THE EFFECTS OF AMINOGUANIDINE ON THE GLYCATION (NONENZYMATIC GLYCOSYLATION) OF LENS PROTEINS
THE EFFECTS OF AMINOGUANIDINE ON THE GLYCATION (NONENZYMATIC GLYCOSYLATION) OF LENS PROTEINS
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DOI：
10.1016/0014-4835(90)90033-q
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发表时间：
1990-05-01
影响因子：
3.4
通讯作者：
HARDING, JJ
中科院分区：
文献类型：
--
作者：
LEWIS, BS;HARDING, JJ
氨基胍正在被研究作为一种可能的药物来预防糖尿病并发症，通过阻断由蛋白质糖化（非酶糖基化）形成的 Amadori 产品的反应性羰基。因此它可以防止随后的褐变和交联步骤。在目前的工作中，我们表明标记的氨基胍与糖化晶状体蛋白结合。我们还表明，氨基胍抑制晶状体蛋白糖化的第一步，但对氨甲酰化（与氰酸盐的反应）没有影响。因此，氨基胍似乎可以防止糖化以及褐变反应，并且可能不像其他假定的抗白内障药物那样通过作用于蛋白质来实现这一点，而是通过降低糖的活性醛形式的浓度来实现这一点。
Aminoguanidine is being studied as a possible drug to prevent diabetic complications, by blocking the reactive carbonyl group of the Amadori product formed by glycation (non-enzymic glycosylation) of proteins. Thus it prevents the later browning and cross-linking steps. In the present work we show that labelled aminoguanidine becomes bound to glycated lens proteins. We also show that aiminoguanidine inhibits the first steps of glycation of lens proteins but has no effect on carbamylation, the reaction with cyanate. It appears, therefore, that aminoguanidine can prevent glycation as well as the browning reactions, and may do so not by acting on the proteins, as other putative anti-cataract drugs do, but by decreasing the concentration of the active aldehyde form of the sugars.