Aggregation and structural changes of αS1-, β- and κ-caseins induced by homocysteinylation

Stroylova, Yulia Yu.; Zimny, Jarosław; Yousefi, Reza; Chobert, Jean‐Marc; Jakubowski, Hieronim; Muronetz, Vladimir I.; Haertlé, Thomas

doi:10.1016/j.bbapap.2011.05.017

Cited by 37 publications

(41 citation statements)

References 33 publications

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“…41,43,49,50 The excitation spectrum presents differences with the UV absorption spectrum of the protein in the same medium (see Figure S1, Supporting Information), suggesting that in the present experimental conditions energy-transfer processes are taking place. At an early stage of the heating treatment (first 6 h), the emission spectra display a gradual red-shift with the maximum moving from 330 to 340 nm ( Figure 2); the red-shift comes together with a remarkable intensity increase (the spectra are corrected for the fraction of absorbed light).…”

Section: ■ Results and Discussionmentioning

confidence: 91%

Spectroscopic and Microscopic Studies of Aggregation and Fibrillation of Lysozyme in Water/Ethanol Solutions

et al. 2015

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The thermal aggregation of lysozyme has been analyzed in water/ethanol solutions at low pH to induce the specific protein aggregation pathway which leads to fibrillar structures in a few hours. In this solvating medium, the protein undergoes a conformational rearrangement promoting the formation of fibrils that are structurally similar to amyloid ones. As the process evolves with different steps, a multitechnique approach has been used by means of analytical probes that can be selectively sensitive in the detection of the different stages of protein association. Fourier transform infrared spectroscopy, intrinsic fluorescence, stationary fluorescence anisotropy, transmission electron microscopy (TEM), and atomic force microscopy (AFM) measurements have been carried out at different times to access and characterize the whole aggregation pathway. The data recorded with different experimental setups revealed different sensitivity to different stages of protein assembling. The whole set of data together with the direct visualization of different aggregate structures by use of TEM and AFM imaging enable to discuss a possible mechanism of fibrillation.

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Section: ■ Results and Discussionmentioning

confidence: 91%

Spectroscopic and Microscopic Studies of Aggregation and Fibrillation of Lysozyme in Water/Ethanol Solutions

et al. 2015

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“…decrease oligomers elongation and/or fibril formation and hence, possibly leads to new toxic protofibrils with low self-assembly and high toxicity [41,42,46,51]. This study proposes a probable mechanism for the correlation between hyperhomocysteinemia and the progress of Alzheimer's disease.…”

Section: Resultsmentioning

confidence: 96%

Effect of N‐homocysteinylation on physicochemical and cytotoxic properties of amyloid β‐peptide

et al. 2011

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a b s t r a c tHyperhomocysteinemia has recently been identified as an important risk factor for Alzheimer's disease (AD). One of the potential mechanisms underlying harmful effects of homocysteine (Hcy) is site-specific acylation of proteins at lysine residues by homocysteine thiolactone (HCTL). The accumulation of amyloid b-peptide (Ab) in the brain is a neuropathological hallmark of AD. In the present study we were interested to investigate the effects of N-homocysteinylation on the aggregation propensity and neurotoxicity of Ab 1-42 . By coupling several techniques, we demonstrated that the homocysteinylation of lysine residues increase the neurotoxicity of the Ab peptide by stabilizing soluble oligomeric intermediates. Structured summary of protein interactions:A Beta 1-42 and A Beta 1-42 bind by fluorescence technology (View interaction) A Beta 1-42 and A Beta 1-42 bind by electron microscopy (View interaction)

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“…While the exact mechanisms of these pathophysiological conditions are not clear and may be multifaceted, many laboratories have identified oxidative stress (57), epigenetic modification of proteins (47), and cellular apoptosis and autophagy (36,55) as being involved in HHcy-associated vascular disorders. Recently, a growing body of evidence suggested that depletion of hydrogen sulfide (H 2 S) in the body during HHcy is one of the possible mechanisms of vasculopathies (2,50).…”

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confidence: 99%

Increased endogenous H₂S generation by CBS, CSE, and 3MST gene therapy improves ex vivo renovascular relaxation in hyperhomocysteinemia

Sen

Sathnur

Kundu

et al. 2012

American Journal of Physiology-Cell Physiology

101

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Hydrogen sulfide (H2S) has recently been identified as a regulator of various physiological events, including vasodilation, angiogenesis, antiapoptotic, and cellular signaling. Endogenously, H2S is produced as a metabolite of homocysteine (Hcy) by cystathionine β-synthase (CBS), cystathionine γ-lyase (CSE), and 3-mercaptopyruvate sulfurtransferase (3MST). Although Hcy is recognized as vascular risk factor at an elevated level [hyperhomocysteinemia (HHcy)] and contributes to vascular injury leading to renovascular dysfunction, the exact mechanism is unclear. The goal of the current study was to investigate whether conversion of Hcy to H2S improves renovascular function. Ex vivo renal artery culture with CBS, CSE, and 3MST triple gene therapy generated more H2S in the presence of Hcy, and these arteries were more responsive to endothelial-dependent vasodilation compared with nontransfected arteries treated with high Hcy. Cross section of triple gene-delivered renal arteries immunostaining suggested increased expression of CD31 and VEGF and diminished expression of the antiangiogenic factor endostatin. In vitro endothelial cell culture demonstrated increased mitophagy during high levels of Hcy and was mitigated by triple gene delivery. Also, dephosphorylated Akt and phosphorylated FoxO3 in HHcy were reversed by H2S or triple gene delivery. Upregulated matrix metalloproteinases-13 and downregulated tissue inhibitor of metalloproteinase-1 in HHcy were normalized by overexpression of triple genes. Together, these results suggest that H2S plays a key role in renovasculopathy during HHcy and is mediated through Akt/FoxO3 pathways. We conclude that conversion of Hcy to H2S by CBS, CSE, or 3MST triple gene therapy improves renovascular function in HHcy.

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Aggregation and structural changes of αS1-, β- and κ-caseins induced by homocysteinylation

Cited by 37 publications

References 33 publications

Spectroscopic and Microscopic Studies of Aggregation and Fibrillation of Lysozyme in Water/Ethanol Solutions

Spectroscopic and Microscopic Studies of Aggregation and Fibrillation of Lysozyme in Water/Ethanol Solutions

Effect of N‐homocysteinylation on physicochemical and cytotoxic properties of amyloid β‐peptide

Increased endogenous H₂S generation by CBS, CSE, and 3MST gene therapy improves ex vivo renovascular relaxation in hyperhomocysteinemia

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Aggregation and structural changes of αS1-, β- and κ-caseins induced by homocysteinylation

Cited by 37 publications

References 33 publications

Spectroscopic and Microscopic Studies of Aggregation and Fibrillation of Lysozyme in Water/Ethanol Solutions

Spectroscopic and Microscopic Studies of Aggregation and Fibrillation of Lysozyme in Water/Ethanol Solutions

Effect of N‐homocysteinylation on physicochemical and cytotoxic properties of amyloid β‐peptide

Increased endogenous H2S generation by CBS, CSE, and 3MST gene therapy improves ex vivo renovascular relaxation in hyperhomocysteinemia

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Increased endogenous H₂S generation by CBS, CSE, and 3MST gene therapy improves ex vivo renovascular relaxation in hyperhomocysteinemia