Lipoprotein lipase with a defect in lipid interface recognition in a case with type I hyperlipidaemia
Lipoprotein lipase with a defect in lipid interface recognition in a case with type I hyperlipidaemia
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脂蛋白脂肪酶脂质界面识别缺陷一例 I 型高脂血症
DOI：
10.1111/j.1365-2362.1989.tb00254.x
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发表时间：
1989
影响因子：
5.5
通讯作者：
S. Yoshida
中科院分区：
文献类型：
--
作者：
J. Kobayashi;K. Shirai;Y. Saito;S. Yoshida
抽象的。在1例严重高甘油三酯血症患者的肝素后血浆中发现缺陷脂蛋白脂酶(LPL)。患者是一名14岁女孩，血浆甘油三酯(TG)最高水平为3600 mg d-1，一直患有复发性胰腺炎。用肝素-琼脂糖层析法和苯基-琼脂糖层析法从患者的PHP中提纯的LPL能降解三丁酸甘油酯，但不能与Triton X-100和磷脂酰胆碱(PC)乳化，也不能在乳糜粒中乳化，而正常的LPL能降解这些底物。此外，Sepharose4B柱层析显示，与正常LPL不同的是，患者的LPL不与VLDL结合。患者的LPL在载脂蛋白CII存在的情况下，以正常速度将三油酸甘油酯与溶血磷脂乳化。这些发现表明，该患者患有LPL，三丁酸甘油酯的催化部位正常，但脂质界面识别缺陷导致失去识别VLDL或乳糜粒的能力，但不能识别与溶血磷脂乳化的三酸甘油酯。
Abstract. Defective lipoprotein lipase (LpL) was found in the postheparin plasma (PHP) of a patient with severe hypertriglyceridaemia. The patient was a 14‐year‐old girl with a maximum plasma triglyceride (TG) level of 3600 mg d‐1 who had been suffering from recurrent pancreatitis. The patient's LpL purified from the PHP by heparin‐Sepharose and phenyl‐Sepharose chromatographies hydrolysed tributryrin, but not triolein emulsified with Triton X‐100 and phosphatidylcholine (PC), or in chylomicrons, whereas normal LpL hydrolysed these substrates. Moreover, unlike normal LpL, LpL from the patient did not associate with VLDL, as shown by Sepharose 4B column chromatography. The patient's LpL hydrolysed triolein emulsified with lysophospholipid at a normal rate in the presence of apolipoprotein CII. These findings suggest that this patient has LpL with a normal catalytic site for tributyrin but with a defect in lipid interface recognition resulting in loss of ability to recognize VLDL or chylomicrons, but not of triolein emulsified with lysophospholipid.