Dentener M A, Francot G J, Buurman W A
Department of Surgery, University of Limburg, Maastricht, Netherlands.
J Infect Dis. 1996 Jan;173(1):252-5. doi: 10.1093/infdis/173.1.252.
Bactericidal/permeability-increasing protein (BPI), a cationic protein present in the azurophilic granule and on the surface of polymorphonuclear leukocytes, specifically interacts with lipopolysaccharide (LPS). This study demonstrates for the first time, using flow cytometry with specific anti-BPI monoclonal antibody (MAb), that human peripheral blood monocytes express BPI on their cell surface. The monocyte cell surface BPI was shown to bind to LPS, because binding of anti-BPI MAb 4E3 (which is known not to react with BPI to which LPS is bound) to cell surface BPI was strongly reduced after preincubation of cells with LPS. However, cell surface BPI did not quantitatively contribute to the interaction of LPS with the monocyte cell membrane, since preincubation of cells with 4E3 did not block binding of LPS-fluorescein isothiocyanate to monocytes. The origin of the monocyte cell surface BPI remains to be further elucidated.
杀菌/通透性增强蛋白（BPI）是一种存在于嗜天青颗粒和多形核白细胞表面的阳离子蛋白，它能特异性地与脂多糖（LPS）相互作用。本研究首次使用特异性抗BPI单克隆抗体（MAb）的流式细胞术证明，人外周血单核细胞在其细胞表面表达BPI。单核细胞表面的BPI被证明能与LPS结合，因为在用LPS预孵育细胞后，抗BPI单克隆抗体4E3（已知不与结合了LPS的BPI反应）与细胞表面BPI的结合力大大降低。然而，细胞表面的BPI在数量上对LPS与单核细胞膜的相互作用没有贡献，因为用4E3预孵育细胞并没有阻止异硫氰酸荧光素标记的LPS与单核细胞的结合。单核细胞表面BPI的来源仍有待进一步阐明。
