Neutrophil gelatinase-associated lipocalin, a siderophore-binding eukaryotic protein
Neutrophil gelatinase-associated lipocalin, a siderophore-binding eukaryotic protein
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DOI：
10.1007/s10534-005-3251-7
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发表时间：
2006-04-01
期刊：
影响因子：
3.5
通讯作者：
Cowland, Jack B.
中科院分区：
文献类型：
--
作者：
Borregaard, Niels;Cowland, Jack B.
NGAL（中性粒细胞明胶酶相关脂质运载蛋白），也称为lcn2或铁黄素，组成型表达于髓细胞中，并储存在中性粒细胞的特定颗粒中。它在炎症期间在各种上皮细胞中高度诱导。在大肠杆菌中表达的NGAL的晶体结构的分析表明，NGAL具有结合儿茶酚酸盐型铁载体的能力，并以这种方式防止细菌获得铁载体结合的铁。NGAL（或命名为24 p3的高度同源的鼠直向同源物）敲除小鼠在腹膜内注射后对大肠杆菌的防御中具有严重缺陷。这种缺陷可以在野生型小鼠中通过提供不能被NGAL螯合的铁载体铁来模拟，证明NGAL作为铁载体结合蛋白在先天免疫中的特定作用。Megalin是一种清道夫受体，作为NGAL的受体发挥作用并介导摄取到内体中，但可能存在其他NGAL受体。
NGAL (neutrophil gelatinase-associated lipocalin) also known as lcn2 or siderochalin is constitutively expressed in myelocytes and stored in specific granules of neutrophils. It is highly induced in a variety of epithelial cells during inflammation. Analysis of the crystal structure of NGAL expressed in E.coli showed that NGAL has the ability to bind catecholate type siderophores and in this way prevent bacteria from acquisition of siderophore-bound iron. NGAL (or 24p3 as the highly homologous murine orthologue is named) knock out mice have a profound defect in defense against E.coli after intraperitoneal injection. This defect can be mimicked in wild-type mice by providing siderophore iron, which cannot be sequestered by NGAL, testifying to the specific role of NGAL as a siderophore binding protein in innate immunity. Megalin, a scavenger receptor functions as a receptor for NGAL and mediates uptake into endosomes, but other NGAL receptors are likely to exist.