STRUCTURE AND FUNCTION OF LIPOPOLYSACCHARIDE BINDING-PROTEIN
STRUCTURE AND FUNCTION OF LIPOPOLYSACCHARIDE BINDING-PROTEIN
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DOI：
10.1126/science.2402637
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发表时间：
1990-09-21
期刊：
影响因子：
56.9
通讯作者：
ULEVITCH, RJ
中科院分区：
文献类型：
--
作者：
SCHUMANN, RR;LEONG, SR;ULEVITCH, RJ
通过对细菌脂多糖（lps）的脂多糖结合蛋白（lipopolaccharide binding protein， LBP）的克隆互补DNA测序，推测了其一级结构。LBP与另一种在粒细胞中发现的LPS结合蛋白、杀菌/通透性增加蛋白以及血浆中的胆固醇酯转运蛋白具有相同的序列。LBP可能在生理条件下通过与LPS形成高亲和力复合物，结合单核细胞和巨噬细胞分泌肿瘤坏死因子，从而控制对LPS的反应。鉴定脂多糖诱导单核细胞刺激的这一途径可能有助于开发革兰氏阴性败血症或内毒素血症相关疾病的治疗方法。
The primary structure of lipopolysaccharide binding protein (LBP), a trace plasma protein that binds to the lipid A moiety of bacterial lipopolysaccharides (LPSs), was deduced by sequencing cloned complementary DNA. LBP shares sequence identity with another LPS binding protein found in granulocytes, bactericidal/permeability-increasing protein, and with cholesterol ester transport protein of the plasma. LBP may control the response to LPS under physiologic conditions by forming high-affinity complexes with LPS that bind to monocytes and macrophages, which then secrete tumor necrosis factor. The identification of this pathway for LPS-induced monocyte stimulation may aid in the development of treatments for diseases in which Gram-negative sepsis or endotoxemia are involved.