Glycation


Glycation

Glycation (sometimes called non-enzymatic glycosylation) is the result of the bonding of a protein or lipid molecule with a sugar molecule, such as fructose or glucose, without the controlling action of an enzyme. All blood sugars are reducing molecules. Glycation may occur either inside the body (endogenous glycation) or outside the body (exogenous glycation). Enzyme-controlled addition of sugars to protein or lipid molecules is termed glycosylation; glycation is a haphazard process that impairs the functioning of biomolecules, whereas glycosylation occurs at defined sites on the target molecule and is required in order for the molecule to function. Much of the early laboratory research work on fructose glycations used inaccurate assay techniques that led to drastic underestimation of the importance of fructose in glycation.[1]

Contents

Exogenous

Exogenous, meaning outside the body, may also be referred to as dietary or pre-formed. Exogenous glycations and Advanced Glycation Endproducts (AGEs) are formed when sugars are cooked with proteins or fats. Temperatures over 120°C (~248°F) greatly accelerate the reactions, but lower temperatures with longer cooking times also promote their formation.

These compounds are absorbed by the body during digestion with about 30% efficiency. Browning reactions (usually Maillard type reactions) are evidence of pre-formed glycations. Indeed, sugar is often added to products such as french fries and baked goods to enhance browning. Glycation may also contribute to the formation of acrylamide,[2] a potential carcinogen, during cooking. Until recently, it was thought that exogenous glycations and AGEs were negligible contributors to inflammation and disease states, but recent work has shown that they are important.[3] Although most of the research on this topic has been done with reference to diabetes, these results are likely to be important for all people, as exogenous AGEs are implicated in the initiation of retinal dysfunction, cardiovascular diseases, type II diabetes, and many other age-related chronic diseases.

Food manufacturers have added AGEs to foods, especially in the last 50 years, as flavor enhancers and colorants to improve appearance.[4] Foods with significant browning, caramelization, or directly added preformed AGEs can be exceptionally high in these proinflammatory and disease-initiating compounds. A very partial listing of foods with very high exogenous AGEs includes donuts, barbecued meats, cake, and dark colored soda pop.[5]

Endogenous

Endogenous glycations occur mainly in the bloodstream to a small proportion of the absorbed simple sugars: glucose, fructose, and galactose. It appears that fructose and galactose have approximately ten times the glycation activity of glucose, the primary body fuel.[6] Glycation is the first step in the evolution of these molecules through a complex series of very slow reactions in the body known as Amadori reactions, Schiff base reactions, and Maillard reactions; which lead to advanced glycation endproducts (AGEs). Some AGEs are benign, but others are more reactive than the sugars they are derived from, and are implicated in many age-related chronic diseases such as: cardiovascular diseases (the endothelium, fibrinogen, and collagen are damaged), Alzheimer's disease (amyloid proteins are side-products of the reactions progressing to AGEs),[7][8] cancer (acrylamide and other side-products are released), peripheral neuropathy (the myelin is attacked), and other sensory losses such as deafness (due to demyelination). This range of diseases is the result of the very basic level at which glycations interfere with molecular and cellular functioning throughout the body and the release of highly-oxidizing side-products such as hydrogen peroxide.

Red blood cells have a consistent lifespan of 120 days and are easily accessible for measurement of recent increased presence of glycating product. This fact is used in monitoring blood sugar control in diabetes by monitoring the glycated hemoglobin level, also known as HbA1c. As a consequence, long-lived cells (such as nerves, brain cells), long-lasting proteins (such as eye crystalline and collagen), and DNA may accumulate substantial damage over time. Cells such as the retina cells in the eyes, and beta cells (insulin-producing) in the pancreas are also at high risk of damage[citation needed]. Damage by glycation results in stiffening of the collagen in the blood vessel walls, leading to high blood pressure, especially in diabetes.[9] Glycations also cause weakening of the collagen in the blood vessel walls[citation needed], which may lead to micro- or macro-aneurisms; this may cause strokes if in the brain.

See also

References

  1. ^ Ahmed N, Furth AJ (July 1992). "Failure of common glycation assays to detect glycation by fructose". Clin. Chem. 38 (7): 1301–3. PMID 1623595. 
  2. ^ Stadler RH, Blank I, Varga N, et al. (October 2002). "Acrylamide from Maillard reaction products". Nature 419 (6906): 449–50. doi:10.1038/419449a. PMID 12368845. 
  3. ^ Vlassara H (June 2005). "Advanced glycation in health and disease: role of the modern environment". Ann. N. Y. Acad. Sci. 1043 (1): 452–60. doi:10.1196/annals.1333.051. PMID 16037266. 
  4. ^ Peppa, Melpomeni et al. (2003). "Glucose, Advanced Glycation End Products, and Diabetes Complications: What Is New and What Works". Clinical Diabetes 21 (4). http://web.archive.org/web/20061023013648/http://www.alteon.com/scientific_publications/role/Vlassara.pdf. 
  5. ^ Koschinsky T, He CJ, Mitsuhashi T, et al. (June 1997). "Orally absorbed reactive glycation products (glycotoxins): an environmental risk factor in diabetic nephropathy". Proc. Natl. Acad. Sci. U.S.A. 94 (12): 6474–9. doi:10.1073/pnas.94.12.6474. PMC 21074. PMID 9177242. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=21074. 
  6. ^ McPherson JD, Shilton BH, Walton DJ (March 1988). "Role of fructose in glycation and cross-linking of proteins". Biochemistry 27 (6): 1901–7. doi:10.1021/bi00406a016. PMID 3132203. 
  7. ^ Münch, Gerald; et al (27). "Influence of advanced glycation end-products and AGE-inhibitors on nucleation-dependent polymerization of β-amyloid peptide". Biochimica et Biophysica Acta 1360 (1): 17–29. doi:10.1016/S0925-4439(96)00062-2. http://www.sciencedirect.com/science/article/pii/S0925443996000622. 
  8. ^ Munch, G; Deuther-Conrad W, Gasic-Milenkovic J. (2002). "Glycoxidative stress creates a vicious cycle of neurodegeneration in Alzheimer's disease--a target for neuroprotective treatment strategies?". J Neural Transm Suppl. 62 (62): 303–307. PMID 12456073. 
  9. ^ Soldatos, G.; Cooper ME (Dec 2006). "Advanced glycation end products and vascular structure and function". Curr Hypertens Rep 8 (6): 472–478. PMID 17087858. 

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Look at other dictionaries:

  • Glycation — La réaction de Maillard, connue dans le monde médical sous le nom de « glycation non enzymatique des protéines », a d’abord été étudiée dans le cadre du diabète sucré grâce à l’hémoglobine glyquée. La glycation est une réaction… …   Wikipédia en Français

  • glycation — The nonenzymic reaction that forms a glycate. * * * n. the chemical linkage of glucose to a protein, to form a glycoprotein. Glycation of body proteins has been postulated as a cause of complications of diabetes mellitus. See advanced… …   Medical dictionary

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  • glycation — noun non enzymatic reaction of a sugar and an amine group of a protein to form a glycoprotein …   Wiktionary

  • Advanced glycation end product — Advanced Glycation End products (AGEs) are the result of a chain of chemical reactions after an initial glycation reaction. The intermediate products are known, variously, as Amadori, Schiff base and Maillard products, named after the researchers …   Wikipedia

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  • advanced glycation end products — (AGE) irreversible products of the glycation of proteins, which cause tissue damage; seen when blood glucose concentrations are chronically elevated such as in diabetes mellitus, arthritis, and aging …   Medical dictionary

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  • nonenzymatic glycosylation — glycation …   Medical dictionary

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