Baveye S, Elass E, Mazurier J, Spik G, Legrand D
Unité Mixte de Recherche du Centre National de la Recherche Scientifique n 111 et Laboratoire de Chimie Biologique, Université des Sciences et Technologies de Lille, Villeneuve d'Ascq, France.
Clin Chem Lab Med. 1999 Mar;37(3):281-6. doi: 10.1515/CCLM.1999.049.
Lactoferrin is an iron-binding glycoprotein found in exocrine secretions of mammals and released from neutrophilic granules during inflammation. This review describes the biological roles of lactoferrin in host defence. Secreted lactoferrin exerts antimicrobial action either by chelation of iron or by destabilization of bacterial membranes. Furthermore, lactoferrin modulates the inflammatory process, mainly by preventing the release of cytokines from monocytes and by regulating the proliferation and differentiation of immune cells. Some of these activities are related to the ability of lactoferrin to bind lipopolysaccharides (LPS) with high affinity. Indeed, recent in vitro studies indicate that lactoferrin is able to compete with the LPS-binding protein for LPS binding and therefore to prevent the transfer of LPS to CD14 present at the surface of monocytes. Moreover, the prophylactic properties of lactoferrin against septicemia in vivo have been demonstrated. Taken as a whole, these observations strongly suggest that lactoferrin is one of the key molecules which modulate the inflammatory response.
乳铁蛋白是一种存在于哺乳动物外分泌液中的铁结合糖蛋白,在炎症过程中从中性粒细胞颗粒中释放出来。本综述描述了乳铁蛋白在宿主防御中的生物学作用。分泌的乳铁蛋白通过螯合铁或破坏细菌膜的稳定性发挥抗菌作用。此外,乳铁蛋白主要通过阻止单核细胞释放细胞因子以及调节免疫细胞的增殖和分化来调节炎症过程。这些活性中的一些与乳铁蛋白以高亲和力结合脂多糖(LPS)的能力有关。事实上,最近的体外研究表明,乳铁蛋白能够与LPS结合蛋白竞争LPS结合,从而防止LPS转移到单核细胞表面存在的CD14上。此外,乳铁蛋白在体内对败血症的预防特性也已得到证实。总体而言,这些观察结果强烈表明乳铁蛋白是调节炎症反应的关键分子之一。