Thematische Bibliographien / Dicarbonyl stress

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Auswahl der wissenschaftlichen Literatur zum Thema „Dicarbonyl stress“

Autor: Grafiati

Veröffentlicht am 25. Mai 2024

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Zeitschriftenartikel zum Thema "Dicarbonyl stress"

Csongová, Melinda, Jean L. J. M. Scheijen, Marjo P. H. van de Waarenburg та ін. "Association of α-Dicarbonyls and Advanced Glycation End Products with Insulin Resistance in Non-Diabetic Young Subjects: A Case-Control Study". Nutrients 14, № 22 (2022): 4929. http://dx.doi.org/10.3390/nu14224929.

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α-Dicarbonyls and advanced glycation end products (AGEs) may contribute to the pathogenesis of insulin resistance by a variety of mechanisms. To investigate whether young insulin-resistant subjects present markers of increased dicarbonyl stress, we determined serum α-dicarbonyls-methylglyoxal, glyoxal, 3-deoxyglucosone; their derived free- and protein-bound, and urinary AGEs using the UPLC/MS-MS method; soluble receptors for AGEs (sRAGE), and cardiometabolic risk markers in 142 (49% females) insulin resistant (Quantitative Insulin Sensitivity Check Index (QUICKI) ≤ 0.319) and 167 (47% females) age-, and waist-to-height ratio-matched insulin-sensitive controls aged 16-to-22 years. The between-group comparison was performed using the two-factor (sex, presence/absence of insulin resistance) analysis of variance; multiple regression via the orthogonal projection to latent structures model. In comparison with their insulin-sensitive peers, young healthy insulin-resistant individuals without diabetes manifest alterations throughout the α-dicarbonyls-AGEs-sRAGE axis, dominated by higher 3-deoxyglucosone levels. Variables of α-dicarbonyls-AGEs-sRAGE axis were associated with insulin sensitivity independently from cardiometabolic risk markers, and sex-specifically. Cleaved RAGE associates with QUICKI only in males; while multiple α-dicarbonyls and AGEs independently associate with QUICKI particularly in females, who displayed a more advantageous cardiometabolic profile compared with males. Further studies are needed to elucidate whether interventions alleviating dicarbonyl stress ameliorate insulin resistance.

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Nigro, Cecilia, Alessia Leone, Francesca Fiory, et al. "Dicarbonyl Stress at the Crossroads of Healthy and Unhealthy Aging." Cells 8, no. 7 (2019): 749. http://dx.doi.org/10.3390/cells8070749.

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Dicarbonyl stress occurs when dicarbonyl metabolites (i.e., methylglyoxal, glyoxal and 3-deoxyglucosone) accumulate as a consequence of their increased production and/or decreased detoxification. This toxic condition has been associated with metabolic and age-related diseases, both of which are characterized by a pro-inflammatory and pro-oxidant state. Methylglyoxal (MGO) is the most reactive dicarbonyl and the one with the highest endogenous flux. It is the precursor of the major quantitative advanced glycated products (AGEs) in physiological systems, arginine-derived hydroimidazolones, which accumulate in aging and dysfunctional tissues. The aging process is characterized by a decline in the functional properties of cells, tissues and whole organs, starting from the perturbation of crucial cellular processes, including mitochondrial function, proteostasis and stress-scavenging systems. Increasing studies are corroborating the causal relationship between MGO-derived AGEs and age-related tissue dysfunction, unveiling a previously underestimated role of dicarbonyl stress in determining healthy or unhealthy aging. This review summarizes the latest evidence supporting a causal role of dicarbonyl stress in age-related diseases, including diabetes mellitus, cardiovascular disease and neurodegeneration.

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Ahmad, Khurshid, Sibhghatulla Shaikh, Eun Ju Lee, Yong-Ho Lee, and Inho Choi. "Consequences of Dicarbonyl Stress on Skeletal Muscle Proteins in Type 2 Diabetes." Current Protein & Peptide Science 21, no. 9 (2020): 878–89. http://dx.doi.org/10.2174/1389203720666191119100759.

