Membrane Integrity and Amyloid Cytotoxicity: A Model Study Involving Mitochondria and Lysozyme Fibrillation Products

Meratan, Ali Akbar; Ghasemi, Ali; Nemat‐Gorgani, Mohsen

doi:10.1016/j.jmb.2011.04.045

Cited by 57 publications

(84 citation statements)

References 74 publications

(92 reference statements)

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“…HEWL protofibrils and fibrillar aggregates were prepared as previously reported with some modifications [46]. Briefly, protein solutions (at a final concentration of 1 mM) were prepared in 30 mM glycine buffer (pH 2.4), containing 0.02% NaN 3 , and aliquots were incubated at 57 • C. To obtain HEWL protofibrils, samples were taken at regular time intervals (4, 7 and 10 days) and centrifuged at 21,000 × g for 1 h to remove any insoluble aggregates.…”

Section: Preparation Of Hewl Protofibrils and Fibrillar Aggregatesmentioning

confidence: 99%

Inhibition of amyloid fibrillation and cytotoxicity of lysozyme fibrillation products by polyphenols

Shariatizi

Meratan

Ghasemi

et al. 2015

International Journal of Biological Macromolecules

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Section: Preparation Of Hewl Protofibrils and Fibrillar Aggregatesmentioning

confidence: 99%

Inhibition of amyloid fibrillation and cytotoxicity of lysozyme fibrillation products by polyphenols

Shariatizi

Meratan

Ghasemi

et al. 2015

International Journal of Biological Macromolecules

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“…Several lines of evidence suggest that oligomeric species display higher membrane-binding affinity compared to mature fibrils. This was demonstrated for several proteins including the N-terminal domain of the hydrogenase maturation factor HypF-N (Relini et al 2004;Canale et al 2006, AC), stefin B (Anderluh et al 2005), α-synuclein (Giannakis et al 2008;Smith et al 2008), lysozyme (Meratan et al 2011) and Abeta (Williams and Serpell 2011). This increased affinity was explained in terms of hydrophobicity-based toxicity mechanism, highlighting the importance of factors such as extensive hydrophobic surfaces and high flexibility of the protein oligomers (Meratan et al 2011).…”

Section: Introductionmentioning

confidence: 95%

“…Membrane damage produced by the early protein oligomers is regarded as the main cause of cytotoxicity (Kinnunen 2009;Relini et al 2009;Stefani 2010;Butterfield and Lashuel 2010). Cytotoxic action of protein oligomers can be attributed to compromised membrane integrity (Meratan et al 2011;Huang et al 2009), formation of non-specific ion channels (Caughey and Lansbury 2003), uptake of lipids into the fibers growing on a membrane template (Sparr et al 2004;Engel et al 2008), alterations in the intracellular redox status and free calcium level (Arispe et al 1993;Squier 2001;Tabner et al 2002), and impaired functions of membrane proteins (Stefani 2007). Several lines of evidence suggest that oligomeric species display higher membrane-binding affinity compared to mature fibrils.…”

Section: Introductionmentioning

confidence: 99%

Interactions of Lipid Membranes with Fibrillar Protein Aggregates

Gorbenko

Trusova

Girych

et al. 2015

Advances in Experimental Medicine and Biology

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Amyloid fibrils are an intriguing class of protein aggregates with distinct physicochemical, structural and morphological properties. They display peculiar membrane-binding behavior, thus adding complexity to the problem of protein-lipid interactions. The consensus that emerged during the past decade is that amyloid cytotoxicity arises from a continuum of cross-β-sheet assemblies including mature fibrils. Based on literature survey and our own data, in this chapter we address several aspects of fibril-lipid interactions, including (i) the effects of amyloid assemblies on molecular organization of lipid bilayer; (ii) competition between fibrillar and monomeric membrane-associating proteins for binding to the lipid surface; and (iii) the effects of lipids on the structural morphology of fibrillar aggregates. To illustrate some of the processes occurring in fibril-lipid systems, we present and analyze fluorescence data reporting on lipid bilayer interactions with fibrillar lysozyme and with the N-terminal 83-residue fragment of amyloidogenic mutant apolipoprotein A-I, 1-83/G26R/W@8. The results help understand possible mechanisms of interaction and mutual remodeling of amyloid fibers and lipid membranes, which may contribute to amyloid cytotoxicity.

