Classification of amyloidosis and protein misfolding disorders in animals 2024: A review on pathology and diagnosis DOI
Susumu Iwaide, Tomoaki Murakami,

Niki Sedghi Masoud

et al.

Veterinary Pathology, Journal Year: 2024, Volume and Issue: unknown

Published: Oct. 10, 2024

Amyloidosis is a group of diseases in which proteins become amyloid, an insoluble fibrillar aggregate, resulting organ dysfunction. Amyloid deposition has been reported various animal species. To diagnose and understand the pathogenesis amyloidosis, it important to identify amyloid precursor protein involved each disease. Although 42 have humans, little known about amyloidosis animals, except for few well-described proteins, including A (AA), light chain (AL), β (Aβ), islet polypeptide-derived amyloid. Recently, several types novel identified animals using immunohistochemistry mass spectrometry-based proteomic analysis. Certain species are predisposed specific suggesting genetic background its pathogenesis. Age-related also emerged due increased longevity captive animals. In addition, experimental studies shown that some amyloids may be transmissible. Accurate diagnosis understanding necessary appropriate therapeutic intervention comparative pathological studies. This review provides updated classification associated misfolding disorders central nervous system, current their Pathologic features presented together with state-of-the-art diagnostic methods can applied routine identification

Language: Английский

Challenges Associated With the Formation of Recombinant Protein Inclusion Bodies in Escherichia coli and Strategies to Address Them for Industrial Applications DOI Creative Commons

Arshpreet Bhatwa,

Weijun Wang, Yousef I. Hassan

et al.

Frontiers in Bioengineering and Biotechnology, Journal Year: 2021, Volume and Issue: 9

Published: Feb. 10, 2021

Recombinant proteins are becoming increasingly important for industrial applications, where Escherichia coli is the most widely used bacterial host their production. However, formation of inclusion bodies a frequently encountered challenge producing soluble and functional recombinant proteins. To overcome this hurdle, different strategies have been developed through adjusting growth conditions, engineering strains E. , altering expression vectors, modifying interest. These approaches will be comprehensively highlighted with some new developments in review. Additionally, unique features protein bodies, mechanism influencing factors formation, potential advantages also discussed.

Language: Английский

Citations

196
Prevalence of cerebral amyloid angiopathy: A systematic review and meta‐analysis DOI
Lieke Jäkel, Anna M. de Kort, Catharina J.M. Klijn

et al.

Alzheimer s & Dementia, Journal Year: 2021, Volume and Issue: 18(1), P. 10 - 28

Published: May 31, 2021

Reported prevalence estimates of sporadic cerebral amyloid angiopathy (CAA) vary widely. CAA is associated with cognitive dysfunction and intracerebral hemorrhage, linked to immunotherapy-related side-effects in Alzheimer's disease (AD). Given ongoing efforts develop AD immunotherapy, accurate are important. can be diagnosed neuropathologically or during life using MRI markers including strictly lobar microbleeds. In this meta-analysis 170 studies over 73,000 subjects, we show that patients AD, based on pathology (48%) twice presence microbleeds (22%); the general population difference three-fold (23% vs 7%). Both methods yield similar estimated prevalences cognitively normal elderly (5% 7%), hemorrhage (19% 24%), (50% 57%). However, observed large heterogeneity among neuropathology protocols, which calls for standardized assessment reporting CAA.

Language: Английский

Citations

186
Structure and Aggregation Mechanisms in Amyloids DOI Creative Commons
Zaida L. Almeida, Rui M. M. Brito

Molecules, Journal Year: 2020, Volume and Issue: 25(5), P. 1195 - 1195

Published: March 6, 2020

The aggregation of a polypeptide chain into amyloid fibrils and their accumulation deposition insoluble plaques intracellular inclusions is the hallmark several misfolding diseases known as amyloidoses. Alzheimer's, Parkinson's Huntington's are some approximately 50 described to date. identification characterization molecular species critical for formation disease development have been focus intense scrutiny. Methods such X-ray electron diffraction, solid-state nuclear magnetic resonance spectroscopy (ssNMR) cryo-electron microscopy (cryo-EM) extensively used they contributed shed new light onto structure amyloid, revealing multiplicity polymorphic structures that generally fit cross-β motif. rational therapeutic approaches against these debilitating increasingly frequent requires thorough understanding mechanisms underlying cascade. Here, we review current knowledge on fibril proteins peptides from kinetic thermodynamic point view, involved in amyloidogenic process, origin cytotoxicity.

Language: Английский

Citations

179
Toxicity and decontamination strategies of Congo red dye DOI
Peter Olusakin Oladoye,

Mutiat Oyedolapo Bamigboye,

Olutobi Daniel Ogunbiyi

et al.

Groundwater for Sustainable Development, Journal Year: 2022, Volume and Issue: 19, P. 100844 - 100844

Published: Sept. 15, 2022

Language: Английский

Citations

138
A guide to studying protein aggregation DOI Open Access
Joëlle A.J. Housmans, Guiqin Wu, Joost Schymkowitz

et al.

FEBS Journal, Journal Year: 2021, Volume and Issue: 290(3), P. 554 - 583

Published: Dec. 4, 2021

Disrupted protein folding or decreased stability can lead to the accumulation of (partially) un- misfolded proteins, which ultimately cause formation aggregates. Much interest in aggregation is associated with its involvement a wide range human diseases and challenges it poses for large-scale biopharmaceutical manufacturing formulation therapeutic proteins peptides. On other hand, aggregates also be functional, as observed nature, triggered use development biomaterials therapeutics well improvement food characteristics. Thus, unmasking various steps involved critical obtain better understanding underlying mechanism amyloid formation. This knowledge will allow more tailored diagnostic methods treatments amyloid-associated diseases, applications fields new (bio)materials, technology therapeutics. However, complex dynamic nature process makes study challenging. To provide guidance on how analyse aggregation, this review we summarize most commonly investigated aspects some popular corresponding methods.

