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首页> 外文期刊>Journal of Leukocyte Biology: An Official Publication of the Reticuloendothelial Society >Structural requirements for intracellular processing and sorting of bactericidal/permeability-increasing protein (BPI): comparison with lipopolysaccharide-binding protein
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Structural requirements for intracellular processing and sorting of bactericidal/permeability-increasing protein (BPI): comparison with lipopolysaccharide-binding protein

机译：细胞内加工和分选杀菌/通透性增强蛋白（BPI）的结构要求：与脂多糖结合蛋白的比较

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The bactericidal/permeability-increasing protein (BPI), which is stored in the azurophil granules of neutrophils, and the circulating lipopolysaccharide-binding protein (LBP) share the same structure. Both bind lipopolysaccharide of gram-negative bacteria through their amino-terminal domains. The carboxy-terminal domain of BPI promotes bacterial attachment to phagocytes, whereas the corresponding domain of LBP delivers lipopolysaccharide to monocytes/macrophages. Our aim was to investigate the role of the amino- and carboxy-terminal domains of BPI and LBP for sorting and storage in myeloid cells after transfection of cDNA to two rodent hematopoietic cell lines. Full-length BPI and LBP were both targeted for storage in these cells. Deletion of the carboxy-terminal half of BPI resulted in storage followed by degradation while the reciprocal deletion of the amino-terminal half led to retention in the endoplasmic reticulum for proteasomal degradation. Chimeras between halves of BPI and LBP were also targeted for storage, but those containing carboxy-terminal BPI had the highest stability, again indicating a role for the carboxy-terminal domain of BPI in protection against degradation. Therefore, we propose a critical stability function for the hydrophobic carboxy-terminal domain of BPI during intracellular sorting for storage while the amino-terminal domain may confer targeting for storage.
机译：储存在嗜中性粒细胞的天青石颗粒中的杀菌/通透性增强蛋白（BPI）与循环脂多糖结合蛋白（LBP）具有相同的结构。两者都通过其氨基末端结构域结合革兰氏阴性细菌的脂多糖。 BPI的羧基末端结构域促进细菌附着于吞噬细胞，而LBP的相应结构域将脂多糖递送至单核细胞/巨噬细胞。我们的目的是研究cDNA转染到两种啮齿动物造血细胞系后，BPI和LBP的氨基末端和羧基末端结构域在髓样细胞中的分类和存储中的作用。全长BPI和LBP均针对在这些细胞中的储存。 BPI羧基末端一半的缺失导致储存，然后降解，而氨基末端一半的相互缺失导致内质网保留下来用于蛋白酶体降解。 BPI和LBP一半之间的嵌合体也可以作为储存对象，但含有羧基末端BPI的嵌合体具有最高的稳定性，再次表明BPI羧基末端结构域在防止降解中起作用。因此，我们提出了细胞内分选过程中BPI的疏水性羧基末端结构域的关键稳定性函数，而氨基末端结构域可能赋予了存储目标。

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