2007
Nutrient-gene interactions in diabetes - advanced glycation end products (AGEs)
KAŇKOVÁ, KateřinaZákladní údaje
Originální název
Nutrient-gene interactions in diabetes - advanced glycation end products (AGEs)
Název česky
Nutrient-gene interactions in diabetes - advanced glycation end products (AGEs)
Autoři
KAŇKOVÁ, Kateřina (203 Česká republika, garant)
Vydání
The Nutrition Society: Diet and Chronic Disease, 2007
Další údaje
Jazyk
angličtina
Typ výsledku
Konferenční abstrakt
Obor
30202 Endocrinology and metabolism
Stát vydavatele
Velká Británie a Severní Irsko
Utajení
není předmětem státního či obchodního tajemství
Kód RIV
RIV/00216224:14110/07:00019461
Organizační jednotka
Lékařská fakulta
Klíčová slova anglicky
Advanced Glycation End-products; RAGE; Maillard Reaction; nutrigenetics
Příznaky
Mezinárodní význam, Recenzováno
Změněno: 2. 4. 2010 15:06, prof. MUDr. Kateřina Kaňková, Ph.D.
V originále
Complex chemical processes called non-enzymatic glycation and glycoxidation taking place in vivo and analogical chemical interactions between sugars and proteins occurring during thermal processing of food (know to the food chemists long ago thanks to the pioneering studies of Louis Camille Maillard almost a century ago) are one of the interesting examples of potentially harmful interaction between nutrition and disease. Non-enzymatic glycation comprise a series of reactions between sugars, a-oxoaldehydes and other sugar derivatives and proteins finally leading - through the early and intermediate stages - to the formation of heterogeneous moieties collectively called Advanced Glycation End-products (AGEs) possessing a wide range of human medicine-related chemical and biological effects. Large body of evidence support causal involvement of glycoxidation and AGEs in the development and/or progression of diabetes-related pathology as wells as several other diseases. Nevertheless, diabetes is of main interest for several reasons: (i) its principal pathogenic feature - chronic hyperglycemia - feeds the substrates for the extra- as well as intracellular glycation, (ii) sustained hyperglycaemia-induced overproduction of superoxide in mitochondrial respiratory chain accelerates AGE formation in the process of glycoxidation, (iii) AGE-modified proteins are subjects of rapid intracellular proteolytic degradation releasing free AGE-adducts into the circulation where they can bind to several pro-inflammatory receptors, especially Receptor of AGEs (RAGE), and, finally, (iv) kidneys are principally involved in the excretion of AGEs and kidney damage (i.e. diabetic nephropathy) is one of the common and unfortunate complications of diabetes further enhancing AGE-toxicity due to diminished AGE clearance. Increased dietary intake of AGEs in highly processed foods by diabetics might thus represent an additional metabolic burden on top of already mentioned alterations. Finally, genetic variability in a class of genes encoding enzymes and receptors involved in either formation or degradation of AGEs (so called "glycoxidation-related genes") is a subject of intense research since an interindividual functional variability in metabolic systems dealing with glycoxidation could have a significant nutrigenomic and nutrigenetic consequences.
Česky
Complex chemical processes called non-enzymatic glycation and glycoxidation taking place in vivo and analogical chemical interactions between sugars and proteins occurring during thermal processing of food (know to the food chemists long ago thanks to the pioneering studies of Louis Camille Maillard almost a century ago) are one of the interesting examples of potentially harmful interaction between nutrition and disease. Non-enzymatic glycation comprise a series of reactions between sugars, a-oxoaldehydes and other sugar derivatives and proteins finally leading - through the early and intermediate stages - to the formation of heterogeneous moieties collectively called Advanced Glycation End-products (AGEs) possessing a wide range of human medicine-related chemical and biological effects. Large body of evidence support causal involvement of glycoxidation and AGEs in the development and/or progression of diabetes-related pathology as wells as several other diseases. Nevertheless, diabetes is of main interest for several reasons: (i) its principal pathogenic feature - chronic hyperglycemia - feeds the substrates for the extra- as well as intracellular glycation, (ii) sustained hyperglycaemia-induced overproduction of superoxide in mitochondrial respiratory chain accelerates AGE formation in the process of glycoxidation, (iii) AGE-modified proteins are subjects of rapid intracellular proteolytic degradation releasing free AGE-adducts into the circulation where they can bind to several pro-inflammatory receptors, especially Receptor of AGEs (RAGE), and, finally, (iv) kidneys are principally involved in the excretion of AGEs and kidney damage (i.e. diabetic nephropathy) is one of the common and unfortunate complications of diabetes further enhancing AGE-toxicity due to diminished AGE clearance. Increased dietary intake of AGEs in highly processed foods by diabetics might thus represent an additional metabolic burden on top of already mentioned alterations. Finally, genetic variability in a class of genes encoding enzymes and receptors involved in either formation or degradation of AGEs (so called "glycoxidation-related genes") is a subject of intense research since an interindividual functional variability in metabolic systems dealing with glycoxidation could have a significant nutrigenomic and nutrigenetic consequences.
Návaznosti
| GP303/02/D127, projekt VaV |
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| KJB501620601, projekt VaV |
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