Cargando…
Erythropoiesis and Iron Sulfur Cluster Biogenesis
Erythropoiesis in animals is a synchronized process of erythroid cell differentiation that depends on successful acquisition of iron. Heme synthesis depends on iron through its dependence on iron sulfur (Fe-S) cluster biogenesis. Here, we review the relationship between Fe-S biogenesis and heme synt...
Autores principales: | , |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
Hindawi Publishing Corporation
2010
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2939393/ https://www.ncbi.nlm.nih.gov/pubmed/20862391 http://dx.doi.org/10.1155/2010/329394 |
_version_ | 1782186715070332928 |
---|---|
author | Ye, Hong Rouault, Tracey A. |
author_facet | Ye, Hong Rouault, Tracey A. |
author_sort | Ye, Hong |
collection | PubMed |
description | Erythropoiesis in animals is a synchronized process of erythroid cell differentiation that depends on successful acquisition of iron. Heme synthesis depends on iron through its dependence on iron sulfur (Fe-S) cluster biogenesis. Here, we review the relationship between Fe-S biogenesis and heme synthesis in erythropoiesis, with emphasis on the proteins, GLRX5, ABCB7, ISCA, and C1orf69. These Fe-S biosynthesis proteins are highly expressed in erythroid tissues, and deficiency of each of these proteins has been shown to cause anemia in zebrafish model. GLRX5 is involved in the production and ABCB7 in the export of an unknown factor that may function as a gauge of mitochondrial iron status, which may indirectly modulate activity of iron regulatory proteins (IRPs). ALAS2, the enzyme catalyzing the first step in heme synthesis, is translationally controlled by IRPs. GLRX5 may also provide Fe-S cofactor for ferrochelatase, the last enzyme in heme synthesis. ISCA and C1orf69 are thought to assemble Fe-S clusters for mitochondrial aconitase and for lipoate synthase, the enzyme producing lipoate for pyruvate dehydrogenase complex (PDC). PDC and aconitase are involved in the production of succinyl-CoA, a substrate for heme biosynthesis. Thus, many steps of heme synthesis depend on Fe-S cluster assembly. |
format | Text |
id | pubmed-2939393 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
publisher | Hindawi Publishing Corporation |
record_format | MEDLINE/PubMed |
spelling | pubmed-29393932010-09-22 Erythropoiesis and Iron Sulfur Cluster Biogenesis Ye, Hong Rouault, Tracey A. Adv Hematol Review Article Erythropoiesis in animals is a synchronized process of erythroid cell differentiation that depends on successful acquisition of iron. Heme synthesis depends on iron through its dependence on iron sulfur (Fe-S) cluster biogenesis. Here, we review the relationship between Fe-S biogenesis and heme synthesis in erythropoiesis, with emphasis on the proteins, GLRX5, ABCB7, ISCA, and C1orf69. These Fe-S biosynthesis proteins are highly expressed in erythroid tissues, and deficiency of each of these proteins has been shown to cause anemia in zebrafish model. GLRX5 is involved in the production and ABCB7 in the export of an unknown factor that may function as a gauge of mitochondrial iron status, which may indirectly modulate activity of iron regulatory proteins (IRPs). ALAS2, the enzyme catalyzing the first step in heme synthesis, is translationally controlled by IRPs. GLRX5 may also provide Fe-S cofactor for ferrochelatase, the last enzyme in heme synthesis. ISCA and C1orf69 are thought to assemble Fe-S clusters for mitochondrial aconitase and for lipoate synthase, the enzyme producing lipoate for pyruvate dehydrogenase complex (PDC). PDC and aconitase are involved in the production of succinyl-CoA, a substrate for heme biosynthesis. Thus, many steps of heme synthesis depend on Fe-S cluster assembly. Hindawi Publishing Corporation 2010 2010-08-31 /pmc/articles/PMC2939393/ /pubmed/20862391 http://dx.doi.org/10.1155/2010/329394 Text en Copyright © 2010 H. Ye and T. A. Rouault. https://creativecommons.org/licenses/by/3.0/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Review Article Ye, Hong Rouault, Tracey A. Erythropoiesis and Iron Sulfur Cluster Biogenesis |
title | Erythropoiesis and Iron Sulfur Cluster Biogenesis |
title_full | Erythropoiesis and Iron Sulfur Cluster Biogenesis |
title_fullStr | Erythropoiesis and Iron Sulfur Cluster Biogenesis |
title_full_unstemmed | Erythropoiesis and Iron Sulfur Cluster Biogenesis |
title_short | Erythropoiesis and Iron Sulfur Cluster Biogenesis |
title_sort | erythropoiesis and iron sulfur cluster biogenesis |
topic | Review Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2939393/ https://www.ncbi.nlm.nih.gov/pubmed/20862391 http://dx.doi.org/10.1155/2010/329394 |
work_keys_str_mv | AT yehong erythropoiesisandironsulfurclusterbiogenesis AT rouaulttraceya erythropoiesisandironsulfurclusterbiogenesis |