Binding and ingestion of human lactoferrin by mouse alveolar macrophages.
59Fe-labelled human lactoferrin was found to be preferentially ingested by mouse alveolar macrophages (MAM) when compared to 59Fe-labelled human transferrin. The cells bound and ingested 125I-labelled iron-saturated and iron-free lactoferrin. The latter was digested faster (t1/2 = 5.8 hours), however, than the iron-saturated compound (t1/2 = 10.5 hours). The constant elimination of the Fe-lactoferrin complex by alveolar macrophages could enhance the bacteriostatic effect of lactoferrin in the pulmonary secretions.
D000818:Animals; D005260:Female; D006207:Half-Life; D066298:In Vitro Techniques; D007501:Iron / Q000378:metabolism; D007781:Lactoferrin / Q000378:metabolism*; D007782:Lactoglobulins / Q000378:metabolism*; D008264:Macrophages / Q000378:metabolism*; D051379:Mice; D011485:Protein Binding; D011650:Pulmonary Alveoli / Q000166:cytology*; D014168:Transferrin / Q000378:metabolism
D007782:Lactoglobulins; D014168:Transferrin; D007501:Iron; D007781:Lactoferrin