Modification of glucose-6-phosphate dehydrogenase by 4-hydroxy-2-nonenal. Formation of cross-linked protein that inhibits the multicatalytic protease.
Modification of glucose-6-phosphate dehydrogenase by 4-hydroxy-2-nonenal. Formation of cross-linked protein that inhibits the multicatalytic protease.
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发表时间：
1994-08
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通讯作者：
B. Friguet;E. Stadtman;L. Szweda
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作者：
B. Friguet;E. Stadtman;L. Szweda
肠膜明串珠菌的葡萄糖-6-磷酸脱氢酶（Glu-6-PDH）与脂质过氧化产物4-羟基-2-壬烯醛一起孵育导致交联蛋白的形成。这是伴随着与蛋白质相关的荧光与激发和发射最大值分别为340和415 nm的外观，并与组氨酸和赖氨酸残基的消失。交联蛋白比天然Glu-6-PDH对多催化蛋白酶的蛋白水解不太敏感，多催化蛋白酶是一种参与受损蛋白质细胞内降解的多酶蛋白水解复合物。此外，4-羟基-2-壬烯醛修饰的Glu-6-PDH抑制多催化蛋白酶，因此可以防止氧化蛋白质的有效降解。这些发现可能对体内改变的蛋白质和荧光物质的积累具有重要意义，这些过程被认为与年龄和疾病相关的细胞功能损伤有关。
Incubation of glucose-6-phosphate dehydrogenase (Glu-6-PDH) from Leuconostoc mesenteroides with the lipid peroxidation product 4-hydroxy-2-nonenal leads to the formation of cross-linked protein. This is accompanied by the appearance of protein-associated fluorescence with excitation and emission maxima of 340 and 415 nm, respectively, and with the disappearance of histidine and lysine residues. Cross-linked protein is less susceptible than native Glu-6-PDH to proteolysis by the multicatalytic protease, a multienzymic proteolytic complex involved in the intracellular degradation of damaged proteins. In addition, 4-hydroxy-2-nonenal-modified Glu-6-PDH inhibits the multicatalytic protease and can therefore prevent the efficient degradation of oxidized protein. These findings may have important implications for the accumulation of altered protein and fluorescent material in vivo, processes that are believed to be involved in age- and disease-related impairment of cellular function.