Binding and ingestion of human lactoferrin by mouse alveolar macrophages.

Abstract
59Fe-labeled human lactoferrin was preferentially ingested by mouse alveolar macrophages (MAM) when compared to 59Fe-labeled human transferrin. The cells bound and ingested 125I-labeled Fe-saturated and Fe-free lactoferrin. The latter was digested faster (t 1/2 [half-life] = 5.8 h) than the Fe-saturated compound (t 1/2 = 10.5 h). The constant elimination of the Fe-lactoferrin complex by alveolar macrophages could enhance the bacteriostatic effect of lactoferrin in the pulmonary secretions.