Consumption of a Diet Low in Advanced Glycation End Products for 4 Weeks Improves Insulin Sensitivity in Overweight Women
Alicja Budek MarkMalene W. PoulsenStine AndersenJeanette Marker AndersenMonika BąkChristian RitzJens J. HolstJohn NielsenBarbora de CourtenLars Ove DragstedSusanne Bügel
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OBJECTIVE High-heat cooking of food induces the formation of advanced glycation end products (AGEs), which are thought to impair glucose metabolism in type 2 diabetic patients. High intake of fructose might additionally affect endogenous formation of AGEs. This parallel intervention study investigated whether the addition of fructose or cooking methods influencing the AGE content of food affect insulin sensitivity in overweight individuals. RESEARCH DESIGN AND METHODS Seventy-four overweight women were randomized to follow either a high- or low-AGE diet for 4 weeks, together with consumption of either fructose or glucose drinks. Glucose and insulin concentrations-after fasting and 2 h after an oral glucose tolerance test-were measured before and after the intervention. Homeostasis model assessment of insulin resistance (HOMA-IR) and insulin sensitivity index were calculated. Dietary and urinary AGE concentrations were measured (liquid chromatography tandem mass spectrometry) to estimate AGE intake and excretion. RESULTS When adjusted for changes in anthropometric measures during the intervention, the low-AGE diet decreased urinary AGEs, fasting insulin concentrations, and HOMA-IR, compared with the high-AGE diet. Addition of fructose did not affect any outcomes. CONCLUSIONS Diets with high AGE content may increase the development of insulin resistance. AGEs can be reduced by modulation of cooking methods but is unaffected by moderate fructose intake.Non-enzymatic glycation of proteins occurs in intrinsic and extrinsic skin aging resulting in the formation of advanced glycation end products (AGEs). Proteins such as collagen and elastin are particularly susceptible to AGE modification. Glycated collagen is cross-linked, stiff, difficult to repair and remove from tissues. Sun exposure exacerbates glycation resulting in AGE modification of elastin which has been identified in areas of actinic elastosis. In addition, AGEs have direct effects on tissue and interact with receptors for AGEs (RAGE) increasing oxidative stress and inflammation. The use of nutritional antioxidants and cosmeceuticals that inhibit glycation will be discussed as a strategy to prevent AGE formation and ultimately skin aging.
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The glycation reaction by fructose, as well as that by glucose, in control and diabetic rat lens was analyzed by using antibodies which specifically recognize adducts of lysine with fructose and with glucose. Levels of fructose adducts in diabetic rat lens were 2.5 times that of the control, and correlated with sorbitol levels. This was mainly due to enhanced glycation of β‐ and γ‐crystallins by fructose under diabetic conditions. These data suggest that glycation by fructose may also play a role in cataract formation under conditions of diabetes and aging.
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Overweight and obesity as well as associated metabolic disorders belong to the most important risk factors. During the exhibition 'Heureka' in Zurich data on body weight and size as well as on other clinical and biochemical parameters were collected by a questionnaire. Age- and gender-specific prevalence rates were calculated. Between 10 and 41% of the visitors showed a body-mass index of > or = 25 kg/m2, as a function of age and gender -0.7 to 6.2% showed a body-mass index of > or = 30 kg/m2. The most important increase in body weight was found in the age groups between 20 and 40 years. The presented epidemiologic data show that overweight is common in Switzerland, too. Prevention of overweight is still one of the most rational medical strategies and should be intensified in the age group between 20 and 40.
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Human lenses of three different ages were used to study the effect of age and aspirin treatment on glycation of alpha-, beta- and gamma-crystallins. Soluble lens proteins were subjected to in vitro glycation with 5 mM [14C]glucose in the presence and absence of 10 mM aspirin. With crystallins from a 27-year-old lens alpha-crystallin was the most readily glycated protein. Glycation of all crystallins decreased substantially (37-77%) in 46- and 67-year-old lenses indicating an age-dependent decline in glycation sites. On the basis of a sensitive chemical assay for protein-bound glycogroups in lenses of 2-82 years of age this decline is apparently due to a 60% increase in in vivo glycation. Aspirin did not show any selectivity with regard to its ability to inhibit glycation of various crystallins. Irrespective of the age glycation of all crystallins was inhibited to a varying extent.
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Advanced glycation end-products (AGEs) are formed during non-enzymatic glycation--the process occurring in vitro and in the organism. The glycation products accumulate in tissues and interact with specific receptors, what induces various cellular responses. Some enzymes important in metabolism can be also glycated. The disturbances of homeostasis, related to the glycation products, are the reason for complications observed in diabetes and aging processes. There are presented in this paper: mechanism of the formation of AGEs, their cellular receptor (RAGE), as well as the effects of glycation in aging, diabetes and Alzheimer disease. Finally, there are described the compounds which could be useful as inhibitors of glycation in clinical practice.
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