Dityrosine Cross-links are Present in Alzheimer’s Disease-derived Tau Oligomers and Paired Helical Filaments (PHF) which Promotes the Stability of the PHF-core Tau (297–391) In Vitro

Maina, Mahmoud Bukar; Al-Hilaly, Youssra K.; Oakley, Sebastian; Burra, Gunashekar; Khanon, Tahmida; Biasetti, Luca; Mengham, Kurtis; Marshall, Karen E.; Harrington, Charles R.; Serpell, Louise C.

doi:10.1016/j.jmb.2022.167785

Cited by 11 publications

(9 citation statements)

References 59 publications

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“…Furthermore, we showed that dGAE fibrils formed DiY to a lower extent than the oligomers and other smaller assemblies ( Maina et al, 2022a ). The reduced ability for these fibrils to form DiY could be due to the reduced accessibility to the tyrosine residue in dGAE (Y310) in the fibrils, unlike in prefibrillar assemblies.…”

Section: Dityrosine Cross-linking On Taumentioning

confidence: 87%

“…Previous work from the Binder’s group showed that DiY cross-linked full length tau fibrils have increased SDS stability ( Reynolds et al, 2006 ). We also recently showed that DiY cross-linked dGAE oligomers and especially fibrils, display a significantly reduced SDS and heat solubility ( Maina et al, 2022a ). The fibrils are particularly difficult to resuspend in solution, are heat and SDS-insoluble and transmission electron microscopy show that they maintain strong lateral association ( Maina et al, 2022a ).…”

Section: Dityrosine Cross-linking On Taumentioning

confidence: 99%

“…DiY cross-links in proteins have also been implicated in many diseases, including AD and PD ( Souza et al, 2000 ; Atwood et al, 2004 ; Al-Hilaly et al, 2013 , 2016 , 2019 ), cystic fibrosis ( Van Der Vliet et al, 2000 ), atherosclerosis ( Leeuwenburgh et al, 1996 ), cataracts in the eye lens ( Bodaness and Zigler, 1983 ; Wells-Knecht et al, 1993 ),, and acute myocardial infarction ( Mayer et al, 2014 ). For example, DiY can be generated in vitro in samples of Aβ ( Galeazzi et al, 1999 ; Atwood et al, 2004 ; Al-Hilaly et al, 2013 ; Maina et al, 2020b ), α-synuclein ( Souza et al, 2000 ; Al-Hilaly et al, 2016 ), and Tau ( Reynolds et al, 2005 ; Maina et al, 2021 , 2022b ). However, there remains more to learn about the specific role played by this modification in these aggregation-prone proteins.…”

Section: Introductionmentioning

confidence: 99%

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Dityrosine cross-linking and its potential roles in Alzheimer’s disease

2023

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Oxidative stress is a significant source of damage that accumulates during aging and contributes to Alzheimer’s disease (AD) pathogenesis. Oxidation of proteins can give rise to covalent links between adjacent tyrosines known as dityrosine (DiY) cross-linking, amongst other modifications, and this observation suggests that DiY could serve as a biomarker of accumulated oxidative stress over the lifespan. Many studies have focused on understanding the contribution of DiY to AD pathogenesis and have revealed that DiY crosslinks can be found in both Aβ and tau deposits – the two key proteins involved in the formation of amyloid plaques and tau tangles, respectively. However, there is no consensus yet in the field on the impact of DiY on Aβ and tau function, aggregation, and toxicity. Here we review the current understanding of the role of DiY on Aβ and tau gathered over the last 20 years since the first observation, and discuss the effect of this modification for Aβ and tau aggregation, and its potential as a biomarker for AD.

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Section: Dityrosine Cross-linking On Taumentioning

confidence: 87%

Section: Dityrosine Cross-linking On Taumentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Dityrosine cross-linking and its potential roles in Alzheimer’s disease

2023

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“…Acupuncture can reduce oxidative stress and reduce neuroinflammation through multiple signal transduction pathways, Aβ Production, aggregation, and phosphorylation of Tau. Beura et al, 2022;Estévez-Silva et al, 2022;Maina et al, 2022). We believe that abnormal mitochondria in susceptible neurons play a source role by providing diffusible hydrogen peroxide on the membrane to the surrounding cytoplasm, as shown in Figure 3.…”

Section: Acupuncture Ameliorates Neuronal Antioxidant Damage As Well ...mentioning

confidence: 95%

Effect and mechanism of acupuncture on Alzheimer’s disease: A review

Dong

Zhu

et al. 2023

Front. Aging Neurosci.

