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

Linda Helmfors, Andrea Boman, Livia Civitelli, Sangeeta Nath, Linnea Sandin, Camilla Janefjord, Heather McCann, Henrik Zetterberg, Kaj Blennow, Glenda Halliday, Ann Christin Brorsson, Katarina Kågedal

Research output: Contribution to journalArticlepeer-review

44 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)122-133
Number of pages12
JournalNeurobiology of Disease
Volume83
DOIs
Publication statusPublished - 01-11-2015

All Science Journal Classification (ASJC) codes

  • Neurology

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