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Relevant bibliographies by topics / Dicarbonyl stress

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Academic literature on the topic 'Dicarbonyl stress'

Author: Grafiati

Published: 25 May 2024

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Journal articles on the topic "Dicarbonyl stress"

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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)

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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

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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 a

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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 imidazop

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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

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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

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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 g

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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 subjec

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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 mal

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Dissertations / Theses on the topic "Dicarbonyl stress"

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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

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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 m

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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

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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 glyoxa

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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,

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Book chapters on the topic "Dicarbonyl stress"

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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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Conference papers on the topic "Dicarbonyl stress"

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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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