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Skeletal muscle is the largest organ in the body and constitutes almost 40% of body mass. It is also the primary site of insulin-mediated glucose uptake, and skeletal muscle insulin resistance, that is, diminished response to insulin, is characteristic of Type 2 diabetes (T2DM). One of the foremost reasons posited to explain the etiology of T2DM involves the modification of proteins by dicarbonyl stress due to an unbalanced metabolism and accumulations of dicarbonyl metabolites. The elevated concentration of dicarbonyl metabolites (i.e., glyoxal, methylglyoxal, 3-deoxyglucosone) leads to DNA and protein modifications, causing cell/tissue dysfunctions in several metabolic diseases such as T2DM and other age-associated diseases. In this review, we recapitulated reported effects of dicarbonyl stress on skeletal muscle and associated extracellular proteins with emphasis on the impact of T2DM on skeletal muscle and provided a brief introduction to the prevention/inhibition of dicarbonyl stress.

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Rabbani, Naila, Mingzhan Xue, and Paul J. Thornalley. "Methylglyoxal-induced dicarbonyl stress in aging and disease: first steps towards glyoxalase 1-based treatments." Clinical Science 130, no. 19 (2016): 1677–96. http://dx.doi.org/10.1042/cs20160025.

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Dicarbonyl stress is the abnormal accumulation of dicarbonyl metabolites leading to increased protein and DNA modification contributing to cell and tissue dysfunction in aging and disease. It is produced by increased formation and/or decreased metabolism of dicarbonyl metabolites. MG (methylglyoxal) is a dicarbonyl metabolite of relatively high flux of formation and precursor of the most quantitatively and functionally important spontaneous modifications of protein and DNA clinically. Major MG-derived adducts are arginine-derived hydroimidazolones of protein and deoxyguanosine-derived imidazopurinones of DNA. These are formed non-oxidatively. The glyoxalase system provides an efficient and essential basal and stress-response-inducible enzymatic defence against dicarbonyl stress by the reduced glutathione-dependent metabolism of methylglyoxal by glyoxalase 1. The GLO1 gene encoding glyoxalase 1 has low prevalence duplication and high prevalence amplification in some tumours. Dicarbonyl stress contributes to aging, disease and activity of cytotoxic chemotherapeutic agents. It is found at a low, moderate and severe level in obesity, diabetes and renal failure respectively, where it contributes to the development of metabolic and vascular complications. Increased glyoxalase 1 expression confers multidrug resistance to cancer chemotherapy and has relatively high prevalence in liver, lung and breast cancers. Studies of dicarbonyl stress are providing improved understanding of aging and disease and the basis for rational design of novel pharmaceuticals: glyoxalase 1 inducers for obesity, diabetes and cardiovascular disease and glyoxalase 1 inhibitors for multidrug-resistant tumours. The first clinical trial of a glyoxalase 1 inducer in overweight and obese subjects showed improved glycaemic control, insulin resistance and vascular function.

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Tatone, Carla, Ursula Eichenlaub-Ritter, and Fernanda Amicarelli. "Dicarbonyl stress and glyoxalases in ovarian function." Biochemical Society Transactions 42, no. 2 (2014): 433–38. http://dx.doi.org/10.1042/bst20140023.

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The ovary is the main regulator of female fertility. Changes in maternal health and physiology can disrupt intraovarian homoeostasis thereby compromising oocyte competence and fertility. Research has only recently devoted attention to the involvement of dicarbonyl stress in ovarian function. On this basis, the present review focuses on clinical and experimental research supporting the role of dicarbonyl overload and AGEs (advanced glycation end-products) as key contributors to perturbations of the ovarian microenvironment leading to lower fertility. Particular emphasis has been given to oocyte susceptibility to methylglyoxal, a powerful glycating agent, whose levels are known to increase during aging and metabolic disorders. According to the literature, the ovary and the oocyte itself can rely on the glyoxalase system to counteract the possible dicarbonyl overload such as that which may occur in reproductive-age women and patients with PCOS (polycystic ovarian syndrome) or diabetes. Overall, although biochemical methods for proper evaluation of dicarbonyl stress in oocytes and the ovarian microenvironment need to be established, AGEs can be proposed as predictive markers and/or therapeutic targets in new strategies for improving reproductive counselling and infertility therapies.

