Abstract
The ability of iron to exist in both ferric and ferrous states underlies its role in critical enzyme reactions concerned with oxygen and electron transport and the cellular production of energy. Because of the poor solubility of iron, living organisms developed a wide variety of proteins involved in its absorption, transport and storage. Intracellular iron homeostasis is achieved by coordinated regulation of transferrin receptor and ferritin at the level of RNA translation by two cytoplasmic iron-dependent proteins, IRP1 and IRP2 to maintain a constant intracellular iron content. Systemic iron homeostasis is controlled by hepcidin, a polypeptide made in the liver. Hepcidin regulates iron homeostasis by binding to cell-surface ferroportin, causing its degradation, thereby inhibiting iron absorption and iron release from macrophages. Hepcidin synthesis is itself regulated by iron stores, inflammatory cytokines and erythropoiesis. Despite these powerful homeostatic mechanisms, iron deficiency is one of the most common nutritional problems. It is the outcome of blood loss, increased physiologic demands and limited supply when the diet is of poor quality and mainly vegetarian. Despite some improvement in recent years, iron deficiency remains the top ranking cause of anaemia worldwide. Pathological alterations in haem synthesis include the porphyrias, and sideroblastic anaemia. Porphyrias are characterized by a defect in haem synthesis resulting in the accumulation of haem intermediates in the liver or the erythron. The sideroblastic anaemias comprise a group of refractory anaemias with an excess of iron appearing as "rings" in the developing erythroblasts.
| Original language | English |
|---|---|
| Title of host publication | Postgraduate Haematology: Seventh Edition |
| Publisher | Wiley Blackwell |
| Pages | 21-39 |
| Number of pages | 19 |
| ISBN (Electronic) | 9781118853771 |
| ISBN (Print) | 9781118854327 |
| DOIs | |
| Publication status | Published - Nov 6 2015 |
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Keywords
- Haem
- Hepcidin
- Iron
- Iron deficiency
- Porphyria
- Sideroblastic anaemia
ASJC Scopus subject areas
- Medicine(all)
Cite this
Iron Metabolism, Iron Deficiency and Disorders of Haem Synthesis. / Camaschella, Clara; Victor Hoffbrand, A.; Hershko, Chaim.
Postgraduate Haematology: Seventh Edition. Wiley Blackwell, 2015. p. 21-39.Research output: Chapter in Book/Report/Conference proceeding › Chapter
}
TY - CHAP
T1 - Iron Metabolism, Iron Deficiency and Disorders of Haem Synthesis
AU - Camaschella, Clara
AU - Victor Hoffbrand, A.
AU - Hershko, Chaim
PY - 2015/11/6
Y1 - 2015/11/6
N2 - The ability of iron to exist in both ferric and ferrous states underlies its role in critical enzyme reactions concerned with oxygen and electron transport and the cellular production of energy. Because of the poor solubility of iron, living organisms developed a wide variety of proteins involved in its absorption, transport and storage. Intracellular iron homeostasis is achieved by coordinated regulation of transferrin receptor and ferritin at the level of RNA translation by two cytoplasmic iron-dependent proteins, IRP1 and IRP2 to maintain a constant intracellular iron content. Systemic iron homeostasis is controlled by hepcidin, a polypeptide made in the liver. Hepcidin regulates iron homeostasis by binding to cell-surface ferroportin, causing its degradation, thereby inhibiting iron absorption and iron release from macrophages. Hepcidin synthesis is itself regulated by iron stores, inflammatory cytokines and erythropoiesis. Despite these powerful homeostatic mechanisms, iron deficiency is one of the most common nutritional problems. It is the outcome of blood loss, increased physiologic demands and limited supply when the diet is of poor quality and mainly vegetarian. Despite some improvement in recent years, iron deficiency remains the top ranking cause of anaemia worldwide. Pathological alterations in haem synthesis include the porphyrias, and sideroblastic anaemia. Porphyrias are characterized by a defect in haem synthesis resulting in the accumulation of haem intermediates in the liver or the erythron. The sideroblastic anaemias comprise a group of refractory anaemias with an excess of iron appearing as "rings" in the developing erythroblasts.
AB - The ability of iron to exist in both ferric and ferrous states underlies its role in critical enzyme reactions concerned with oxygen and electron transport and the cellular production of energy. Because of the poor solubility of iron, living organisms developed a wide variety of proteins involved in its absorption, transport and storage. Intracellular iron homeostasis is achieved by coordinated regulation of transferrin receptor and ferritin at the level of RNA translation by two cytoplasmic iron-dependent proteins, IRP1 and IRP2 to maintain a constant intracellular iron content. Systemic iron homeostasis is controlled by hepcidin, a polypeptide made in the liver. Hepcidin regulates iron homeostasis by binding to cell-surface ferroportin, causing its degradation, thereby inhibiting iron absorption and iron release from macrophages. Hepcidin synthesis is itself regulated by iron stores, inflammatory cytokines and erythropoiesis. Despite these powerful homeostatic mechanisms, iron deficiency is one of the most common nutritional problems. It is the outcome of blood loss, increased physiologic demands and limited supply when the diet is of poor quality and mainly vegetarian. Despite some improvement in recent years, iron deficiency remains the top ranking cause of anaemia worldwide. Pathological alterations in haem synthesis include the porphyrias, and sideroblastic anaemia. Porphyrias are characterized by a defect in haem synthesis resulting in the accumulation of haem intermediates in the liver or the erythron. The sideroblastic anaemias comprise a group of refractory anaemias with an excess of iron appearing as "rings" in the developing erythroblasts.
KW - Haem
KW - Hepcidin
KW - Iron
KW - Iron deficiency
KW - Porphyria
KW - Sideroblastic anaemia
UR - http://www.scopus.com/inward/record.url?scp=84976351114&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84976351114&partnerID=8YFLogxK
U2 - 10.1002/9781118853771.ch3
DO - 10.1002/9781118853771.ch3
M3 - Chapter
AN - SCOPUS:84976351114
SN - 9781118854327
SP - 21
EP - 39
BT - Postgraduate Haematology: Seventh Edition
PB - Wiley Blackwell
ER -