Conversion of Amino Acid Residues in Proteins and Amino Acid Homopolymers to Carbonyl Derivatives by Metal-catalyzed Oxidation Reactions

Amici, Augusto; Levine, Rodney L.; Tsai, Lin; Stadtman, Earl R.

doi:10.1016/s0021-9258(18)94071-8

Cited by 447 publications

(105 citation statements)

References 25 publications

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“…Carbonylation is another feature of proteins subjected to oxidative damage [129]. Carbonylated proteins form aggregates that are chemically irreversible and cannot be degraded via proteasomes, leading to the permanent loss of function in these proteins [130,131]. Gurunathan et al [132] showed that PtNPs could enhance the generation of ROS and increase carbonylated protein levels, which inhibited osteosarcoma proliferation and contributed to apoptosis.…”

Section: Ros Attacks Proteins and Results In Functional Inactivationmentioning

confidence: 99%

Reactive Oxygen Species-Related Nanoparticle Toxicity in the Biomedical Field

et al. 2020

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The unique physicochemical characteristics of nanoparticles have recently gained increasing attention in a diverse set of applications, particularly in the biomedical field. However, concerns about the potential toxicological effects of nanoparticles remain, as they have a higher tendency to generate excessive amounts of reactive oxygen species (ROS). Due to the strong oxidation potential, the excess ROS induced by nanoparticles can result in the damage of biomolecules and organelle structures and lead to protein oxidative carbonylation, lipid peroxidation, DNA/RNA breakage, and membrane structure destruction, which further cause necrosis, apoptosis, or even mutagenesis. This review aims to give a summary of the mechanisms and responsible for ROS generation by nanoparticles at the cellular level and provide insights into the mechanics of ROS-mediated biotoxicity. We summarize the literature on nanoparticle toxicity and suggest strategies to optimize nanoparticles for biomedical applications.

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Section: Ros Attacks Proteins and Results In Functional Inactivationmentioning

confidence: 99%

Reactive Oxygen Species-Related Nanoparticle Toxicity in the Biomedical Field

et al. 2020

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“…ROS can lead to oxidation in both amino acid side chains and protein backbone, forming protein-protein cross-links or protein fragments [261]. In the lens, oxidation of methionine (Met) amino acid to methionine sulfoxide or sulfone and cysteine (Cys) to cystine occur [247,262]. The oxidative damage accumulates over time, which occurs at higher rates in the cataractous lens [30,263] compared to normal lenses.…”

Section: Oxidationmentioning

confidence: 99%

Association of Alpha-Crystallin with Fiber Cell Plasma Membrane of the Eye Lens Accompanied by Light Scattering and Cataract Formation

Timsina

Mainali

2021

Membranes

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α-crystallin is a major protein found in the mammalian eye lens that works as a molecular chaperone by preventing the aggregation of proteins and providing tolerance to stress in the eye lens. These functions of α-crystallin are significant for maintaining lens transparency. However, with age and cataract formation, the concentration of α-crystallin in the eye lens cytoplasm decreases with a corresponding increase in the membrane-bound α-crystallin, accompanied by increased light scattering. The purpose of this review is to summarize previous and recent findings of the role of the: 1) lens membrane components, i.e., the major phospholipids (PLs) and sphingolipids, cholesterol (Chol), cholesterol bilayer domains (CBDs), and the integral membrane proteins aquaporin-0 (AQP0; formally MIP26) and connexins, and 2) α-crystallin mutations and post-translational modifications (PTMs) in the association of α-crystallin to the eye lens’s fiber cell plasma membrane, providing thorough insights into a molecular basis of such an association. Furthermore, this review highlights the current knowledge and need for further studies to understand the fundamental molecular processes involved in the association of α-crystallin to the lens membrane, potentially leading to new avenues for preventing cataract formation and progression.

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“…The formation of reactive oxygen species under oxidative stress results in the carbonylation of proteins (Davis et al, 1987). Reactive oxygen species can produce carbonyl residues directly by oxidative cleavage of proteins or by the oxidation of arginine, lysine, threonine, and proline residues (Levine, 1983;Davis et al, 1987;Amici et al, 1989;Stadtman and Berlett, 1991). Carbonyl groups may also be introduced into proteins by reaction with a,b-unsaturated carbonyl fragments of membrane lipids during lipid peroxidation or by glycation and glycoxidation reactions (Berlett and Stadtman, 1997).…”

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confidence: 99%

Increased Oxidative Damage to Fibroblasts in Skin With and Without Lesions in Psoriasis

Dimon-Gadal

Gerbaud

Thérond

et al. 2000

Journal of Investigative Dermatology

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Differences in oxidative damage, as measured by an increase in the carbonylation of macromolecules, were determined in situ with skin biopsies from psoriatic patients and controls. High levels of carbonyl residues were consistently detected in the dermis and never in the epidermis of sections of these skin biopsy samples. The dermis of psoriatic skin without lesions had a higher level of carbonylation than the dermis of normal skin. In this study, we found that there was more oxidative damage in cultured fibroblasts prepared from skin with and without lesions from psoriasis patients than in normal fibroblasts from the skin of age-matched controls. The extent of protein carbonylation in cell extracts was determined by immunoblotting, using an antidinitrophenylhydrazone antibody, and in intact cells was determined by immunocytochemical analysis with the same antibody. The higher level of carbonylation detected was used here as a measure of oxidative stress, and showed that some oxidative damage occurred before the appearance of typical psoriatic plaques. These results suggest that fibroblasts are affected before the onset of psoriasis and that this damage is independent of any inflammatory infiltrate.

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Conversion of Amino Acid Residues in Proteins and Amino Acid Homopolymers to Carbonyl Derivatives by Metal-catalyzed Oxidation Reactions

Cited by 447 publications

References 25 publications

Reactive Oxygen Species-Related Nanoparticle Toxicity in the Biomedical Field

Reactive Oxygen Species-Related Nanoparticle Toxicity in the Biomedical Field

Association of Alpha-Crystallin with Fiber Cell Plasma Membrane of the Eye Lens Accompanied by Light Scattering and Cataract Formation

Increased Oxidative Damage to Fibroblasts in Skin With and Without Lesions in Psoriasis

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