Porcine pancreatic lipase related protein 2 has high triglyceride lipase activity in the absence of colipase.
Porcine pancreatic lipase related protein 2 has high triglyceride lipase activity in the absence of colipase.
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猪胰脂肪酶相关蛋白2在辅脂肪酶不存在的情况下具有高甘油三酯脂肪酶活性。
DOI：
10.1016/j.bbalip.2013.06.002
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发表时间：
2013
期刊：
影响因子：
--
通讯作者：
Lowe,MarkE
中科院分区：
文献类型：
--
作者：
Xiao,Xunjun;Ross,LeahE;Sevilla,WednesdayA;Wang,Yan;Lowe,MarkE
有效的膳食脂肪消化对于新生儿来说是至关重要的，因为他们每体重摄入的膳食脂肪比生命中任何时候都要多。在许多哺乳动物新生儿中，胰腺脂肪酶相关蛋白2(PLRP2)是主要的十二指肠脂肪酶。猪可能是个例外，因为PLRP2在肠道中有表达，但在胰腺中没有。由于组织特异性表达的差异，我们假设猪PLRP2的动力学特性将不同于其他哺乳动物。为了鉴定重组猪PLRP2的性质，在HEK293T细胞中表达了重组猪PLRP2，并进行了纯化。猪PLRP2对三丁酸甘油酯、三辛酸甘油酯和三油酸甘油酯有一定的抑制作用。胆盐和磷脂酶对胰甘油三酯脂肪酶(PTL)活性无抑制作用，但对PLRP2活性有最小的刺激作用。与其他物种的PLRP2相似，猪的PLRP2具有抗半乳糖和磷脂的活性。重要的是，猪PLRP2能降解多种饮食底物，包括巴氏杀菌的母乳和婴儿配方奶粉，其活性与PTL相当。综上所述，猪PLRP2具有广泛的底物特异性，即使在没有脂肪酶的情况下也具有较高的甘油三酯脂肪酶活性。这些数据表明，猪PLRP2可能是一种适合用于胰腺酶替代治疗的重组制剂中的脂肪酶。
Efficient dietary fat digestion is essential for newborns who consume more dietary fat per body weight than at any other time of life. In many mammalian newborns, pancreatic lipase related protein 2 (PLRP2) is the predominant duodenal lipase. Pigs may be an exception since PLRP2 expression has been documented in the intestine but not in the pancreas. Because of the differences in tissue-specific expression, we hypothesized that the kinetic properties of porcine PLRP2 would differ from those of other mammals. To characterize its properties, recombinant porcine PLRP2 was expressed in HEK293T cells and purified to homogeneity. Porcine PLRP2 had activity against tributyrin, trioctanoin and triolein. The activity was not inhibited by bile salts and colipase, which is required for the activity of pancreatic triglyceride lipase (PTL), minimally stimulated PLRP2 activity. Similar to PLRP2 from other species, PLRP2 from pigs had activity against galactolipids and phospholipids. Importantly, porcine PLRP2 hydrolyzed a variety of dietary substrates including pasteurized human mother's milk and infant formula and its activity was comparable to that of PTL. In conclusion, porcine PLRP2 has broad substrate specificity and has high triglyceride lipase activity even in the absence of colipase. The data suggest that porcine PLRP2 would be a suitable lipase for inclusion in recombinant preparations for pancreatic enzyme replacement therapy.