Bijvoet S M, Bruin T, Tuzgöl S, Bakker H D, Hayden M R, Kastelein J J
Centre for Haemostasis, Thrombosis, Atherosclerosis and Inflammation Research, Academic Medical Centre, University of Amsterdam, The Netherlands.
Hum Genet. 1994 Mar;93(3):339-43. doi: 10.1007/BF00212035.
The enzyme lipoprotein lipase (LPL) plays a crucial role in triglyceride metabolism through catalysis of triglyceride-rich chylomicrons and very low density lipoproteins. Primary LPL deficiency manifests with chylomicronaemia and is caused by mutations in the LPL gene. In this paper we report a novel molecular defect (G670-->A) in exon 4 of the LPL gene, resulting in a substitution of serine for glycine at position 139 in the mature protein. We identified homozygosity for this mutation in a boy of Spanish descent. In vitro mutagenesis provided formal proof that this missense mutation completely abolishes LPL function and therefore is the cause of LPL deficiency.
脂蛋白脂肪酶（LPL）通过催化富含甘油三酯的乳糜微粒和极低密度脂蛋白，在甘油三酯代谢中发挥关键作用。原发性LPL缺乏症表现为乳糜微粒血症，由LPL基因突变引起。在本文中，我们报告了LPL基因第4外显子中的一种新型分子缺陷（G670→A），导致成熟蛋白第139位的丝氨酸替代了甘氨酸。我们在一名西班牙裔男孩中鉴定出该突变的纯合性。体外诱变提供了正式证据，证明这种错义突变完全消除了LPL功能，因此是LPL缺乏症的病因。
