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transferriniron

Transferriniron is the complex of iron ions bound to transferrin, a circulating plasma glycoprotein whose main function is to transport iron from sites of absorption and storage to cells that require it. Transferrin has two high-affinity iron-binding sites; each binds one Fe3+ ion in a coordinated fashion and typically requires a carbonate anion as a synergist. In its iron-loaded form, holo-transferrin circulates and delivers iron to most tissues via the transferrin receptor (TfR1) on the cell surface. The receptor binds holo-transferrin with high affinity at neutral pH and mediates receptor-mediated endocytosis. In the acidic endosome, iron is released, reduced from Fe3+ to Fe2+ by ferrireductases such as the STEAP family, and transported into the cytosol primarily by DMT1. The apotransferrin and TfR1 recycle to the cell surface, where apo-transferrin is released at neutral pH and can bind iron again.

Serum composition is described by transferrin concentration and transferrin saturation, the fraction of iron-binding sites occupied

by
iron;
total
iron-binding
capacity
(TIBC)
reflects
transferrin
levels.
Alterations
in
transferriniron
homeostasis
occur
in
iron
deficiency
(low
saturation,
high
TIBC)
and
iron
overload
(high
saturation).
Disease
states
such
as
hereditary
hemochromatosis
and
chronic
inflammation
can
influence
transferrin
levels
and
receptor
expression,
affecting
iron
delivery
to
cells
and
iron-related
pathology.