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A high concentration of glucose can result in non-enzymatic oxidation of proteins by reaction of glucose and lysine residues (glycation). Zusätzlich bieten wir Ihnen Fructosamine 3 Kinase Antikörper (55) und Fructosamine 3 Kinase Proteine (8) und viele weitere Produktgruppen zu diesem Protein an.
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Data conclude that FN3K may play a key role in the GGap and thus diabetes complications such that FN3K may be a potential predictor of the risk of diabetes complications. Pharmacological modifications of its activity may provide a novel approach to their prevention.
We conclude that, despite its ability to reduce the glycation of intracellular islet proteins, FN3K is neither required for the maintenance of beta-cell survival and function under control conditions.
fructosamine 3-kinase and fructosamine 3-kinase-related protein have roles in repairing damage caused by ribose 5-phosphate
These data indicate that FN3K serves as a protein repair enzyme and also in the metabolism of endogenously produced free fructose-epsilon-lysine.
In a multiple regression analysis, FN3K rs1056534, TF polymorphism and presence of diabetes mellitus were predictors for HHV-8 infection.
FN3K could act in concert with other molecular mechanisms and may impact on gene expression and activity of other enzymes involved in deglycation process
Report association of rs1056534 and rs3848403 of fructosamine 3-kinase gene with sRAGE in patients with diabetes.
The marginal association of rs1056534 of FN3K is located in exon 6 with diabetic nephropathy progression.
two new mutations and additional variants within the FN3K gene in diabetic patients
These findings suggest that deglycating enzymes Glyoxalase I and fructosamine-3-kinase may be involved in the malignant transformation of colon mucosa.
G900C polymorphism associates with the level of HbA (1c) and the onset of type 2 diabetes mellitus, but not with either of the diabetic microvascular complications.
involved in the removal of fructosamine residues from hemoglobin in erythrocytes.
The aim of this work was to identify the fructosamine residues on hemoglobin that are removed as a result of the action of FN3K in intact erythrocytes.
These data suggest that FN3K and FN3KRP act as protein repair enzymes and are expressed constitutively in human cells independently of some of the variables altered in the diabetic state.
Enzyme is a constitutive "housekeeping" gene and that ig plays an important role in cell metabolism, possibly as a deglycating enzyme.
No significant correlation between FN3K activity and the levels of HbA1c, total glycated haemoglobin (GHb) and haemoglobin fructoselysine residues, either in the normoglycaemic or diabetic group.
In this paper we propose a resolution of both these quandaries by proposing that fructosamine-6-phosphates are deglycated by phosphorylation to fructosamine-3,6-bisphosphates catalyzed by FN3KRP and/or possibly FN3K.
A high concentration of glucose can result in non-enzymatic oxidation of proteins by reaction of glucose and lysine residues (glycation). Proteins modified in this way, fructosamines, are less active or functional. This gene encodes an enzyme which catalyzes the phosphorylation of fructosamines which may result in deglycation.
, fructosamine 3-kinase