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The ferritin levels measured usually have a direct correlation with the total amount of iron stored in the body. However, ferritin levels may be artificially high in cases of anemia of chronic disease, where ferritin is elevated in its capacity as an inflammatory acute phase protein and not as a marker for iron overload. [citation needed]
Serum ferritin testing is a low-cost, readily available, and minimally invasive method for assessing body iron stores. However ferritin levels may be elevated due to a variety of other causes including obesity, infection, inflammation (as an acute phase protein), chronic alcohol intake, liver disease, kidney disease, and cancer.
Export occurs through ferroportin, often aided by hephaestin (Hp) and/or ceruloplasmin (Cp), and repressed by hepcidin. Human iron metabolism is the set of chemical reactions that maintain human homeostasis of iron at the systemic and cellular level. Iron is both necessary to the body and potentially toxic.
Low, as the body holds iron intracellularly with ferritin. Low. The body produces less transferrin (but more ferritin), presumably to keep iron away from pathogens that require it for their metabolism. This is mainly regulated by increased hepcidin production. Normal Pregnancy or use of hormonal contraception, but without iron deficiency Normal ...
Hemosiderin or haemosiderin is an iron -storage complex that is composed of partially digested ferritin and lysosomes. The breakdown of heme gives rise to biliverdin and iron. [1][2] The body then traps the released iron and stores it as hemosiderin in tissues. [3] Hemosiderin is also generated from the abnormal metabolic pathway of ferritin.
Serum ferritin is a low cost, readily available, and minimally invasive method for assessing body iron stores. However, the major problem with using it as an indicator of hemosiderosis is that it can be elevated in a range of other medical conditions unrelated to iron levels including infection, inflammation, fever, liver disease, renal disease ...
Ferritin, a protein synthesized by the liver, is the primary form of iron storage within cells and tissues. Measuring ferritin provides a crude estimate of whole-body iron stores, though is raised in many conditions, particularly inflammatory conditions.
Structure. In humans, transferrin consists of a polypeptide chain containing 679 amino acids and two carbohydrate chains. The protein is composed of alpha helices and beta sheets that form two domains. [18] The N- and C- terminal sequences are represented by globular lobes and between the two lobes is an iron-binding site.