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Masania, Jinit, Malgorzata Malczewska-Malec, Urszula Razny, et al. "Dicarbonyl stress in clinical obesity." Glycoconjugate Journal 33, no. 4 (2016): 581–89. http://dx.doi.org/10.1007/s10719-016-9692-0.

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Alouffi, Sultan, and Mohd Wajid Ali Khan. "Dicarbonyls Generation, Toxicities, Detoxifications and Potential Roles in Diabetes Complications." Current Protein & Peptide Science 21, no. 9 (2020): 890–98. http://dx.doi.org/10.2174/1389203720666191010155145.

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It has been well established that advanced glycation end-products (AGEs) have a strong correlation with diabetes and its secondary complications. Moreover, dicarbonyls, especially, methylglyoxal (MG) and glyoxal, accelerate AGEs formation and hence, have potential roles in the pathogenesis of diabetes. They can also induce oxidative stress and concomitantly decrease the efficiency of antioxidant enzymes. Increased proinflammatory cytokines (tumor necrosis factor-α and interleukin- 1β) are secreted by monocytes due to the dicarbonyl-modified proteins. High levels of blood dicarbonyls have been identified in diabetes and its associated complications (retinopathy, nephropathy and neuropathy). This review aims to provide a better understanding by including in-depth information about the formation of MG and glyoxal through multiple pathways with a focus on their biological functions and detoxifications. The potential role of these dicarbonyls in secondary diabetic complications is also discussed.

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Rabbani, Naila, and Paul J. Thornalley. "Dicarbonyls linked to damage in the powerhouse: glycation of mitochondrial proteins and oxidative stress." Biochemical Society Transactions 36, no. 5 (2008): 1045–50. http://dx.doi.org/10.1042/bst0361045.

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Protection of mitochondrial proteins from glycation by endogenous dicarbonyl compounds, methylglyoxal and glyoxal, was found recently to prevent increased formation of reactive oxygen species and oxidative and nitrosative damage to the proteome during aging and produce life extension in the nematode Caenorhabditis elegans. This suggests that dicarbonyl glycation damage to the mitochondrial proteome may be a preceding event to mitochondrial dysfunction leading to oxidative stress. Future research will address the functional charges in mitochondrial proteins that are the targets for dicarbonyl glycation.

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Mey, Jacob T., Brian K. Blackburn, Edwin R. Miranda, et al. "Dicarbonyl stress and glyoxalase enzyme system regulation in human skeletal muscle." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 314, no. 2 (2018): R181—R190. http://dx.doi.org/10.1152/ajpregu.00159.2017.

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Skeletal muscle insulin resistance is a hallmark of Type 2 diabetes (T2DM) and may be exacerbated by protein modifications by methylglyoxal (MG), known as dicarbonyl stress. The glyoxalase enzyme system composed of glyoxalase 1/2 (GLO1/GLO2) is the natural defense against dicarbonyl stress, yet its protein expression, activity, and regulation remain largely unexplored in skeletal muscle. Therefore, this study investigated dicarbonyl stress and the glyoxalase enzyme system in the skeletal muscle of subjects with T2DM (age: 56 ± 5 yr.; BMI: 32 ± 2 kg/m2) compared with lean healthy control subjects (LHC; age: 27 ± 1 yr.; BMI: 22 ± 1 kg/m2). Skeletal muscle biopsies obtained from the vastus lateralis at basal and insulin-stimulated states of the hyperinsulinemic (40 mU·m−2·min−1)–euglycemic (5 mM) clamp were analyzed for proteins related to dicarbonyl stress and glyoxalase biology. At baseline, T2DM had increased carbonyl stress and lower GLO1 protein expression (−78.8%), which inversely correlated with BMI, percent body fat, and HOMA-IR, while positively correlating with clamp-derived glucose disposal rates. T2DM also had lower NRF2 protein expression (−31.6%), which is a positive regulator of GLO1, while Keap1 protein expression, a negative regulator of GLO1, was elevated (207%). Additionally, insulin stimulation during the clamp had a differential effect on NRF2, Keap1, and MG-modified protein expression. These data suggest that dicarbonyl stress and the glyoxalase enzyme system are dysregulated in T2DM skeletal muscle and may underlie skeletal muscle insulin resistance. Whether these phenotypic differences contribute to the development of T2DM warrants further investigation.

