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Hemoglobin in the blood carries oxygen from the respiratory organs (lungs or gills) to the other tissues of the body, where it releases the oxygen to enable aerobic respiration which powers an animal's metabolism. A healthy human has 12 to 20 grams of hemoglobin in every 100 mL of blood. Hemoglobin is a metalloprotein, a chromoprotein, and ...
The liver produces hepcidin. Hepcidin controls iron absorption in the gastrointestinal tract and iron release from reticuloendothelial tissue. Iron must be released from macrophages in the bone marrow to be incorporated into the heme group of hemoglobin in erythrocytes. There are colony forming units that the cells follow during their formation.
Hemoglobin A (HbA), also known as adult hemoglobin, hemoglobin A1 or α 2 β 2, is the most common human hemoglobin tetramer, accounting for over 97% of the total red blood cell hemoglobin. [1] Hemoglobin is an oxygen-binding protein, found in erythrocytes , which transports oxygen from the lungs to the tissues. [ 2 ]
The most famous mutation in the globin fold is a change from glutamate to valine in one chain of the hemoglobin molecule. This mutation creates a "hydrophobic patch" on the protein surface that promotes intermolecular aggregation, the molecular event that gives rise to sickle-cell disease. [citation needed]
In biochemistry, the Luebering–Rapoport pathway (also called the Luebering–Rapoport shunt) is a metabolic pathway in mature erythrocytes involving the formation of 2,3-bisphosphoglycerate (2,3-BPG), which regulates oxygen release from hemoglobin and delivery to tissues. 2,3-BPG, the reaction product of the Luebering–Rapoport pathway was first described and isolated in 1925 by the ...
Increased erythrocyte synthesis also stimulates iron absorption in the gut. [15] Therefore, oral bioavailability of iron varies greatly, ranging from less than 1% to greater than 50%. [ 16 ] Uptake of iron can be enhanced by dietary heme iron and vitamin C , while inhibited by calcium , polyphenols , tannins and phytates .
Owing to this unique heme-sensing capacity, it plays a crucial role in shutting off protein synthesis during acute heme-deficient conditions. In red blood cells (RBCs), it controls hemoglobin synthesis ensuring a coordinated regulation of the synthesis of the heme and globin moieties of hemoglobin. Thus plays an essential protective role for ...
In vivo, starting with the proerythroblast stage, erythroid cells undergo several more cell divisions while at the same time upregulating survival genes such as Bcl-xL, acquiring and storing large amounts of iron, ramping up the synthesis of hemoglobin and other erythroid genes (in large part a GATA-1 dependent process that is augmented by the ...