Intermediate amyloid oligomers of lysozyme: Is their cytotoxicity a particular case or general rule for amyloid?
Identifieur interne : 002253 ( PubMed/Curation ); précédent : 002252; suivant : 002254Intermediate amyloid oligomers of lysozyme: Is their cytotoxicity a particular case or general rule for amyloid?
Auteurs : M. Malisauskas [Suède] ; A. Darinskas ; V V Zamotin ; A. Gharibyan ; I A Kostanyan ; L A Morozova-RocheSource :
- Biochemistry. Biokhimiia [ 0006-2979 ] ; 2006.
Descripteurs français
- KwdFr :
- Amyloïde (), Amyloïde (métabolisme), Amyloïde (toxicité), Amyloïdose (anatomopathologie), Amyloïdose (métabolisme), Amyloïdose (étiologie), Animaux, Benzothiazoles, Cellules cultivées, Cinétique, Concentration en ions d'hydrogène, Dimérisation, Equus caballus, Femelle, Humains, Lignée cellulaire tumorale, Lysozyme (), Lysozyme (métabolisme), Lysozyme (toxicité), Microscopie à force atomique (), Modèles moléculaires, Peptides bêta-amyloïdes (), Peptides bêta-amyloïdes (métabolisme), Rouge Congo (), Souris, Souris de lignée BALB C, Structure secondaire des protéines, Structures macromoléculaires (), Structures macromoléculaires (métabolisme), Survie cellulaire (), Thiazoles ().
- MESH :
- anatomopathologie : Amyloïdose.
- métabolisme : Amyloïde, Amyloïdose, Lysozyme, Peptides bêta-amyloïdes, Structures macromoléculaires.
- toxicité : Amyloïde, Lysozyme.
- étiologie : Amyloïdose.
- Amyloïde, Animaux, Benzothiazoles, Cellules cultivées, Cinétique, Concentration en ions d'hydrogène, Dimérisation, Equus caballus, Femelle, Humains, Lignée cellulaire tumorale, Lysozyme, Microscopie à force atomique, Modèles moléculaires, Peptides bêta-amyloïdes, Rouge Congo, Souris, Souris de lignée BALB C, Structure secondaire des protéines, Structures macromoléculaires, Survie cellulaire, Thiazoles.
English descriptors
- KwdEn :
- Amyloid (chemistry), Amyloid (metabolism), Amyloid (toxicity), Amyloid beta-Peptides (chemistry), Amyloid beta-Peptides (metabolism), Amyloidosis (etiology), Amyloidosis (metabolism), Amyloidosis (pathology), Animals, Benzothiazoles, Cell Line, Tumor, Cell Survival (drug effects), Cells, Cultured, Congo Red (chemistry), Dimerization, Female, Horses, Humans, Hydrogen-Ion Concentration, Kinetics, Macromolecular Substances (chemistry), Macromolecular Substances (metabolism), Mice, Mice, Inbred BALB C, Microscopy, Atomic Force (methods), Models, Molecular, Muramidase (chemistry), Muramidase (metabolism), Muramidase (toxicity), Protein Structure, Secondary, Thiazoles (chemistry).
- MESH :
- chemical , chemistry : Amyloid, Amyloid beta-Peptides, Congo Red, Macromolecular Substances, Muramidase, Thiazoles.
- chemical , metabolism : Amyloid, Amyloid beta-Peptides, Macromolecular Substances, Muramidase.
- chemical , toxicity : Amyloid, Muramidase.
- drug effects : Cell Survival.
- etiology : Amyloidosis.
- metabolism : Amyloidosis.
- methods : Microscopy, Atomic Force.
- pathology : Amyloidosis.
- Animals, Benzothiazoles, Cell Line, Tumor, Cells, Cultured, Dimerization, Female, Horses, Humans, Hydrogen-Ion Concentration, Kinetics, Mice, Mice, Inbred BALB C, Models, Molecular, Protein Structure, Secondary.
Abstract
In the current study we investigated the molecular mechanisms of cytotoxicity of amyloid oligomers of horse milk lysozyme. We have shown that lysozyme forms soluble amyloid oligomers and protofibrils during incubation at pH 2.0 and 4.5 and 57 degrees C. These structures bind the amyloid-specific dyes thioflavin T and Congo Red, and their morphology and size were analyzed by atomic force microscopy. Monomeric lysozyme and its fibrils did not affect the viability of three cell types used in our experiments including primary murine neurons and fibroblasts, as well as neuroblastoma cell line IMR-32. However, soluble amyloid oligomers of lysozyme caused death of all these cell types, as estimated by flow-cytometry counting dead cells stained with ethidium bromide. The primary cell cultures appeared to be more sensitive to amyloid than neuroblastoma cell line IMR-32. Amyloid cytotoxicity depends on the size of oligomeric particles: samples containing 20-mers formed at pH 4.5 were more toxic than tetramers and octamers present in the solution at pH 2.0. Soluble amyloid oligomers can self-assemble into doughnut-like structures; however, no correlation was observed between the amount of the doughnut-like structures in the sample and its cytotoxicity. The fact that the intermediate oligomers of such an abundant protein as lysozyme display cytotoxicity confirms a hypothesis that cytotoxicity is a common feature of protein amyloid. Inhibition of intermediate oligomer formation is crucial in preventing amyloid pathogeneses.
