The DOI matches its Crossref record; 37 of the 37 references it cites were found in a registry or an index.
Dysfunction of the heme recycling system in heme oxygenase 1–deficient mice: effects on macrophage viability and tissue iron distribution
Open accessAbstract
To better understand the tissue iron overload and anemia previously reported in a human patient and mice that lack heme oxygenase-1 (HO-1), we studied iron distribution and pathology in HO-1(Hmox1)−/− mice. We found that resident splenic and liver macrophages were mostly absent in HO-1−/− mice. Erythrophagocytosis caused the death of HO-1−/− macrophages in in vitro experiments, supporting the hypothesis that HO-1−/− macrophages died of exposure to heme released on erythrophagocytosis. Rupture of HO-1−/− macrophages in vivo and release of nonmetabolized heme probably caused tissue inflammation. In the spleen, initial splenic enlargement progressed to red pulp fibrosis, atrophy, and functional hyposplenism in older mice, recapitulating the asplenia of an HO-1–deficient patient. We postulate that the failure of tissue macrophages to remove senescent erythrocytes led to intravascular hemolysis and increased expression of the heme and hemoglobin scavenger proteins, hemopexin and haptoglobin. Lack of macrophages expressing the haptoglobin receptor, CD163, diminished the ability of haptoglobin to neutralize circulating hemoglobin, and iron overload occurred in kidney proximal tubules, which were able to catabolize heme with HO-2. Thus, in HO-1−/− mammals, the reduced function and viability of erythrophagocytosing macrophages are the main causes of tissue damage and iron redistribution.
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Cites
Reduced stress defense in heme oxygenase 1-deficient cells
Poss, K. D., & Tonegawa, S. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.20.10925 · Cited by 1,291
Oxidative stress causes enhanced endothelial cell injury in human heme oxygenase-1 deficiency
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Heme oxygenase 1 is required for mammalian iron reutilization
Poss, K. D., & Tonegawa, S. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.20.10919 · Cited by 1,016
Megalin and cubilin: multifunctional endocytic receptors
Christensen, E. I., & Birn, H. (2002) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm778 · Cited by 842
LaVaute, T., Smith, S., Cooperman, S., Iwai, K., Land, W., Meyron-Holtz, E., Drake, S. K., Miller, G., Abu-Asab, M., Tsokos, M., et al. (2001) · Nature Genetics · doi:10.1038/84859 · Cited by 509
Self-citationIdentification of the receptor scavenging hemopexin-heme complexes
Hvidberg, V., Maniecki, M. B., Jacobsen, C., Højrup, P., Møller, H. J., & Moestrup, S. K. (2005) · Blood · doi:10.1182/blood-2005-03-1185 · Cited by 473
The macrophage scavenger receptor CD163
Fabriek, B. O., Dijkstra, C. D., & van den Berg, T. K. (2005) · Immunobiology · doi:10.1016/j.imbio.2005.05.010 · Cited by 454
CD163: a regulated hemoglobin scavenger receptor with a role in the anti‐inflammatory response
Moestrup, S., & Møller, H. (2004) · Annals of Medicine · doi:10.1080/07853890410033171 · Cited by 442
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Hemopexin: structure, function, and regulation
Tolosano, E., & Altruda, F. (2002) · DNA and Cell Biology · doi:10.1089/104454902753759717 · Cited by 426
Cited by
Molecular Pathophysiology of Cerebral Hemorrhage: Secondary Brain Injury
Aronowski, J., & Zhao, X. (2011) · Stroke · doi:10.1161/strokeaha.110.596718 · Cited by 832
Metabolism of tissue macrophages in homeostasis and pathology
Wculek, S. K., Dunphy, G., Heras-Murillo, I., Mastrangelo, A., & Sancho, D. (2022) · Cellular & Molecular Immunology · doi:10.1038/s41423-021-00791-9 · Cited by 501
Heme in pathophysiology: a matter of scavenging, metabolism and trafficking across cell membranes
Chiabrando, D., Vinchi, F., Fiorito, V., Mercurio, S., & Tolosano, E. (2014) · Frontiers in Pharmacology · doi:10.3389/fphar.2014.00061 · Cited by 450
Heme-mediated SPI-C induction promotes monocyte differentiation into iron-recycling macrophages
Haldar, M., Kohyama, M., So, A. Y.-L., KC, W., Wu, X., Briseño, C. G., Satpathy, A. T., Kretzer, N. M., Arase, H., Rajasekaran, N. S., et al. (2014) · Cell · doi:10.1016/j.cell.2014.01.069 · Cited by 431
“The enzyme HO1 converts heme to biliverdin releasing the heme-associated iron while the enzyme biliverdin reductase (BLVR) converts biliverdin to bilirubin (Beaumont and Delaby, 2009).”
InfluentialRegulation of inflammation by the antioxidant haem oxygenase 1
Campbell, N. K., Fitzgerald, H. K., & Dunne, A. (2021) · Nature Reviews Immunology · doi:10.1038/s41577-020-00491-x · Cited by 420
Metadata
- Authors
- Kovtunovych, G., Eckhaus, M. A., Ghosh, M. C., Ollivierre-Wilson, H., & Rouault, T. A.
- Venue
- Blood
- Publisher
- American Society of Hematology
- Published
- 2010-12-23
- Volume
- 116
- Issue
- 26
- Pages
- 6054-6062
- ISSN
- 0006-4971 (ISSN-L)
- 1528-0020
- OpenAlex
- W2027427419
- Cited by
- 271
- References
- 37
- FWCI
- 4.84
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Kovtunovych, G., Eckhaus, M. A., Ghosh, M. C., Ollivierre-Wilson, H., & Rouault, T. A. (2010). Dysfunction of the heme recycling system in heme oxygenase 1–deficient mice: effects on macrophage viability and tissue iron distribution. Blood. https://doi.org/10.1182/blood-2010-03-272138
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