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Science Forum Index » Life Extension Forum » Fructose-mediated non-enzymatic glycation: sweet...
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| Olafur Pall Olafsson... |
 Posted: Sat May 24, 2008 11:59 am |
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Diabetes Metab Res Rev. 2004 Sep-Oct;20(5):369-82.
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Fructose-mediated non-enzymatic glycation: sweet coupling or bad
modification.
Schalkwijk CG, Stehouwer CD, van Hinsbergh VW.
Department of Clinical Chemistry, VU University Medical Centre,
Amsterdam, The Netherlands. c.schalkwijk at (no spam) vumc.nl
The Maillard reaction is a process in which reducing sugars react
spontaneously with amino groups in proteins to advanced glycation end
products (AGEs). Although an elevated level of glucose had been
thought to play a primary role in the Maillard reaction, on a
molecular basis, glucose is among the least reactive sugars within
biological systems. The formation of AGEs is now also known to result
from the action of various metabolites other than glucose, which are
primarily located intracellularly and participate in the non-enzymatic
glycation reaction at a much faster rate, such as fructose, trioses
and dicarbonyl compounds. In this review, we considered the glycation
reaction with particular attention to the potential role of fructose
and fructose metabolites. The two sources for fructose are an
exogenous supply from the diet and the endogenous formation from
glucose through the aldose reductase pathway. Despite its
approximately eightfold higher reactivity, the contribution of
extracellular glycation by fructose is considerably less than that by
glucose, because of the low plasma concentration of fructose (5 mmol/L
glucose vs 35 micro mol/L fructose). Intracellularly, fructose is
elevated in a number of tissues of diabetic patients in which the
polyol pathway is active. In the cells of these tissues, the
concentrations of fructose and glucose are of the same magnitude.
Although direct evidence is not yet available, it is likely that the
high reactivity of fructose and its metabolites may substantially
contribute to the formation of intracellular AGEs and may contribute
to alterations of cellular proteins, dysfunction of cells and,
subsequently, to vascular complications. Copyright 2004 John Wiley &
Sons, Ltd.
Publication Types:
* Research Support, Non-U.S. Gov't
* Review
PMID: 15343583 [PubMed - indexed for MEDLINE]
Related Articles
* Rapid formation of advanced glycation end products by
intermediate metabolites of glycolytic pathway and polyol pathway.
[Biochem Biophys Res Commun. 1996]
* Maillard reactions by alpha-oxoaldehydes: detection of glyoxal-
modified proteins. [Biochim Biophys Acta. 2000]
* Intrinsic toxicity of glucose, due to non-enzymatic glycation,
is controlled in-vivo by deglycation systems including: FN3K-mediated
deglycation of fructosamines and transglycation of aldosamines. [Med
Hypotheses. 2005]
* Acceleration of fructose mediated collagen glycation. [J Int Med
Res. 1989]
* TAGE (toxic AGEs) theory in diabetic complications. [Curr Mol
Med. 2006]
* » See all Related Articles |
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