Department of Cell Biology and Neurosciences, Istituto Superiore di Sanità, Viale Regina Elena 299, Rome, Italy.
Biometals. 2010 Jun;23(3):387-97. doi: 10.1007/s10534-010-9307-3. Epub 2010 Feb 27.
Lactoferrin (Lf) is a mammalian exclusive protein widely distributed in milk and exocrine secretions exhibiting multifunctional properties. Many of the proven or proposed functions of Lf, apart from its iron binding activity, depend on its capacity to bind to other macromolecules. Lf can bind and sequester lipopolysaccharide (LPS), thus preventing pro-inflammatory pathway activation, sepsis and tissue damage. However, the interplay between Lf and LPS is complex, and may result in different outcomes, including both suppression of the inflammatory response and immune activation. These findings are critically relevant in the development of Lf-based therapeutic interventions in humans. Understanding the molecular basis and functional consequences of Lf-LPS interaction will provide insights for determining its role in health and disease.
乳铁蛋白（Lf）是一种哺乳动物特有的蛋白，广泛分布于乳和外分泌液中，具有多种功能。Lf 的许多已证实或提出的功能，除了其铁结合活性外，还依赖于其与其他大分子结合的能力。Lf 可以与脂多糖（LPS）结合并将其隔离，从而防止促炎途径的激活、败血症和组织损伤。然而，Lf 和 LPS 之间的相互作用很复杂，可能导致不同的结果，包括抑制炎症反应和免疫激活。这些发现对于开发基于 Lf 的人类治疗干预措施至关重要。了解 Lf-LPS 相互作用的分子基础和功能后果将为确定其在健康和疾病中的作用提供依据。
