Nilsson A, Landin B, Schotz M C
J Lipid Res. 1987 May;28(5):510-7.
Chylomicrons labeled with [3H]arachidonic and [14C]linoleic acid were incubated with bovine milk lipoprotein lipase or rat postheparin plasma, containing both lipoprotein lipase and hepatic lipase. During incubation with bovine lipoprotein lipase, [3H]arachidonic acid was released from chylomicron triacylglycerols at a slower rate than [14C]linoleic acid. Only small amounts of [14C]linoleic acid were found as 1,2(2,3)-diacylglycerols, whereas a transient accumulation as [14C]monoacylglycerols was observed. In contrast, significantly more [3H]arachidonic acid was found as 1,2(2,3)-diacylglycerols than as monoacylglycerols at all time intervals investigated. The initial pattern of triacylglycerol hydrolysis by postheparin plasma was similar to that of bovine lipoprotein lipase. However, in contrast to the results obtained with bovine lipoprotein lipase, little [3H]1,2(2,3)-diacylglycerol accumulated. The addition of antiserum to hepatic lipase increased the amount of 3H found in 1,2(2,3)-diacylglycerols and inhibited the formation of free [3H]arachidonic acid. The antiserum also caused a significant inhibition of the hydrolysis of [3H]-but not of [14C]triacylglycerol. With regard to chylomicron phospholipids, the rate of hydrolysis of [14C]linoleoyl phosphatidylcholine with milk lipoprotein lipase was twofold higher than that of the [3H]arachidonyl phosphatidylcholine. However, the hepatic lipase of postheparin plasma had similar activity towards the two phosphatidylcholine species. Postheparin plasma rapidly hydrolyzed chylomicron 3H-labeled and 14C-labeled phosphatidylethanolamine to the same degree, and lipoprotein lipase similarly hydrolyzed 3H-labeled and 14C-labeled phosphatidylethanolamine at approximately equal rates. Antiserum to hepatic lipase inhibited the postheparin plasma hydrolysis of phosphatidylethanolamine and 3H-labeled phosphatidylcholine by about 60%, but the 14C-labeled phosphatidylcholine by only 27%.(ABSTRACT TRUNCATED AT 250 WORDS)
用[3H]花生四烯酸和[14C]亚油酸标记的乳糜微粒与牛脂蛋白脂肪酶或大鼠肝素后血浆一起孵育,大鼠肝素后血浆中同时含有脂蛋白脂肪酶和肝脂酶。在与牛脂蛋白脂肪酶孵育期间,[3H]花生四烯酸从乳糜微粒三酰甘油中释放的速度比[14C]亚油酸慢。仅发现少量[14C]亚油酸以1,2(2,3)-二酰甘油形式存在,而观察到[14C]单酰甘油有短暂积累。相比之下,在所有研究的时间间隔内,发现作为1,2(2,3)-二酰甘油存在的[3H]花生四烯酸比作为单酰甘油存在的显著更多。肝素后血浆对三酰甘油的初始水解模式与牛脂蛋白脂肪酶相似。然而,与用牛脂蛋白脂肪酶获得的结果相反,几乎没有[3H]1,2(2,3)-二酰甘油积累。加入抗肝脂酶血清增加了1,2(2,3)-二酰甘油中3H的含量,并抑制了游离[3H]花生四烯酸的形成。该抗血清还显著抑制了[3H] - 但不抑制[14C]三酰甘油的水解。关于乳糜微粒磷脂,用乳脂蛋白脂肪酶水解[14C]亚油酰磷脂酰胆碱的速度比[3H]花生四烯酰磷脂酰胆碱高两倍。然而,肝素后血浆的肝脂酶对这两种磷脂酰胆碱的活性相似。肝素后血浆以相同程度快速水解乳糜微粒的3H标记和14C标记的磷脂酰乙醇胺,脂蛋白脂肪酶以大致相等的速率类似地水解3H标记和14C标记的磷脂酰乙醇胺。抗肝脂酶血清抑制肝素后血浆对磷脂酰乙醇胺和3H标记的磷脂酰胆碱的水解约60%,但对14C标记的磷脂酰胆碱仅抑制27%。(摘要截短于250字)