ferrittisiin

Ferritin is a globular protein found in all living organisms, serving as the primary intracellular iron-storage protein. It is composed of a protein shell, called an apoferritin, which encases a core of ferric hydroxide-phosphate. This structure allows ferritin to store up to 4,500 iron atoms in a soluble and non-toxic form. The release of iron from ferritin is a tightly regulated process, essential for cellular functions such as DNA synthesis, energy metabolism, and oxygen transport.

In humans, ferritin levels are often measured in blood tests as an indicator of the body's iron stores. Low ferritin levels can suggest iron deficiency anemia, a condition where the body lacks sufficient iron to produce adequate hemoglobin, the protein in red blood cells that carries oxygen. Conversely, elevated ferritin levels can be indicative of iron overload conditions like hemochromatosis, or can be a marker of inflammation or certain cancers.

The synthesis of ferritin is regulated by cellular iron levels. When iron is abundant, the cell increases ferritin production to store the excess. Conversely, when iron is scarce, ferritin synthesis decreases, allowing stored iron to be released. This dynamic regulation ensures that iron is available when needed and prevented from accumulating to toxic levels. Ferritin plays a crucial role in maintaining iron homeostasis, a delicate balance vital for health.