Proteins, proteomics


Ferritin is an an acute phase protein synthesized in response to pro-inflammatory cytokines early in the inflammatory response.

Ferritin is the chief iron storage protein for both eukaryotes and prokaryotes, and is termed apoferritin when not combined with Fe(3+) ions. The globular ferritin protein complex comprises 24 subunits – hetero-oligomers of light (L) and heavy (H) chains encoded by homologous genes (vertebrates), H chains only in bacteria and plants. Free Fe is toxic, so cells employ ferritin molecules or aggregates (hemosiderin) to form protective Fe-protein complexes. Each ferritin molecule complexes around 4500 (Fe3+)ions.

Ferritin is found in most tissues, particularly in the bone marrow and reticuloendothelial system (or mononuclear phagocytic system). Serum ferritin levels are proportional to iron storage levels in humans and are employed as a part of the work-up for anemia, particurlarly iron-deficiency anemia. However, ferritin levels are increased by acute inflammation, hemochromatosis, malignancy, hyperthyroidism, Still's Disease, or hepatic disease (necrotic hepatocytes), so ferritin levels may be misleading when anemia is concomitant with these conditions.


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. . . since 11/21/06