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“…According to the current concepts, the cytotoxic potential of aggregated proteins may originate from the loss of membrane integrity [21], appearance of non-specific ion channels [22], uptake of lipids into the growing fiber [23], modifications of the intracellular redox status and free calcium level [24], and impaired functional activity of membrane proteins [20]. Obviously, an initial step of membrane damage involves the binding of protein aggregates with the surface of lipid bilayer.…”

Section: кафедра ядерной и медицинской физики харьковский национальнmentioning

confidence: 99%

Effect of Amyloid Fibrils on Electrokinetic Properties of Lipid Vesicles

Tarabara

Vus

Girnyk

et al. 2017

EEJP

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The influence of the lysozyme and serum albumin in their native and amyloid forms on the electrokinetic behavior of the negatively charged uni-and multilamellar liposomes from the zwitterionic lipid phosphatidylcholine and anionic lipid cardiolipin has been investigated using the microelectrophoresis technique. The zeta -potential, the surface electrostatic potential and surface charge density of the lipid vesicles have been determined upon varying the lipid-to-protein molar ratio. The complex dependencies of the electrophoretic mobility on the protein concentration and reversal of the surface charge observed for the multilamellar vesicles have been explained by the multilayer protein adsorption on the liposomal surface. It has been found that the native and fibrillar proteins differ in their ability to modify the charge state of the model membranes. мікроелектрофорезу досліджено вплив нативної та амілоїдної форм лізоциму та сироваткового альбуміну на електрокінетичну поведінку моно-и мультиламелярних ліпосом із цвіттеріонного ліпіду фосфатидилхоліну та аніонного ліпіду кардіоліпіну. При варіюванні молярного співвідношення ліпід:білок було визначено дзета -потенціал, поверхневий електростатичний потенціал та поверхневу густину заряду ліпідних везикул. Складна залежність електрофоретичної рухливості від концентрації білка та зміна знаку поверхневого заряду, виявлені для мультиламелярних везикул, було пояснено мультишаровою адсорбцією білків на поверхні ліпосом. Встановлено, що нативна та фібрилярна форми білків відрізняються за їх здатністю модифікувати зарядовий стан модельних мембран. КЛЮЧОВІ СЛОВА: електрофоретична рухливість, ліпідні везикули, лізоцим, сироватковий альбумін, амілоїдні фібрили Electrostatic phenomena are known to play an essential role in determining the structural and functional properties of biological systems [1,2]. In particular, electrostatics controls a wide variety of processes occurring in cellular membranes, among which are non-specific and specific protein-lipid interactions, protein folding, translocation and orientation in the lipid bilayer [3][4][5], enzyme functioning , ion binding and transport, structural and phase transitions in the lipid phase [1], recognition events [6,7], pharmacological effects [8], etc. Biological membranes consist of hundreds of different molecular species including lipids, proteins and carbohydrates bearing numerous ionized groups which account for the net negative charge of the membrane surface [1]. An essential part of such groups belong to anionic lipids such as phosphatidylglycerol, cardiolipin, phosphatidylserine, phosphatidic acid and phosphatidylinositol, whose KEYWORDS

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Membrane Integrity and Amyloid Cytotoxicity: A Model Study Involving Mitochondria and Lysozyme Fibrillation Products

Cited by 57 publications

References 74 publications

Inhibition of amyloid fibrillation and cytotoxicity of lysozyme fibrillation products by polyphenols

Inhibition of amyloid fibrillation and cytotoxicity of lysozyme fibrillation products by polyphenols

Interactions of Lipid Membranes with Fibrillar Protein Aggregates

Effect of Amyloid Fibrils on Electrokinetic Properties of Lipid Vesicles

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