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Antognelli, Cinzia, Andrea Perrelli, Tatiana Armeni, Vincenzo Nicola Talesa, and Saverio Francesco Retta. "Dicarbonyl Stress and S-Glutathionylation in Cerebrovascular Diseases: A Focus on Cerebral Cavernous Malformations." Antioxidants 9, no. 2 (2020): 124. http://dx.doi.org/10.3390/antiox9020124.

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Dicarbonyl stress is a dysfunctional state consisting in the abnormal accumulation of reactive α-oxaldehydes leading to increased protein modification. In cells, post-translational changes can also occur through S-glutathionylation, a highly conserved oxidative post-translational modification consisting of the formation of a mixed disulfide between glutathione and a protein cysteine residue. This review recapitulates the main findings supporting a role for dicarbonyl stress and S-glutathionylation in the pathogenesis of cerebrovascular diseases, with specific emphasis on cerebral cavernous malformations (CCM), a vascular disease of proven genetic origin that may give rise to various clinical signs and symptoms at any age, including recurrent headaches, seizures, focal neurological deficits, and intracerebral hemorrhage. A possible interplay between dicarbonyl stress and S-glutathionylation in CCM is also discussed.

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Dissertationen zum Thema "Dicarbonyl stress"

Ashour, Amal. "Dicarbonyl stress and dysfunction of the glyoxalase system in periodontal diseases." Thesis, University of Warwick, 2016. http://wrap.warwick.ac.uk/80026/.

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Periodontal ligament inflammation or periodontitis is a common disease characterised by gradual destruction of connective tissue fibres that attach a tooth to the alveolar bone within which it sits. Diabetes and inflammation enhances periodontal bone loss through enhanced resorption and diminished bone formation. Periodontal ligament fibroblast attachment to collagen-I and function was impaired by methylglyoxal (MG) modification in vitro. The glyoxalase system is an anti-glycation defence in all cells that metabolises MG and thereby suppresses MG-mediated protein damage. Overexpression of Glo1 decreased the intracellular levels of MG The aim of this investigation was to improve the understanding of protein damage in PDL in diabetes, focusing on protein damage by MG in human periodontal ligament fibroblasts (hPDLFs) in hyperglycaemia and to evaluate the effects of high and low glucose concentrations on MG metabolism in hPDLFs with or without Glo1 inducers. The effect of high glucose concentration on the formation and metabolism of MG was studied in hPDLFs in vitro. The ability of two small molecule Glo1 inducers, individually and in synergistic combination, to counter dicarbonyl stress in hPDLFs in vitro was studied. Interactions between hPDLFs to the extracellular matrix protein, collagen-I, were investigated and impairments in hPDLFs adhesion to MG-modified collagen-I coated plates were assessed. Protein susceptible to MG modification and inactivation in the cytosol of hPDLFs were identified by high resolution mass spectrometry proteomics. The effect of clinical periodontitis on plasma protein glycation, oxidation and nitration was also investigated in a pilot clinical investigation. When hPDLFs were incubated with high glucose concentration in vitro there was a 45% decrease in Glo1 activity and 42% increase in D-lactate flux – surrogate indication of MG flux of formation, which contributed to increased cellular concentration of MG and increase in MG-H1 residue content of cell protein, compared to low glucose control. This indicated dicarbonyl stress was induced in hPDLFs by high glucose concentration in vitro, a model for hyperglycaemia in vivo. Decrease of Glo1 activity and increase in cellular MG concentration and MG-H1 residue content of cell protein was corrected with the addition of Glo1 inducers. The binding of hPDLFs to collagen-I was decreased by 30% in high glucose concentration and was corrected by addition of Glo1 inducers. Proteomics analysis of cytosolic extracts of hPDLFs indicated that high glucose incubations produced changes in MG-modified proteins and also up-regulated and down-regulated unmodified proteins in hPDLFs. The pilot investigation of clinical periodontitis suggested a systemic effect of this local inflammation which was associated with changes in plasma protein glycation, oxidation and nitration. This study reveals that dicarbonyl stress is a potential contributory pathogenic mechanism in hPDLFs in periodontitis and countering it may provide new treatment options to prevent and treat decline in periodontal health, particularly in diabetes. Small molecule inducers of Glo1 expression may in future contribute to improving periodontal health, particularly in diabetes.

