratory, Department of Neuroscience and Physiology, Sahlgrenska University Hospital, Mölndal, Sweden / UCL Institute of Neurology, Queen Square, London, United Kingdom (author)
  • Blennow, KajClinical Neurochemistry Laboratory, Department of Neuroscience and Physiology, Sahlgrenska University Hospital, Mölndal, Sweden (author)
  • Halliday, GlendaUCL Institute of Neurology, Queen Square, London, United Kingdom (author)
  • Brorsson, Ann-ChristinLinköpings universitet,Molekylär Bioteknik,Tekniska fakulteten(Swepub:liu)annbr05 (author)
  • Kågedal, KatarinaLinköpings universitet,Avdelningen för cellbiologi,Medicinska fakulteten(Swepub:liu)katka10 (author)
  • Linköpings universitetMolekylär Bioteknik (creator_code:org_t)

Related titles

  • In:Neurobiology of Disease: Elsevier83, s. 122-1330969-99611095-953X

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