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...
11:56
Differential Labeling of Cell-surface and Internalized Proteins after Antibody Feeding of Live Cultured Neurons
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Cited by 24 •
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.
09:46
Simultaneous pH Measurement in Endocytic and Cytosolic Compartments in Living Cells using Confocal Microscopy
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Cited by 20 •
2014
Several methods are available for measuring intracellular pH but very few of these allow simultaneous measurement of cytoplasmic and organellar pH. Here, we describe in detail a rapid and accurate methodology to simultaneously measure cytoplasmic and vesicular pH by ratiometric imaging of living cells.
09:51
Standards for Quantitative Metalloproteomic Analysis Using Size Exclusion ICP-MS
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Cited by 34 •
2016
Size exclusion chromatography hyphenated with inductively coupled plasma - mass spectrometry (ICP-MS) is a powerful tool to measure changes in the abundance of metalloproteins directly from biological samples. Here we describe a set of metalloprotein standards used to estimate molecular mass and the amount of metal associated with unknown proteins.
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.