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Kimzey, Michael John. "Identification, Characterization, and Quantification of Dicarbonyl Adducts in the Plasma Proteome in Type-2 Diabetes." Diss., The University of Arizona, 2011. http://hdl.handle.net/10150/145123.

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Glyco-oxidation is linked to the pathophysiology of diabetes and diabetic complications. The process of glyco-oxidation generates reactive dicarbonyls, which form adducts on arginine residues in distributions throughout the proteome that are site-specific depending on the protein microenvironment. Dicarbonyl adducts are thus markers for glyco-oxidative stress. Various approaches using mass spectrometry permits the identification, localization, and quantification of these dicarbonyl adducts. Using MG as a model dicarbonyl, a shotgun proteomics approach identified the sites for modification of major plasma proteins. Thirty five sites on seven abundant plasma proteins were found, and investigation into the microenvironment surrounding the target arginine sites revealed a neighboring charged residue motif where adjacent residues were either negatively or positively charged. One of the sites identified was R257 in HSA, which is located in the important drug binding site I. We validated drug site I as a target for MG modification by the adaptation of two assays to monitor the effect of MG modification. MG significantly decreases the rate of hydrolysis of PGE2 in drug site I, and induces the displacement of prodan from drug site I. Molecular modeling of warfarin docking at drug site I with the MG-modified R257 resulted in significantly decreased binding and change in binding orientation. The oxidation products of susceptible residues methionine, tryptophan, and cysteine were evaluated using MRM of oxidized HSA peptides. Oxidation of methionine gave the M+16 single oxidized product, and M329 in HSA was the most responsive site. Oxidation of the sole W214 tryptophan produced the W+32 double oxidation product, and oxidation of C34 produced the C+48 triple oxidation product. MG, 3DG, and glucosone were evaluated for propensity to modify 12 HSA sites based on MRM of dicarbonyl modified HSA. Dicarbonyl modification was independent of arginine solvent accessibility. In a clinical study using nephropathy as an endpoint, sites of oxidation and modification of HSA by MG, 3DG, and glucosone were quantified by MRM. The most important variable among diabetic subjects was metformin use, and subjects taking metformin had significantly reduced markers for glyco-oxidation. These findings may be useful in the development of new diabetes therapies that aim to ameliorate glyco-oxidative stress.

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Rosenstock, Philip [Verfasser], Iris [Gutachter] Thondorf, Rüdiger [Gutachter] Horstkorte, and Lars-Oliver [Gutachter] Klotz. "Untersuchungen humaner natürlicher Killer-Zellen und ihrer Sialyltransferasen nach Dicarbonyl-Stress / Philip Rosenstock ; Gutachter: Iris Thondorf, Rüdiger Horstkorte, Lars-Oliver Klotz." Halle (Saale) : Universitäts- und Landesbibliothek Sachsen-Anhalt, 2020. http://d-nb.info/1215098855/34.

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Halkoum, Rym. "Rôle du glyoxal dans la sénescence cellulaire : implications dans le vieillissement de la peau." Electronic Thesis or Diss., Sorbonne université, 2021. https://accesdistant.sorbonne-universite.fr/login?url=https://theses-intra.sorbonne-universite.fr/2021SORUS016.pdf.

