Assay for lipid peroxides in animal tissues by thiobarbituric acid reaction

Structure-antioxidant activity relationships of flavonoids and phenolic acids

Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes.

Ju Mei,†,‡,∥ Nelson L. C. Leung,†,‡,∥ Ryan T. K. Kwok,†,‡ Jacky W. Y. Lam,†,‡ and Ben Zhong Tang*,†,‡,§ †HKUST-Shenzhen Research Institute, Hi-Tech Park, Nanshan, Shenzhen 518057, China ‡Department of Chemistry, HKUST Jockey Club Institute for Advanced Study, Institute of Molecular Functional Materials, Division of Biomedical Engineering, State Key Laboratory of Molecular Neuroscience, Division of Life Science, The Hong Kong University of Science and Technology, Clear Water Bay, Kowloon, Hong Kong, China Guangdong Innovative Research Team, SCUT-HKUST Joint Research Laboratory, State Key Laboratory of Luminescent Materials and Devices, South China University of Technology, Guangzhou 510640, China

Aggregation-Induced Emission: Together We Shine, United We Soar!

N epsilon-(carboxymethyl)lysine, N epsilon-(carboxymethyl)hydroxylysine, and the fluorescent cross-link pentosidine are formed by sequential glycation and oxidation reactions between reducing sugars and proteins. These compounds, termed glycoxidation products, accumulate in tissue collagen with age and at an accelerated rate in diabetes. Although glycoxidation products are present in only trace concentrations, even in diabetic collagen, studies on glycation and oxidation of model proteins in vitro suggest that these products are biomarkers of more extensive underlying glycative and oxidative damage to the protein. Possible sources of oxidative stress and damage to proteins in diabetes include free radicals generated by autoxidation reactions of sugars and sugar adducts to protein and by autoxidation of unsaturated lipids in plasma and membrane proteins. The oxidative stress may be amplified by a continuing cycle of metabolic stress, tissue damage, and cell death, leading to increased free radical production and compromised free radical inhibitory and scavenger systems, which further exacerbate the oxidative stress. Structural characterization of the cross-links and other products accumulating in collagen in diabetes is needed to gain a better understanding of the relationship between oxidative stress and the development of complications in diabetes. Such studies may lead to therapeutic approaches for limiting the damage from glycation and oxidation reactions and for complementing existing therapy for treatment of the complications of diabetes.

Role of Oxidative Stress in Development of Complications in Diabetes

Lipid peroxide level in plasma of diabetic patients.

Reaction of linoleic acid hydroperoxide with thiobarbituric acid.

Loss of Molecular Interaction between Cytochrome c and Cardiolipin Due to Lipid Peroxidation

The restriction endonuclease Sma I has been used for the diagnosis of neurogenic muscle weakness, ataxia and retinitis pigmentosa disease or Leigh’s disease, caused by the Mt8993T→G

Nobuko Ohishi

Papers

Assay for lipid peroxides in animal tissues by thiobarbituric acid reaction

Lipid peroxide level in plasma of diabetic patients.

Reaction of linoleic acid hydroperoxide with thiobarbituric acid.

Loss of Molecular Interaction between Cytochrome c and Cardiolipin Due to Lipid Peroxidation

Gene therapy for mitochondrial disease by delivering restriction endonuclease SmaI into mitochondria.