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...

Descripción completa

Detalles Bibliográficos
Autores principales: Ye, Hong, Rouault, Tracey A.
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