van Snick J L, Markowetz B, Masson P L
J Exp Med. 1977 Sep 1;146(3):817-27. doi: 10.1084/jem.146.3.817.
Human lactoferrin (Lf) labeled with 125I and/or 59Fe was found to be ingested in vitro by mouse peritoneal macrophages (MPM). The uptake measured after 15 h incubation reached a saturation point at a concentration of 200 microgram/ml in the culture medium, whatever was the iron content of Lf. In such conditions, the uptake of transferrin (Tf) used as a control was 10 times lower. At a concentration of 80 microgram/ml in the medium, one cell picked up about 0.7 X 10(6) molecules of Lf per hour, and 0.13 X 10(6) molecules of Tf per hour. Iron-saturated Lf disappeared from MPM with a half life of 14.5 h, whereas the halflife of iron-free Lf was 4.2 h. Concomitant with the intracellular digestion of Lf, the iron was transmitted to ferritin. These data provide additional support for the hypothesis that Lf plays a key role in iron turnover, especially at the level of the reticuloendothelial system where iron is recovered from the catabolism of erythrocytes.
用125I和/或59Fe标记的人乳铁蛋白(Lf)在体外被小鼠腹腔巨噬细胞(MPM)摄取。无论Lf的铁含量如何,在培养基中孵育15小时后测得的摄取量在200微克/毫升的浓度下达到饱和点。在这种情况下,用作对照的转铁蛋白(Tf)的摄取量低10倍。在培养基中浓度为80微克/毫升时,一个细胞每小时摄取约0.7×10⁶个Lf分子,每小时摄取0.13×10⁶个Tf分子。铁饱和的Lf以14.5小时的半衰期从MPM中消失,而无铁Lf的半衰期为4.2小时。伴随着Lf的细胞内消化,铁被传递给铁蛋白。这些数据为Lf在铁周转中起关键作用的假说提供了额外支持,特别是在从红细胞分解代谢中回收铁的网状内皮系统水平。