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Fe(III) delivery from blood plasma to cells via the transferrin (Tf) cycle is studied intensively due to its crucial role in Fe homeostasis. Tf-cycle disruptions are linked to anemia, infections, immunodeficiency and neurodegeneration. Bio-layer interferometry (BLI) enabled direct kinetic and thermodynamic measurements for all Tf-cycle steps in a single in-vitro experiment using Tf within blood serum or released into the medium by cultured liver cells. In these media, known Tf cycle features were reproduced as well as unprecedented insights into conditions of rapid endosomal (pH 5.6) Fe(III) release from the Tf-Tf receptor 1 (TfR1) adduct. This release occurred via synergistic citrate and ascorbate effects, which pointed to respective roles as the likely elusive Fe chelator and reductant within the Tf cycle. These results explain enhanced cellular Fe uptake by ascorbate, the clinical efficacy of anemia treatment with Fe citrate and ascorbate, and dietary effects associated with loss of Fe homeostasis including the large health burden of infections and neurodegeneration.
This article was published in the following journal.
Name: ACS chemical biology
Most cells in the body acquire iron via receptor-mediated endocytosis of transferrin, the circulating iron transport protein. When cellular iron levels are sufficient, the uptake of transferrin decrea...
This review discusses the chemical mechanisms of ascorbate-dependent reduction and solubilization of ferritin's ferric iron core and subsequent release of ferrous iron. The process is accelerated by l...
Which blood-based indicator best reflects the iron status in pregnant women is unclear. Better assessments of iron status in today's multiethnic populations are needed to optimize treatment and clinic...
Iron metabolism is an essential process that when dysregulated causes disease. Mammalian serum transferrin (TF) plays a primary role in delivering iron to cells. To improve our understanding of the co...
The exact route of iron through the kidney and its regulation during iron overload are not completely elucidated. Under physiologic conditions, non-transferrin and transferrin bound iron passes the gl...
The main objective of the study is to compare the impact of oral ferric citrate compared to standard of care oral ferrous sulfate on serum iron, percent transferrin saturation, ferritin, h...
This study aims to investigate a possible effect of iron status on temporary build-up of non-transferrin bound iron (NTBI) in healthy volunteers upon iron supplementation.
This study aims to evaluate a prototype device detecting zinc protoporphyrin-IX fluorescence non-invasively from the intact oral mucosa. Zinc protoporphyrin-IX is an established indicator ...
This is a randomized non inferiority trial to evaluate the response to iron therapy in the standard daily vs. intermittent (three-four times a week on nonconsecutive days) groups by using ...
Several iron compounds are used for fortification, including ferrous sulphate and NaFeEDTA. The absorption profile of these may differ because of differences in their dissolution in the ga...
Membrane glycoproteins found in high concentrations on iron-utilizing cells. They specifically bind iron-bearing transferrin, are endocytosed with its ligand and then returned to the cell surface where transferrin without its iron is released.
A class of carrier proteins that bind to TRANSFERRIN. Many strains of pathogenic bacteria utilize transferrin-binding proteins to acquire their supply of iron from serum.
A complex of proteins that forms a receptor for TRANSFERRIN in BACTERIA. Many pathogenic bacteria utilize the transferrin-binding complex to acquire their supply of iron from serum.
Anemia characterized by decreased or absent iron stores, low serum iron concentration, low transferrin saturation, and low hemoglobin concentration or hematocrit value. The erythrocytes are hypochromic and microcytic and the iron binding capacity is increased.
Enzyme that catalyzes the first step of the tricarboxylic acid cycle (CITRIC ACID CYCLE). It catalyzes the reaction of oxaloacetate and acetyl CoA to form citrate and coenzyme A. This enzyme was formerly listed as EC 220.127.116.11.
Blood is a specialized bodily fluid that delivers necessary substances to the body's cells (in animals) – such as nutrients and oxygen – and transports waste products away from those same cells. In vertebrates, it is composed of blo...