Language: Английский

Citations

135
Simultaneous removal of Ni2+ and Congo red from wastewater by crystalline nanocellulose - Modified coal bionanocomposites: Continuous adsorption study with mathematical modeling DOI
Md. Mahmudur Rahman,

Md. Aftab Ali Shaikh,

Mst. Sarmina Yeasmin

et al.

Groundwater for Sustainable Development, Journal Year: 2024, Volume and Issue: 26, P. 101244 - 101244

Published: June 17, 2024

Language: Английский

Citations

21
The role of amyloid oligomers in neurodegenerative pathologies DOI Creative Commons
Cameron I. Wells,

Samuel Brennan,

Matt Keon

et al.

International Journal of Biological Macromolecules, Journal Year: 2021, Volume and Issue: 181, P. 582 - 604

Published: March 23, 2021

Many neurodegenerative diseases are rooted in the activities of amyloid-like proteins which possess conformations that spread to healthy proteins. These include Alzheimer's disease (AD), Parkinson's (PD), Huntington's (HD) and amyotrophic lateral sclerosis (ALS). While their clinical manifestations vary, protein-level mechanisms remarkably similar. Aberrant monomeric undergo conformational shifts, facilitating aggregation formation solid fibrils. However, there is growing evidence intermediate oligomeric stages key drivers neuronal toxicity. Analysis protein dynamics complicated by fact nucleation growth not a linear pathway. Feedback within this pathway results exponential acceleration aggregation, but exerted oligomers fibrils can alter cellular interactions environment as whole. The resulting cascade effects likely contributes late onset accelerating progression disorders widespread they have on body. In review we explore associated with AD, PD, HD ALS, well common aggregation. From this, identify core elements pathological been targeted for therapies, may become future therapeutic targets.

Language: Английский

Citations

86
Green Tea Polyphenol Epigallocatechin-Gallate in Amyloid Aggregation and Neurodegenerative Diseases DOI Creative Commons
Luiza Fernandes, Thyago R. Cardim-Pires, Débora Foguel

et al.

Frontiers in Neuroscience, Journal Year: 2021, Volume and Issue: 15

Published: Sept. 14, 2021

The accumulation of protein aggregates in human tissues is a hallmark more than 40 diseases called amyloidoses. In seven these disorders, the aggregation associated with neurodegenerative processes central nervous system such as Alzheimer’s disease (AD), Parkinson’s (PD), and Huntington’s (HD). occurs when certain soluble proteins lose their physiological function become toxic amyloid species. assembly consists filament interactions, which can form fibrillar structures rich β-sheets. Despite frequent incidence among elderly, available treatments are limited at best palliative, new therapeutic approaches needed. Among many natural compounds that have been evaluated for ability to prevent or delay amyloidogenic process epigallocatechin-3-gallate (EGCG), an abundant potent polyphenolic molecule present green tea has extensive biological activity. There evidence EGCG’s inhibit α-synuclein, amyloid-β, huntingtin proteins, respectively PD, AD, HD. It prevents fibrillogenesis ( vitro vivo ), reduces cytotoxicity, remodels fibrils non-toxic amorphous species lack seed propagation. Although it antioxidant, EGCG oxidized state promote fibrils’ remodeling through formation Schiff bases crosslinking fibrils. Moreover, microparticles drug delivery were synthesized from loaded second anti-amyloidogenic molecule, obtaining synergistic effect. Here, we describe several pre-clinical clinical studies involving related mechanisms.

Language: Английский

Citations

67
Green synthesis of ZnFe2O4@ZnO nanocomposites using Chrysanthemum spp. floral waste for photocatalytic dye degradation DOI

Ngoan Thi Thao Nguyen,

Luan Minh Nguyen, Thuy Thi Thanh Nguyen

et al.

Journal of Environmental Management, Journal Year: 2022, Volume and Issue: 326, P. 116746 - 116746

Published: Nov. 16, 2022

Language: Английский

Citations

51
Monitoring α-synuclein aggregation DOI Creative Commons
Juan Estaun-Panzano, Marie-Laure Arotçarena, Erwan Bézard

et al.

Neurobiology of Disease, Journal Year: 2022, Volume and Issue: 176, P. 105966 - 105966

Published: Dec. 15, 2022

Synucleinopathies, including Parkinson's disease (PD), dementia with Lewy Bodies (DLB), and multiple system atrophy (MSA), are characterized by the misfolding subsequent aggregation of alpha-synuclein (α-syn) that accumulates in cytoplasmic inclusions bodies cells affected brain regions. Since seminal report likely-aggregated α-syn presence within Spillantini et al. 1997, keyword "synuclein aggregation" has appeared over 6000 papers (Source: PubMed October 2022). Studying, observing, describing, quantifying is therefore paramount importance, whether it happens tubo, vitro, post-mortem samples, or vivo. The past few years have witnessed tremendous progress understanding mechanisms identifying various polymorphs. In this context growing complexity, utmost importance to understand what tools we possess, exact information they provide, may be applied. Nonetheless, also crucial rationalize relevance limitations these methods for gauging final result. review, present main techniques shaped current views about structure dynamics, particular emphasis on recent breakthroughs change our synucleinopathies.

Language: Английский

Citations

49