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La sénescence est une réponse cellulaire associée à des marqueurs spécifiques comme un arrêt irréversible du cycle cellulaire ainsi que la sécrétion d’un ensemble de facteurs comme les cytokines, chimiokines et protéases, constituant le SASP, pour Senescence-Associated Secretory Phenotype. Le SASP peut avoir des rôles autocrine et paracrine qui contribuent au renforcement et à la propagation du phénotype sénescent. La composition du SASP et par conséquent son rôle, dépendent notamment du type cellulaire et de la nature du stress inducteur de sénescence. Du fait de sa fonction de barrière avec l’environnement externe, la peau est particulièrement soumise à différents types de stress induisant la sénescence des cellules et un vieillissement prématuré. Le glyoxal, composé dicarbonylé formé au cours des réactions de glycation, d’auto-oxydation du glucose ou de la peroxydation lipidique, est un précurseur des produits avancés de glycation impliqués dans le vieillissement normal et pathologique. Mes travaux de thèse ont permis de montrer que le glyoxal induit la sénescence de kératinocytes humains normaux ainsi qu’une accumulation d’espèces réactives de l’oxygène et de produits avancés de glycation intracellulaires traduisant un état de stress oxydant. L’initiation de cette sénescence est due à l’activation de la voie d’arrêt du cycle cellulaire AKT/FOXO3a/p27KIP1 suivie d’une phase tardive caractérisée par l’activation de la voie p16INK4A/pRb. La caractérisation du phénotype sécrétoire associé à la phase précoce de cette sénescence, a été réalisée par spectrométrie de masse afin d’identifier des facteurs pouvant être ciblés par des ingrédients sénomorphiques<br>Senescence is a well-characterized cellular state associated with specific markers such as permanent cell proliferation arrest, and the secretion of messenger molecules by cells expressing the Senescence-Associated Secretory Phenotype (SASP). The SASP can display autocrine and paracrine effects which contribute to the senescent phenotype reinforcement and propagation. The SASP composition depends on many factors such as the cell type or the nature of the stress that induces senescence. Since the skin constitutes a barrier with the external environment, it is particularly subjected to different types of stresses, and consequently prone to premature cellular aging. Glyoxal, a dicarbonyl compound produced during glucose metabolism and lipid peroxidation, is a precursor of Advanced Glycation End-products (AGEs), whose presence marks normal and pathological aging. My thesis work showed that glyoxal treatment provokes oxidative stress by increasing reactive oxygen species and AGEs levels and induce senescence in human keratinocytes. Furthermore, glyoxal-induced senescence bears a unique molecular progression profile: an “early-stage” when AKT-FOXO3a-p27KIP1 pathway mediates cell-cycle arrest, and a “late-stage” senescence maintained by the p16INK4/pRb pathway. Moreover, we characterized the resulting secretory phenotype during early senescence by mass spectrometry in order to find new targets for senomorphic ingredients. Our study provides evidence that glyoxal can affect keratinocyte functions and act as a driver of human skin aging

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Yang, Kai. "Formation and Metabolism of Sugar Metabolites, Glyoxal and Methylglyoxal, and their Molecular Cytotoxic Mechanisms in Isolated Rat Hepatocytes." Thesis, 2011. http://hdl.handle.net/1807/31650.

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High chronic fructose consumption has been linked to many diseases. Sugar metabolites, especially glyoxal and methylglyoxal can form advanced glycation products, which contribute to the pathology of diabetic complications. Our objective was to study the metabolism of these metabolites and the associated protein carbonyation and cytotoxicity in isolated hepatocytes. In addition, the effect of oxidative stress on the metabolism of these toxins was also investigated. Methylglyoxal and glyoxal can induce protein carbonylation, which contributes to hepatocyte toxicity. Methylglyoxal, but not glyoxal, was detoxified mainly by the glyoxalase system. Both toxins can be metabolized by mitochondrial aldehyde dehydrogenase. The detoxification of glyoxal was impaired under oxidative stress conditions (i.e. increased hydrogen peroxide level). Glyoxal was found to be a common autoxidation product from glyceraldehyde, hydroxypyruvate and glycolaldehyde. Glyoxal and the reactive oxygen species formation during the autoxidation process contributed to the hepatocyte toxicity of glyceraldehyde, hydroxypyruvate and glycolaldehyde.

