Effects of glutathione on amyloid fibrillation of hen egg-white lysozyme

Wang, Steven S.‐S.; Chou, Shu-Hua; Liu, Kuan-Nan; Wu, Chia-Hung

doi:10.1016/j.ijbiomac.2009.08.003

Cited by 37 publications

(16 citation statements)

References 75 publications

(112 reference statements)

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“…GSH is a potent antioxidant that has been shown to attenuate A␤-induced oxidative damage [109,110]. Preliminary in vitro evidence also suggests that GSH may be directly involved in attenuating AD pathogenesis [111][112][113]. Finally, in vitro studies have provided preliminary evidence that A␤ may directly disrupt GSH cycle homeostasis and lead to GSH depletion [44][45][46][47][48].…”

Section: Os In Ad Pathology: Relationship Between Os and Aβmentioning

confidence: 99%

“…In vitro studies that examined the effect of GSH on aggregation and fibrillation of amyloidogenic proteins have demonstrated that GSH significantly attenuates fibril formation [111,112]. An in vitro biochemical study directly assessed whether GSH levels modulate A␤-mediated cytotoxicity by exogenous addition of A␤ peptides to human neuroblastoma cells [113].…”

Section: Role Of Gsh In Ad Pathologymentioning

confidence: 99%

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The Emerging Role of Glutathione in Alzheimer's Disease

Saharan

Mandal

2014

JAD

150

100

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With millions of older individuals presently suffering from Alzheimer's disease (AD) worldwide, AD is an unduly common form of dementia that exacts a heavy toll on affected individuals and their families. One of the emerging causative factors associated with AD pathology is oxidative stress. This AD-related increase in oxidative stress has been attributed to decreased levels of the brain antioxidant, glutathione (GSH). In this article, we review the role of GSH in AD from a pathological as well as a diagnostic point of view. We recapitulate the literature that has assessed the role of GSH in AD onset and progression. We discuss the various methodologies through which alterations in GSH levels might be monitored, and highlight the yet uncharted potential of assaying GSH levels in vivo with magnetic resonance spectroscopy in AD therapeutics and prognostics. Finally, the present manuscript integrates findings from various studies to elucidate the possible molecular mechanisms through which disruptions in GSH homeostasis may contribute to AD pathology.

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Section: Os In Ad Pathology: Relationship Between Os and Aβmentioning

confidence: 99%

Section: Role Of Gsh In Ad Pathologymentioning

confidence: 99%

The Emerging Role of Glutathione in Alzheimer's Disease

Saharan

Mandal

2014

JAD

150

100

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“…Proteins in aqueous solution are only marginally stable, therefore precipitation can be easily induced by heating, altering pH and/or salt concentration, organic additives, and other manipulations [1][2][3]. Protein precipitation is a ubiquitous problem in the fields of life science and biotechnology.…”

Section: Introductionmentioning

confidence: 99%

Investigation into the mechanism of (−)-epigallocatechin-3-gallate-induced precipitation of insulin

Wang

Dong

Sun

2012

International Journal of Biological Macromolecules

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“…ANS is a hydrophobic marker that exhibits unique fluorescence along with a notable blue shift upon binding to the hydrophobic regions of proteins (31)(32)(33). Thus, ANS has been widely used for the detection of hydrophobic regions of proteins.…”

Section: Alteration In the Hydrophobic Exposure Of β-Lg In The Presenmentioning

confidence: 99%

Folic acid inhibits the amyloid fibrils formation of β-lactoglobulin

Li²,

Zhu

et al. 2017

Eur J Bio Med Res

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Abstract:It is well known that amyloid fibrils are associated with a lot of neurodegenerative diseases. Thus, inhibition of protein aggregation and disruption of the formed amyloid fibrils have been attractive therapeutic strategies for amyloid-associated diseases. Here, we take the widely studied protein, β-lactoglobulin (β-LG), as a model protein to study the inhibition of amyloid fibrils. Using multiple biophysical and biochemical approaches, we successfully identify that folic acid can strongly inhibit amyloid fibrils formation of β-LG in 5 M urea solution. In the presence of folic acid, both the nucleation step and elongation step of β-LG fibrillation can be affected and the suppression efficiency followed a dose depended manner. Furthermore, the studies of protein intrinsic-fluorescence and anilinonaphthalene-8-sulfonic acid (ANS) fluorescence demonstrated that the folic acid decreased the hydrophobicity of the urea-denatured β-LG and changed the conformation of β-LG. Our study provides a convenient way to inhibit the amyloid fibrils formation, which has potential help to study the mechanism of amyloid-diseases.

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Effects of glutathione on amyloid fibrillation of hen egg-white lysozyme

Cited by 37 publications

References 75 publications

The Emerging Role of Glutathione in Alzheimer's Disease

The Emerging Role of Glutathione in Alzheimer's Disease

Investigation into the mechanism of (−)-epigallocatechin-3-gallate-induced precipitation of insulin

Folic acid inhibits the amyloid fibrils formation of β-lactoglobulin

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