DOI: 10.1134/s0006297906050063
PubMed: 16732728
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<term>Amyloid beta-Peptides (metabolism)</term>
<term>Amyloidosis (etiology)</term>
<term>Amyloidosis (metabolism)</term>
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<term>Models, Molecular</term>
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<term>Amyloïdose (métabolisme)</term>
<term>Amyloïdose (étiologie)</term>
<term>Animaux</term>
<term>Benzothiazoles</term>
<term>Cellules cultivées</term>
<term>Cinétique</term>
<term>Concentration en ions d'hydrogène</term>
<term>Dimérisation</term>
<term>Equus caballus</term>
<term>Femelle</term>
<term>Humains</term>
<term>Lignée cellulaire tumorale</term>
<term>Lysozyme ()</term>
<term>Lysozyme (métabolisme)</term>
<term>Lysozyme (toxicité)</term>
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<term>Souris de lignée BALB C</term>
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<term>Cells, Cultured</term>
<term>Dimerization</term>
<term>Female</term>
<term>Horses</term>
<term>Humans</term>
<term>Hydrogen-Ion Concentration</term>
<term>Kinetics</term>
<term>Mice</term>
<term>Mice, Inbred BALB C</term>
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<term>Animaux</term>
<term>Benzothiazoles</term>
<term>Cellules cultivées</term>
<term>Cinétique</term>
<term>Concentration en ions d'hydrogène</term>
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<term>Equus caballus</term>
<term>Femelle</term>
<term>Humains</term>
<term>Lignée cellulaire tumorale</term>
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<term>Microscopie à force atomique</term>
<term>Modèles moléculaires</term>
<term>Peptides bêta-amyloïdes</term>
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<term>Souris</term>
<term>Souris de lignée BALB C</term>
<term>Structure secondaire des protéines</term>
<term>Structures macromoléculaires</term>
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<front><div type="abstract" xml:lang="en">In the current study we investigated the molecular mechanisms of cytotoxicity of amyloid oligomers of horse milk lysozyme. We have shown that lysozyme forms soluble amyloid oligomers and protofibrils during incubation at pH 2.0 and 4.5 and 57 degrees C. These structures bind the amyloid-specific dyes thioflavin T and Congo Red, and their morphology and size were analyzed by atomic force microscopy. Monomeric lysozyme and its fibrils did not affect the viability of three cell types used in our experiments including primary murine neurons and fibroblasts, as well as neuroblastoma cell line IMR-32. However, soluble amyloid oligomers of lysozyme caused death of all these cell types, as estimated by flow-cytometry counting dead cells stained with ethidium bromide. The primary cell cultures appeared to be more sensitive to amyloid than neuroblastoma cell line IMR-32. Amyloid cytotoxicity depends on the size of oligomeric particles: samples containing 20-mers formed at pH 4.5 were more toxic than tetramers and octamers present in the solution at pH 2.0. Soluble amyloid oligomers can self-assemble into doughnut-like structures; however, no correlation was observed between the amount of the doughnut-like structures in the sample and its cytotoxicity. The fact that the intermediate oligomers of such an abundant protein as lysozyme display cytotoxicity confirms a hypothesis that cytotoxicity is a common feature of protein amyloid. Inhibition of intermediate oligomer formation is crucial in preventing amyloid pathogeneses.</div>
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<Abstract><AbstractText>In the current study we investigated the molecular mechanisms of cytotoxicity of amyloid oligomers of horse milk lysozyme. We have shown that lysozyme forms soluble amyloid oligomers and protofibrils during incubation at pH 2.0 and 4.5 and 57 degrees C. These structures bind the amyloid-specific dyes thioflavin T and Congo Red, and their morphology and size were analyzed by atomic force microscopy. Monomeric lysozyme and its fibrils did not affect the viability of three cell types used in our experiments including primary murine neurons and fibroblasts, as well as neuroblastoma cell line IMR-32. However, soluble amyloid oligomers of lysozyme caused death of all these cell types, as estimated by flow-cytometry counting dead cells stained with ethidium bromide. The primary cell cultures appeared to be more sensitive to amyloid than neuroblastoma cell line IMR-32. Amyloid cytotoxicity depends on the size of oligomeric particles: samples containing 20-mers formed at pH 4.5 were more toxic than tetramers and octamers present in the solution at pH 2.0. Soluble amyloid oligomers can self-assemble into doughnut-like structures; however, no correlation was observed between the amount of the doughnut-like structures in the sample and its cytotoxicity. The fact that the intermediate oligomers of such an abundant protein as lysozyme display cytotoxicity confirms a hypothesis that cytotoxicity is a common feature of protein amyloid. Inhibition of intermediate oligomer formation is crucial in preventing amyloid pathogeneses.</AbstractText>
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