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Banach, Monica Sofia. "Hepatocyte Cytotoxicity Induced by Hydroperoxide (Oxidative Stress Model) or Dicarbonyls (Carbonylation Model): Prevention by Bioactive Nut Extracts or Catechins." Thesis, 2009. http://hdl.handle.net/1807/18164.

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Carbonyl and oxidative stress augment the development of diabetic complications. We evaluated the cytoprotectiveness of walnut and hazelnut extracts and catechins for decreasing cytotoxicity, lipid peroxidation, reactive oxygen species (ROS) formation, and protein carbonylation in cell death models of carbonyl and oxidative stress. Polar extracts (methanol or water) showed better cytoprotection than the non-polar (ethyl acetate) nut extracts against hydroperoxide-induced hepatocyte cell death and oxidative stress markers. Catechin flavonoids found in plants, including walnuts and hazelnuts, prevented serum albumin carbonylation in a carbonyl stress model (using glyoxal or methylglyoxal). Hepatocyte protein carbonylation and cell death were prevented and UV spectra data suggested a catechin:methylglyoxal adduct was formed. We conclude that (a) bioactive nut constituents in polar extracts were more protective than non-polar extracts against oxidative stress, and (b) catechins were effective under physiological temperature and pH, at preventing dicarbonyl induced cytotoxicity likely by trapping dicarbonyls or reversing early stage carbonylation.

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Buchteile zum Thema "Dicarbonyl stress"

Kovacic, Peter, and Ratnasamy Somanathan. "Novel Mechanism for Advanced Glycation End Product (AGE) Toxicity: α-Dicarbonyls, Electron Transfer, Radicals, Oxidative Stress, and Antioxidants." In Systems Biology of Free Radicals and Antioxidants. Springer Berlin Heidelberg, 2014. http://dx.doi.org/10.1007/978-3-642-30018-9_153.

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Rabbani, Naila, Mingzhan Xue, and Paul J. Thornalley. "Dicarbonyl stress and the glyoxalase system." In Oxidative Stress. Elsevier, 2020. http://dx.doi.org/10.1016/b978-0-12-818606-0.00036-5.

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Konferenzberichte zum Thema "Dicarbonyl stress"

Bulkescher, R., S. Herzig, J. Szendrödi, PP Nawroth, and J. Zemva. "Dicarbonyl stress in endothelial cells alters mitochondrial protein homeostasis." In Late Breaking Abstracts Diabetes Kongress 2021 – 55. Jahrestagung der DDG Präzisionsmedizin – Eine Reise in die Zukunft der Diabetologie www.diabeteskongress.de. Georg Thieme Verlag KG, 2021. http://dx.doi.org/10.1055/s-0041-1730861.

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Bellier, J., MJ Nokin, F. Durieux, et al. "PO-219 Methylglyoxal-induced dicarbonyl stress: role in melanoma progression and response to therapy." In Abstracts of the 25th Biennial Congress of the European Association for Cancer Research, Amsterdam, The Netherlands, 30 June – 3 July 2018. BMJ Publishing Group Ltd, 2018. http://dx.doi.org/10.1136/esmoopen-2018-eacr25.254.

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Bellahcene, A., J. Bellier, O. Peulen, et al. "PO-226 Dicarbonyl stress induces ECM remodelling and MAPK signalling activation in metastatic breast cancer cells." In Abstracts of the 25th Biennial Congress of the European Association for Cancer Research, Amsterdam, The Netherlands, 30 June – 3 July 2018. BMJ Publishing Group Ltd, 2018. http://dx.doi.org/10.1136/esmoopen-2018-eacr25.260.

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