ferritina

Ferritin (Spanish: ferritina) is the primary iron-storage protein in virtually all living cells. It forms a spherical, hollow protein shell made of 24 subunits that can store thousands of iron atoms in a mineral form. In humans, ferritin consists of two subunit types, H (heavy) and L (light), in varying ratios by tissue. The protein keeps iron in a soluble, non-toxic form and supplies it for essential processes such as heme and DNA synthesis when needed. Most ferritin is intracellular, but small amounts circulate in the blood.

Ferritin functions as an iron reservoir and regulator of iron availability. Intracellular ferritin stores iron safely, releasing it through cellular pathways when the cell requires it. Serum ferritin is commonly used as a clinical proxy for total body iron stores, though the relationship is influenced by factors beyond iron status.

Clinical relevance is centered on ferritin levels. Low ferritin indicates iron deficiency, often guiding iron supplementation. Elevated ferritin can indicate iron overload disorders or conditions with increased iron storage. However, ferritin is also an acute-phase reactant, rising during inflammation, infection, liver disease, or malignancy, which can complicate interpretation of iron status.

Measurement and interpretation considerations include that ferritin is assessed in blood serum or plasma. Because levels can be affected by inflammation and other conditions, interpretation typically considers inflammatory markers and patient context (age, sex, pregnancy, comorbidities). Ferritin remains a widely used, accessible marker in evaluating iron balance and related disorders.