How is ferritin translation regulated?

How is ferritin translation regulated?

Translational regulation of ferritin by oxidative stress. Ferritin is subject to translational control by the IRE binding proteins IRP-1 and IRP-2. When activated, these proteins can bind to the IRE in the 5′ UTR of ferritin H or L mRNA and inhibit translation of the mRNA.

How is translation regulated?

Translation can be regulated globally (for every mRNA in the cell) through changes in the availability or activity of the “helper” proteins. For example, in order for translation to begin, a protein called eukaryotic initiation factor-2 (eIF-2) must bind to a part of the ribosome called the small subunit.

How does iron regulate transferrin receptor gene expression?

For most non-erythroid cells, iron can regulate the TfR expression in a reciprocal manner through modulating the stability of the receptor mRNA whereas in hemoglobin-synthesizing cells, the TfR expression is independent of the cellular iron loading.

What drives iron Ferroportin?

Ferroportin is the only known iron exporter. After dietary iron is absorbed into the cells of the small intestine, ferroportin allows that iron to be transported out of those cells and into the bloodstream….

Ferroportin
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n a n/a

Where does translational regulation take place?

initiation of translation
In most of these cases regulation takes place at the level of initiation of translation, which is often attributable to structural peculiarities of the mRNA in question, especially of the 5′-untranslated region or leader. This review summarizes the mechanisms which lie at the root of translational control.

Where does translational regulation occur?

ribosomes
Initiation of translation is regulated by the accessibility of ribosomes to the Shine-Dalgarno sequence. This stretch of four to nine purine residues are located upstream the initiation codon and hybridize to a pyrimidine-rich sequence near the 3′ end of the 16S RNA within the 30S bacterial ribosomal subunit.

What is the difference between ferritin and transferrin?

Ferritin isn’t the same thing as iron in your body. Instead, ferritin is a protein that stores iron, releasing it when your body needs it. Transferrin is a protein that combines with ferritin to transport it to where new red blood cells are made.

How is cytoplasmic ferritin regulated?

The content of cytoplasmic ferritin is regulated by the translation of ferritin H and L mRNAs in response to an intracellular pool of “chelatable” or “labile” iron. 45, 46 Thus, when iron levels are low, ferritin synthesis is decreased; conversely, when iron levels are high, ferritin synthesis increases.

What is Frank Torti’s theory of ferritin regulation?

Frank M. Torti, Suzy V. Torti; Regulation of ferritin genes and protein. Blood 2002; 99 (10): 3505–3516. doi: https://doi.org/10.1182/blood.V99.10.3505 Increasingly, perturbations in cellular iron and ferritin are emerging as an important element in the pathogenesis of disease.

What are the subunits of ferritin?

Ferritin is a ubiquitous and highly conserved iron-binding protein. In vertebrates, the cytosolic form consists of 2 subunits, termed H and L. Twenty-four ferritin subunits assemble to form the apoferritin shell.

Why is ferritin important in the pathophysiology of hemochromatosis?

These changes in ferritin are important not only in the classic diseases of iron acquisition, transport, and storage, such as primary hemochromatosis, but also in diseases characterized by inflammation, infection, injury, and repair.

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