Transferrin
Transferrin - Related Videos
01:28
The Early Endosome: Endocytosis of Transferrin
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2023
Essential proteins such as insulin or low-density lipoprotein (LDL) and micronutrients such as iron enter a eukaryotic cell through receptor-mediated endocytosis. Subsequently, the early endosomes fuse with the vesicles containing such receptor-ligand complexes and play a vital role in sorting the incoming ligands and receptors. While the ligands are either degraded inside the vesicle or released into the cytosol, their receptors are returned to the plasma membrane for further rounds of...
08:45
Quantitating Iron Transport Across the Mouse Placenta In Vivo Using Nonradioactive Iron Isotopes
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Cited by 3 •
2022
This article demonstrates how to prepare and administer transferrin-bound nonradioactive isotopic iron for studies of iron transport in mouse pregnancy. The approach for quantifying isotopic iron in fetoplacental compartments is also described.
10:56
Endothelial Cell Transcytosis Assay as an In Vitro Model to Evaluate Inner Blood-Retinal Barrier Permeability
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Cited by 6 •
2022
This protocol illustrates an in vitro endothelial cell transcytosis assay as a model to evaluate inner blood-retinal barrier permeability by measuring the ability of human retinal microvascular endothelial cells to transport horseradish peroxidase across cells in caveolae-mediated transcellular transport processes.
11:56
Differential Labeling of Cell-surface and Internalized Proteins after Antibody Feeding of Live Cultured Neurons
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Cited by 23 •
2014
We describe a method to label protein on the surface of living neurons using a specific polyclonal antibody to extracellular epitopes. Protein bound by the antibody on the cell surface and subsequently internalized via endocytosis can be distinguished from protein remaining on, or trafficked to, the surface during the incubation.
11:56
A Rapid and Specific Microplate Assay for the Determination of Intra- and Extracellular Ascorbate in Cultured Cells
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Cited by 4 •
2014
Ascorbate plays numerous important roles in cellular metabolism, many of which have only come to light in recent years. Here we describe a medium-throughput, specific and inexpensive microplate assay for the determination of both intra- and extracellular ascorbate in cell culture.
FAQs
Endosomal acidification is the key release condition. After transferrin has entered a cell with its receptor, the lower-pH environment promotes ferric iron dissociation from the protein. The receptor and transferrin can then return to the cell surface, separating iron release from the outward recycling step. This sequence links intracellular trafficking to iron availability.
The transferrin receptor determines how cells access circulating iron. Binding at the cell surface initiates receptor-mediated endocytosis, placing the transferrin-receptor complex inside an endosome rather than allowing nonspecific entry. Because the complex subsequently returns to the surface, receptor engagement supports continued uptake and release through an organized cellular pathway.
High-affinity ferric-iron binding gives transferrin a dual role in iron balance. It keeps iron available for delivery through a controlled carrier while limiting the amount of unbound iron in plasma, which is associated with toxicity. This balance makes transferrin relevant to normal cellular iron supply and to studies of disrupted iron homeostasis.
A study can follow the pathway from transferrin-receptor association at the cell surface through receptor-mediated endocytosis, endosomal iron release, and return of the receptor and protein to the surface. Examining these linked stages helps characterize cellular iron uptake and provides context for interpreting transferrin receptor behavior as a marker of cellular iron metabolism.
Transferrin is relevant because erythropoiesis is one of the biological processes connected to iron availability. Researchers can examine transferrin binding, receptor uptake, and intracellular iron release when investigating how cells obtain iron during red blood cell production. This approach connects a defined transport pathway with broader questions about iron supply and erythropoiesis.
These conditions provide contrasting contexts for examining iron handling. Comparing transferrin-associated transport and receptor-pathway behavior can help researchers investigate whether iron availability or cellular processing is disrupted. The protein therefore offers a common framework for studying insufficient iron supply, excessive iron burden, and their relationship to cellular iron homeostasis.
Because the pathway naturally links a cell-surface receptor to receptor-mediated endocytosis, it offers a route for studying how targeted delivery approaches may use receptor-associated uptake. In biomedical research, transferrin receptor interactions are therefore relevant to delivery design, while the normal iron-transport pathway provides biological context for evaluating cellular entry.