Mechanism of iron uptake.

نویسنده

  • S Pollack
چکیده

In the June 1, 1991 issue of Blood, Cochran et all found that the primary pathway for initial uptake of AI-transferrin and Fetransferrin by human fetal red cells (obtained from placentas) was through a high-affinity saturable receptor that did not distinguish between the two metallo-transferrins; that a process that followed initial uptake did distinguish between the two metallo-transferrins; and that as much as 20% of the uptake of metallo-transferrin, at physiologic concentrations of protein, was by way of a low-affinity, nonsaturable receptor. The differential handling of Al-transferrin and Fe-transferrin after they have been endocytosed, as discussed by the Cochran et all may be due to the differential release of Al and Fe from the endocytosed metallo-transferrins or differential transport of the two metals after their release. There is another possibility. Recent experiments have shown that mitochondria have receptors for ironzs3; AI and Fe might compete for binding to these receptors. The postulate of a low-affinity nonsaturable receptor seems at odds with the usual characteristics of a receptor, of which saturability is one. The low-affinity, nonsaturable uptake may perhaps be more easily explained by the receptor-independent endocytosis that is characteristic of fetal erythrocytes.'

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عنوان ژورنال:
  • Blood

دوره 78 8  شماره 

صفحات  -

تاریخ انتشار 1991