Glycation: Difference between revisions
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These compounds are absorbed by the body during digestion with about 30% efficiency. Browning reactions (usually [[Maillard reaction | 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]]<ref>{{cite journal |author=Stadler RH, Blank I, Varga N, ''et al.'' |title=Acrylamide from Maillard reaction products |journal=Nature |volume=419 |issue=6906 |pages=449–50 |year=2002 |month=October |pmid=12368845 |doi=10.1038/419449a}}</ref>, 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<ref>{{cite journal |author=Vlassara H |title=Advanced glycation in health and disease: role of the modern environment |journal=Ann. N. Y. Acad. Sci. |volume=1043 |issue= |pages=452–60 |year=2005 |month=June |pmid=16037266 |doi=10.1196/annals.1333.051}}</ref>. Although most of the research work has been done with reference to diabetes, these results are most likely 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. |
These compounds are absorbed by the body during digestion with about 30% efficiency. Browning reactions (usually [[Maillard reaction | 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]]<ref>{{cite journal |author=Stadler RH, Blank I, Varga N, ''et al.'' |title=Acrylamide from Maillard reaction products |journal=Nature |volume=419 |issue=6906 |pages=449–50 |year=2002 |month=October |pmid=12368845 |doi=10.1038/419449a}}</ref>, 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<ref>{{cite journal |author=Vlassara H |title=Advanced glycation in health and disease: role of the modern environment |journal=Ann. N. Y. Acad. Sci. |volume=1043 |issue= |pages=452–60 |year=2005 |month=June |pmid=16037266 |doi=10.1196/annals.1333.051}}</ref>. Although most of the research work has been done with reference to diabetes, these results are most likely 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. |
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Food manufacturers have added AGEs to foods, especially in the last 50 years, as flavor enhancers and colorants to improve appearance <ref>Melpomeni Peppa, et al., "[http://www.alteon.com/scientific_publications/role/Vlassara.pdf Glucose, Advanced Glycation End Products, and Diabetes Complications: What Is New and What Works]", ''Clinical Diabetes'' • Volume '''21''', Number 4, 2003</ref>. Foods with significant browning, caramelization, or with 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<ref>{{cite journal |author=Koschinsky T, He CJ, Mitsuhashi T, ''et al.'' |title=Orally absorbed reactive glycation products (glycotoxins): an environmental risk factor in diabetic nephropathy |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue=12 |pages=6474–9 |year=1997 |month=June |pmid=9177242 |pmc=21074}}</ref>. |
Food manufacturers have added AGEs to foods, especially in the last 50 years, as flavor enhancers and colorants to improve appearance <ref>Melpomeni Peppa, et al., "[http://www.alteon.com/scientific_publications/role/Vlassara.pdf Glucose, Advanced Glycation End Products, and Diabetes Complications: What Is New and What Works]", ''Clinical Diabetes'' • Volume '''21''', Number 4, 2003</ref>. Foods with significant browning, caramelization, or with 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<ref>{{cite journal |doi=10.1073/pnas.94.12.6474 |author=Koschinsky T, He CJ, Mitsuhashi T, ''et al.'' |title=Orally absorbed reactive glycation products (glycotoxins): an environmental risk factor in diabetic nephropathy |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue=12 |pages=6474–9 |year=1997 |month=June |pmid=9177242 |pmc=21074}}</ref>. |
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==Endogenous== |
==Endogenous== |
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{{Unreferenced section|date=November 2009}} |
{{Unreferenced section|date=November 2009}} |
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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<ref>{{cite journal |author=McPherson JD, Shilton BH, Walton DJ |title=Role of fructose in glycation and cross-linking of proteins |journal=Biochemistry |volume=27 |issue=6 |pages=1901–7 |year=1988 |month=March |pmid=3132203}}</ref>. |
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<ref>{{cite journal |doi=10.1021/bi00406a016 |author=McPherson JD, Shilton BH, Walton DJ |title=Role of fructose in glycation and cross-linking of proteins |journal=Biochemistry |volume=27 |issue=6 |pages=1901–7 |year=1988 |month=March |pmid=3132203}}</ref>. |
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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 product|Amadori reaction]]s, [[Schiff base|Schiff base reaction]]s, and [[Maillard reaction]]s; all lead to [[advanced glycation endproduct]]s (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 disease]]s (the endothelium, fibrinogen, and collagen are damaged), [[Alzheimer's disease]] (amyloid proteins are side-products of the reactions progressing to AGEs), [[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]]. |
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 product|Amadori reaction]]s, [[Schiff base|Schiff base reaction]]s, and [[Maillard reaction]]s; all lead to [[advanced glycation endproduct]]s (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 disease]]s (the endothelium, fibrinogen, and collagen are damaged), [[Alzheimer's disease]] (amyloid proteins are side-products of the reactions progressing to AGEs), [[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]]. |
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Revision as of 13:33, 30 July 2010
Glycation (sometimes called non-enzymatic glycosylation) is the result of a sugar molecule, such as fructose or glucose, bonding to a protein or lipid molecule 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].
Exogenous
Exogenous, meaning outside the body, may also be referred to as dietary or pre-formed. Exogenous glycations and Advanced Glycation Endproducts (AGEs) are typically 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 work has been done with reference to diabetes, these results are most likely 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 with 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; all 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), 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.
Glycated substances are eliminated from the body slowly, since the renal clearance factor is only about 30%[citation needed]. This implies that the half-life of a glycation within the body is about double the average cell life [original research?]. 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[citation needed]. 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
- ^ Ahmed N, Furth AJ (1992). "Failure of common glycation assays to detect glycation by fructose". Clin. Chem. 38 (7): 1301–3. PMID 1623595.
{{cite journal}}: Unknown parameter|month=ignored (help) - ^ Stadler RH, Blank I, Varga N; et al. (2002). "Acrylamide from Maillard reaction products". Nature. 419 (6906): 449–50. doi:10.1038/419449a. PMID 12368845.
{{cite journal}}: Explicit use of et al. in:|author=(help); Unknown parameter|month=ignored (help)CS1 maint: multiple names: authors list (link) - ^ Vlassara H (2005). "Advanced glycation in health and disease: role of the modern environment". Ann. N. Y. Acad. Sci. 1043: 452–60. doi:10.1196/annals.1333.051. PMID 16037266.
{{cite journal}}: Unknown parameter|month=ignored (help) - ^ Melpomeni Peppa, et al., "Glucose, Advanced Glycation End Products, and Diabetes Complications: What Is New and What Works", Clinical Diabetes • Volume 21, Number 4, 2003
- ^ Koschinsky T, He CJ, Mitsuhashi T; et al. (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.
{{cite journal}}: Explicit use of et al. in:|author=(help); Unknown parameter|month=ignored (help)CS1 maint: multiple names: authors list (link) - ^ McPherson JD, Shilton BH, Walton DJ (1988). "Role of fructose in glycation and cross-linking of proteins". Biochemistry. 27 (6): 1901–7. doi:10.1021/bi00406a016. PMID 3132203.
{{cite journal}}: Unknown parameter|month=ignored (help)CS1 maint: multiple names: authors list (link)