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首页> 外文期刊>Biochemistry >Activation of Phospholipase C epsilon by Free Fatty Acids and Cross Talk with Phospholipase D and Phospholipase A_2
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Activation of Phospholipase C epsilon by Free Fatty Acids and Cross Talk with Phospholipase D and Phospholipase A_2

机译:游离脂肪酸活化磷脂酶Cε以及与磷脂酶D和磷脂酶A_2的串扰

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This paper uses phospholipase C epsilon as a model to demonstrate that lipids can act as ligands to bind to specific motifs and regulate protein activity via allosteric effects.Phospholipids such as phosphatidic acid and free fatty acids such as arachidonate are potent activators of PLC epsilon,increasing the rate of PI hydrolysis by 8-fold and 50-fold,respectively.The mechanism appears to be a reduction of K_m,as the substrate dependence curve is shifted to the left and K_m is reduced 10-fold.The regulation of PLC epsilon by lipids appears to be physiologic,as reconstitution or cotransfection of either cPLA_2 or PLD with PLC epsilon leads to activation of phosphodiesterase activity.Additionally,TSA-201 cells transfected with PLC epsilon and fed arachidonic acid complexed with BSA had increased (4-5-fold) hydrolysis of polyphosphoinositides.This study demonstrates the ability of lipids to act as potent and direct mediators of protein function and identifies cross talk between different classes of phospholipase (PLD and PLA_2 with PLC) mediated via lipid products.
机译:本文以磷脂酶Cε为模型,证明脂质可以通过变构作用与特定基序结合并调节蛋白质活性。磷脂如磷脂酸和游离脂肪酸如花生四烯酸是PLCε的有效激活剂,其增加PI水解速率分别是8倍和50倍。机理似乎是K_m的降低,因为底物依赖性曲线向左移动,K_m降低了10倍。脂质似乎是生理性的,因为cPLA_2或PLD与PLC epsilon的重组或共转染会导致磷酸二酯酶活性的激活。此外,用PLC epsilon转染并饲喂花生四烯酸与BSA复合的TSA-201细胞增加了(4-5倍)这项研究证明了脂质具有作为蛋白质功能的有效和直接介体的能力,并可以识别不同蛋白质之间的串扰类脂酶介导的磷脂酶类别(PLD和带有PLC的PLA_2)。

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