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首页> 外文期刊>The Biochemical Journal >Fructosamine 3-kinase is involved in an intracellular deglycation pathway in human erythrocytes
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Fructosamine 3-kinase is involved in an intracellular deglycation pathway in human erythrocytes

机译：果糖胺3激酶参与人红细胞的细胞内去糖途径

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摘要

Fructosamine 3-kinase, which phosphorylates low-molecular-mass and protein-bound fructosamines on the third carbon of their deoxyfructose moiety, is quite active in erythrocytes, and was proposed to initiate a process removing fructosamine residues from proteins. In the present study, we show that incubation of human erythrocytes with 200 mM glucose not only caused the progressive formation of glycated haemoglobin, but also increased the level of an anionic form of haemoglobin containing alkali-labile phosphate, to approx. 5% of total haemoglobin. 1-Deoxy-1-morpholinofructose (DMF), a substrate and competitive inhibitor of fructosamine 3-kinase, doubled the rate of accumulation of glycated haemoglobin, but markedly decreased the amount of haemoglobin containing alkali-labile phosphate. The latter corresponds therefore to haemoglobin bound to a fructosamine 3-phosphate group (FN3P-Hb). Returning erythrocytes incubated with 200 mM glucose and DMF to a low-glucose medium devoid of DMF caused a decrease in the amount of glycated haemoglobin, a transient increase in FN3P-Hb and a net decrease in the sum (glycated haemoglobin+FN3P-Hb). These effects were prevented by DMF, indicating that fructosamine 3-kinase is involved in the removal of fructosamine residues. The second step of this 'deglycation' process is most likely a spontaneous decomposition of the fructosamine 3-phosphate residues to a free amine, 3-deoxyglucosone and P-1. This is consistent with the findings that 2-oxo-3-deoxygluconate, the product of 3-deoxyglucosone oxidation, is formed in erythrocytes incubated for 2 days with 200 mM glucose in a sufficient amount to account for the removal of fructosamine residues from proteins, and that DMF appears to inhibit the formation of 2-oxo-3-deoxygluconate from elevated glucose concentrations. [References: 30]
机译：果糖胺3-激酶可在其脱氧果糖部分的第三个碳上磷酸化低分子质量和与蛋白质结合的果糖胺，在红细胞中非常活跃，并提出启动从蛋白质中去除果糖胺残基的方法。在本研究中，我们显示了将人类红细胞与200 mM葡萄糖一起孵育不仅会导致糖化血红蛋白的逐步形成，而且还会使阴离子型血红蛋白的含量增加至碱性（大约）。占总血红蛋白的5％。果糖3激酶的底物和竞争性抑制剂1-脱氧-1-吗啉果糖（DMF）使糖化血红蛋白的积累速率增加了一倍，但显着降低了含碱不稳定磷酸盐的血红蛋白含量。因此，后者对应于与果糖胺3-磷酸基团（FN3P-Hb）结合的血红蛋白。用200 mM葡萄糖和DMF孵育的红细胞返回到不含DMF的低葡萄糖培养基中会导致糖化血红蛋白量减少，FN3P-Hb瞬时增加和总和净减少（糖化血红蛋白+ FN3P-Hb） 。 DMF阻止了这些作用，表明果糖胺3激酶参与了果糖胺残基的去除。 “脱糖”过程的第二步很可能是果糖胺3-磷酸残基自发分解为游离胺，3-脱氧葡糖苷和P-1。这与以下发现相吻合：在含有200 mM葡萄糖的条件下孵育2天的红细胞中形成了2-脱氧3-脱氧葡萄糖酸氧化产物2-氧化3-脱氧葡萄糖酸酯，该量足以说明从蛋白质中去除了果糖胺残基，而且DMF似乎可以抑制葡萄糖浓度升高引起的2-oxo-3-deoxygluconate的形成。 [参考：30]

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