Tag: in vitro study

β-Lactoglobulin Enhances Clay and Activated Carbon Binding and Protection Properties for Cadmium and Lead

This 2024 in vitro study explored the use of β-lactoglobulin, a whey protein, to enhance the heavy metal-binding capabilities of clay and activated carbon for detoxifying cadmium and lead. Researchers found that combining β-lactoglobulin with these adsorbents significantly increased their binding capacity, likely due to the protein’s chelating properties, which

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Carnosine protects proteins against methylglyoxal-mediated modifications

This in vitro study explores the potential of carnosine, a naturally occurring dipeptide, in protecting proteins from methylglyoxal (MG)-induced modifications, which are associated with the formation of advanced glycation end-products (AGEs) and diabetic complications. The research demonstrates that carnosine effectively inhibits MG-induced protein modifications and prevents AGE formation, suggesting it

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α-Lipoic acid prevents senescence, cell cycle arrest, and inflammatory cues in fibroblasts by inhibiting oxidative stress

This 2019 in vitro study published in Pharmacological Research (DOI: 10.1016/j.phrs.2019.01.003, PMID: 30611855) investigated the protective effects of alpha-lipoic acid (ALA) on fibroblast cells exposed to oxidative stress. The results demonstrated that ALA effectively reduced oxidative stress, inhibited DNA damage, and prevented cellular senescence by modulating key redox-sensitive pathways. Specifically,

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Reduction of molecular oxygen by redox active thiols: comparison of glutathione, N-acetylcysteine, cysteine, and homocysteine

This in vitro study compared the redox activity of four thiol compounds—glutathione (GSH), N-acetylcysteine (NAC), cysteine (Cys), and homocysteine (HCS)—to evaluate their potential to reduce molecular oxygen and influence oxidative or reductive stress. The researchers found that GSH and Cys can reduce O₂ to generate reactive oxygen species (ROS), particularly

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Mercury binding to the chelation therapy agents DMSA and DMPS and the rational design of custom chelators for mercury

This study investigates the efficacy of two commonly used chelation therapy agents, meso-2,3-dimercaptosuccinic acid (DMSA) and 2,3-dimercaptopropane-1-sulfonic acid (DMPS), in binding mercuric ions (Hg²⁺). Using mercury L(III)-edge X-ray absorption spectroscopy and density functional theory calculations, researchers found that neither DMSA nor DMPS forms true chelate complexes with Hg²⁺, which may

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Alternative mitochondrial electron transfer for the treatment of neurodegenerative diseases and cancers: Methylene blue connects the dots

Methylene blue (MB) demonstrates potential as a therapeutic agent by enhancing mitochondrial function and altering energy metabolism. Acting as an alternative electron carrier, MB bypasses mitochondrial dysfunction, increasing oxygen consumption, decreasing glycolysis, and improving glucose uptake. In rodent models, MB enhanced regional cerebral blood flow and provided neuroprotection, while in

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Enhanced hydrogen peroxide generation accompanies the beneficial bioenergetic effects of methylene blue in isolated brain mitochondria

This in vitro study examined the effects of methylene blue (MB) on mitochondrial function in isolated guinea pig brain mitochondria, assessing its impact on oxygen consumption, ATP production, mitochondrial membrane potential, calcium uptake, and hydrogen peroxide (H₂O₂) production. MB enhanced mitochondrial bioenergetics by increasing ATP production, restoring membrane potential, and

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Activation of Nrf2 by methylene blue is associated with the neuroprotection against MPP+ induced toxicity via ameliorating oxidative stress and mitochondrial dysfunction

Methylene blue (MB) demonstrates neuroprotective potential against MPP+-induced neurotoxicity, a model for Parkinson’s disease, by reducing oxidative stress and mitochondrial dysfunction. The study, conducted in vitro and in animal models, highlights MB’s ability to restore mitochondrial complex I activity, increase ATP levels, and activate the Nrf2 pathway via AKT signaling,

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