Oka K, Wang-Iverson P, Paterniti J R, Brown W V
Department of Medicine, Mount Sinai School of Medicine, New York, New York 10029.
Ann N Y Acad Sci. 1989;556:173-80. doi: 10.1111/j.1749-6632.1989.tb22501.x.
The hydrolysis of triglyceride-rich plasma lipoproteins is initiated by lipoprotein lipase (LPL) located at the luminal surface of endothelial cells. We previously reported that LPL binds to cultured endothelial cells with a Km of 2.7 x 10(-7) M and that this binding is inhibited by heparinase, heparin, or heparan sulfate. We and others recently isolated LPL cDNAs from various animals. The deduced amino acid sequence from cDNA sequence is highly conserved among animal species. The structural analysis revealed two regions rich in basic amino acid residues at the carboxyl-terminal region that may interact with the anionic heparin-like molecules. Amino acid residues 292 to 300 of bovine LPL are extremely similar to the reported heparin binding sites on apolipoproteins B-100 (amino acid residues 3359-3367) and E (amino acid residues 142-150).
富含甘油三酯的血浆脂蛋白的水解由位于内皮细胞腔表面的脂蛋白脂肪酶（LPL）启动。我们之前报道过，LPL以2.7×10⁻⁷M的Km值与培养的内皮细胞结合，且这种结合受到肝素酶、肝素或硫酸乙酰肝素的抑制。我们和其他人最近从各种动物中分离出了LPL cDNA。从cDNA序列推导的氨基酸序列在动物物种间高度保守。结构分析显示，在羧基末端区域有两个富含碱性氨基酸残基的区域，它们可能与阴离子类肝素分子相互作用。牛LPL的氨基酸残基292至300与载脂蛋白B-100（氨基酸残基3359 - 3367）和E（氨基酸残基142 - 150）上报道的肝素结合位点极为相似。