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With the development trend of an aging society, Alzheimer’s disease (AD) has become an urgent problem in the field of medicine worldwide. Cognitive impairment in AD patients leads to a decline in the ability to perform daily living and abnormalities in behavior and personality, causing abnormal psychiatric symptoms, which seriously affect the daily life of patients. Currently, mainly drug therapy is used for AD patients in the clinic, but a large proportion of patients will experience drug efficacy not working, and even some drugs bring severe sleep disorders. Acupuncture, with its unique concept and treatment method, has been validated through a large number of experiments and proved its reliability of acupuncture in the treatment of AD. Many advances have been made in the study of the neurobiological mechanisms of acupuncture in the treatment of AD, further demonstrating the good efficacy and unique advantages of acupuncture in the treatment of AD. This review first summarizes the pathogenesis of AD and then illustrates the research progress of acupuncture in the treatment of AD, which includes the effect of acupuncture on the changes of biochemical indicators in AD in vivo and the specific mechanism of action to exert the therapeutic effect. Changes in relevant indicators of AD similarly further validate the effectiveness of acupuncture treatment. The clinical and mechanistic studies of acupuncture in the treatment of AD are intensified to fit the need for social development. It is believed that acupuncture will achieve new achievements in the treatment of AD as research progresses.

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“…The development of AD is associated with an increase in the deposition of various abnormal peptides: beta -amyloid (Aβ, amyloid theory) and tau protein (an overly phosphorylated protein involved in the movement of microtubules-tau-peptide [ 13 ]). Beta -amyloid (type β42) is contained in the intercellular space and cerebrospinal fluid of healthy people in the amount of 10% of all beta -amyloids.…”

Section: Introductionmentioning

confidence: 99%

New TEMPO–Appended 2,2′-Bipyridine-Based Eu(III), Tb(III), Gd(III) and Sm(III) Complexes: Synthesis, Photophysical Studies and Testing Photoluminescence-Based Bioimaging Abilities

et al. 2022

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Linked to Alzheimer’s disease (AD), amyloids and tau-protein are known to contain a large number of cysteine (Cys) residues. In addition, certain levels of some common biogenic thiols (cysteine (Cys), homocysteine (Hcy), glutathione (GSH), etc.) in biological fluids are closely related to AD as well as other diseases. Therefore, probes with a selective interaction with the above-mentioned thiols can be used for the monitoring and visualizing changes of (bio)thiols in the biological fluids as well as in the brain of animal models of Alzheimer’s disease. In this study, new Eu(III), Tb(III), Gd(III) and Sm(III) complexes of 2,2′-bipyridine ligands containing TEMPO fragments as receptor units for (bio)thiols are reported. The presence of free radical fragments of the ligand in the complexes was proved by using the electronic paramagnetic resonance (EPR) method. Among all the complexes, the Eu(III) complex turned out to be the most promising one as luminescence- and spin-probe for the detection of biogenic thiols. The EPR and fluorescent titration methods showed the interaction of the resulting complex with free Cys and GSH in solution. To study the practical applicability of the probes for the monitoring of AD in-vivo, by using the above-mentioned Eu(III)-based probe, the staining of the brain of mice with amyloidosis and Vero cell cultures supplemented with the cysteine-enriched medium was studied as well as the fluorescence titration of Bovine Serum Albumin, BSA (as the model for the thiol moieties containing protein), was carried out. Based on the results of fluorescence titration, the formation of a non-covalent inclusion complex between the above-mentioned Eu(III) complex and BSA was suggested.

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Dityrosine Cross-links are Present in Alzheimer’s Disease-derived Tau Oligomers and Paired Helical Filaments (PHF) which Promotes the Stability of the PHF-core Tau (297–391) In Vitro

Cited by 11 publications

References 59 publications

Dityrosine cross-linking and its potential roles in Alzheimer’s disease

Dityrosine cross-linking and its potential roles in Alzheimer’s disease

Effect and mechanism of acupuncture on Alzheimer’s disease: A review

New TEMPO–Appended 2,2′-Bipyridine-Based Eu(III), Tb(III), Gd(III) and Sm(III) Complexes: Synthesis, Photophysical Studies and Testing Photoluminescence-Based Bioimaging Abilities

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