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小鼠腹腔巨噬细胞对人乳铁蛋白的摄取与消化及其铁向铁蛋白的转移。

The ingestion and digestion of human lactoferrin by mouse peritoneal macrophages and the transfer of its iron into ferritin.

作者信息

van Snick J L, Markowetz B, Masson P L

出版信息

J Exp Med. 1977 Sep 1;146(3):817-27. doi: 10.1084/jem.146.3.817.

Abstract

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.

摘要

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。

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