Zerounian Nora R., Linder Maria C.
Department of Chemistry and Biochemistry and Institute for Molecular Biology, California State University, 92834-6866, Fullerton, CA, USA
J Nutr Biochem. 2002 Mar;13(3):138-148. doi: 10.1016/s0955-2863(01)00205-4.
Previous studies have implicated copper proteins, including ceruloplasmin, in intestinal iron transport. Polarized Caco2 cells with tight junctions were used to examine the possibilities that (a) ceruloplasmin promotes iron absorption by enhancing release at the basolateral cell surface and (b) copper deficiency reduces intestinal iron transport. Iron uptake and overall transport were followed for 90 min with 1 &mgr;M 59Fe(II) applied to the apical surface of Caco2 cell monolayers. Apotransferrin (38 &mgr;M) was in the basolateral chamber. Induction of iron deficiency with desferrioxamine (100 &mgr;M; 18 h) markedly increased uptake and overall transport of iron. Uptake increased from about 20% to about 65% of dose, and overall 59Fe transport from <1% to 60% of dose. On the basis of actual iron released into the basal chamber (measured with bathophenanthroline), transport increased 8-fold. Desferrioxamine pretreatment reduced cellular Fe by 55%. The addition of freshly isolated, enzymatically active human ceruloplasmin to the basolateral chamber during absorption had no effect on uptake or transport of iron by the cells. Unexpectedly, pretreatment with three different chelators of copper (18 h), which reduced cellular levels about 40%, more than doubled iron uptake and raised overall transport to 20%. This was so, whether or not cells were also made iron deficient with desferrioxamine. Acute addition of 1 &mgr;M Cu(II) to the apical chamber had no significant effect upon iron uptake, retention, or transport in iron deficient or normal cells, in the presence of absence of ascorbate. We conclude that intestinal absorption of Fe(II) is unlikely to depend upon plasma ceruloplasmin, and that cuproproteins involved in this form of iron transport must be binding copper tightly.
先前的研究表明,包括铜蓝蛋白在内的铜蛋白与肠道铁转运有关。利用具有紧密连接的极化Caco2细胞来研究以下可能性:(a)铜蓝蛋白通过增强铁在基底外侧细胞表面的释放来促进铁吸收;(b)铜缺乏会降低肠道铁转运。将1 μM 59Fe(II)施加到Caco2细胞单层的顶端表面,追踪90分钟内的铁摄取和整体转运情况。脱铁转铁蛋白(38 μM)存在于基底外侧腔室中。用去铁胺(100 μM;18小时)诱导缺铁显著增加了铁的摄取和整体转运。摄取量从剂量的约20%增加到约65%,59Fe的整体转运从剂量的<1%增加到60%。根据释放到基底腔室中的实际铁量(用bathophenanthroline测量),转运增加了8倍。去铁胺预处理使细胞内铁减少了55%。在吸收过程中,向基底外侧腔室添加新鲜分离的、具有酶活性的人铜蓝蛋白对细胞的铁摄取或转运没有影响。出乎意料的是,用三种不同的铜螯合剂预处理(18小时)使细胞内铜水平降低约40%,铁摄取增加了一倍多,整体转运提高到20%。无论细胞是否也用去铁胺诱导缺铁,情况都是如此。在存在或不存在抗坏血酸的情况下,向顶端腔室急性添加1 μM Cu(II)对缺铁或正常细胞的铁摄取、保留或转运均无显著影响。我们得出结论,Fe(II)的肠道吸收不太可能依赖于血浆铜蓝蛋白,参与这种铁转运形式的铜蛋白必须紧密结合铜。