A family of lipopolysaccharide binding proteins involved in responses to gram-negative sepsis.
A family of lipopolysaccharide binding proteins involved in responses to gram-negative sepsis.
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DOI：
10.1016/s0021-9258(18)68262-6
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发表时间：
1988-09
期刊：
影响因子：
--
通讯作者：
P. Tobias;J. Mathison;R. Ulevitch
中科院分区：
文献类型：
--
作者：
P. Tobias;J. Mathison;R. Ulevitch
革兰氏阴性杆菌的脂多糖在许多宿主体内启动了潜在的致死过程。最近发表的氨基酸序列数据表明，有一类脂多糖结合蛋白家族可能参与宿主对革兰氏阴性菌血症的反应。首先确定的两个成员是在人类、小鼠、兔子和大鼠的急性时相反应后存在于血清中的脂多糖结合蛋白和存在于人和兔中性粒细胞初级颗粒中的杀菌/通透性增加蛋白。内毒素结合蛋白和杀菌/通透性增加蛋白具有与内毒素结合的能力，具有同源的NH2末端氨基酸序列，并且具有免疫交叉反应。然而，这两个分子对内毒素和革兰氏阴性菌的作用不同，它们的生物合成部位和体内定位不同。
The lipopolysaccharides (LPS) of Gram-negative bacteria initiate potentially fatal processes in many host organisms. Recently published amino acid sequence data suggest that there is a family of LPS binding proteins that may participate in the host response to Gram-negative bacteremia. The first two members of the family to be identified are an LPS binding protein present in serum after an acute phase response in humans, mice, rabbits, and rats and a bactericidal/permeability increasing protein present in the primary granules of human and rabbit neutrophils. LPS binding protein and bactericidal/permeability increasing protein share an ability to bind to LPS, have homologous NH2-terminal amino acid sequences, and are immunologically cross-reactive. Nevertheless, these two molecules differ in their effects on LPS and Gram-negative bacteria, in their sites of biosynthesis, and localization in vivo.