Reference : The non-core regions of human lysozyme amyloid fibrils influence cytotoxicity.
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
The non-core regions of human lysozyme amyloid fibrils influence cytotoxicity.
Mossuto, Maria F [> > > >]
Dhulesia, Anne [> > > >]
Devlin, Glyn [> > > >]
Frare, Erica [> > > >]
Kumita, Janet R [> > > >]
Polverino de Laureto, Patrizia [ > > ]
Dumoulin, Mireille mailto [Université de Liège - ULiège > Département des sciences de la vie > Enzymologie et repliement des protéines >]
Fontana, Angelo [> > > >]
Dobson, Christopher M [> > > >]
Salvatella, Xavier [> > > >]
Journal of Molecular Biology
Academic Press
Yes (verified by ORBi)
United Kingdom
[en] Amyloid/chemistry/toxicity ; Cell Line ; Cell Survival ; Humans ; Microscopy, Electron, Transmission ; Muramidase/chemistry/toxicity ; Neurons/metabolism/physiology ; Protein Stability ; Spectrophotometry, Infrared ; Tetrazolium Salts/metabolism ; Thiazoles/metabolism
[en] Identifying the cause of the cytotoxicity of species populated during amyloid formation is crucial to understand the molecular basis of protein deposition diseases. We have examined different types of aggregates formed by lysozyme, a protein found as fibrillar deposits in patients with familial systemic amyloidosis, by infrared spectroscopy, transmission electron microscopy, and depolymerization experiments, and analyzed how they affect cell viability. We have characterized two types of human lysozyme amyloid structures formed in vitro that differ in morphology, molecular structure, stability, and size of the cross-beta core. Of particular interest is that the fibrils with a smaller core generate a significant cytotoxic effect. These findings indicate that protein aggregation can give rise to species with different degree of cytotoxicity due to intrinsic differences in their physicochemical properties.
Copyright (c) 2010 Elsevier Ltd. All rights reserved.

File(s) associated to this reference

Fulltext file(s):

Open access
Mossuto_2010.pdfPublisher postprint1.68 MBView/Open

Bookmark and Share SFX Query

All documents in ORBi are protected by a user license.