The DOI matches its Crossref record; 88 of the 88 references it cites were found in a registry or an index.
Mammalian Siderophores, Siderophore-binding Lipocalins, and the Labile Iron Pool
Open accessAbstract
Bacteria use tight-binding, ferric-specific chelators called siderophores to acquire iron from the environment and from the host during infection; animals use proteins such as transferrin and ferritin to transport and store iron. Recently, candidate compounds that could serve endogenously as mammalian siderophore equivalents have been identified and characterized through associations with siderocalin, the only mammalian siderophore-binding protein currently known. Siderocalin, an antibacterial protein, acts by sequestering iron away from infecting bacteria as siderophore complexes. Candidate endogenous siderophores include compounds that only effectively transport iron as ternary complexes with siderocalin, explaining pleiotropic activities in normal cellular processes and specific disease states.
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“These are best characterized in bacteria, but eukaryotes including fungi and mammals produce siderophores, too [16, 42, 67, 86, 106].”
From “Pumping iron”—how macrophages handle iron at the systemic, microenvironmental, and cellular levels (2017) · cites this paper as [42]
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Cites
Two to tango: Regulation of Mammalian iron metabolism
Hentze, M. W., Muckenthaler, M. U., Galy, B., & Camaschella, C. (2010) · Cell · doi:10.1016/j.cell.2010.06.028 · Cited by 2,120
Lipocalin 2 mediates an innate immune response to bacterial infection by sequestrating iron
Flo, T. H., Smith, K. D., Sato, S., Rodriguez, D. J., Holmes, M. A., Strong, R. K., Akira, S., & Aderem, A. (2004) · Nature · doi:10.1038/nature03104 · Cited by 1,877
Self-citationMicroorganisms pumping iron: anaerobic microbial iron oxidation and reduction
Weber, K. A., Achenbach, L. A., & Coates, J. D. (2006) · Nature Reviews Microbiology · doi:10.1038/nrmicro1490 · Cited by 1,831
Siderophore-Based Iron Acquisition and Pathogen Control
Miethke, M., & Marahiel, M. A. (2007) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00012-07 · Cited by 1,774
Siderophores: Structure and Function of Microbial Iron Transport Compounds
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Self-citationNeilands, J. B. (1981) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.50.070181.003435 · Cited by 1,232
Enterobactin: an archetype for microbial iron transport.
Raymond, K. N., Dertz, E. A., & Kim, S. S. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0630018100 · Cited by 933
Bacterial Iron Sources: From Siderophores to Hemophores
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Iron withholding: a defense against infection and neoplasia
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Nutritional immunity: the battle for nutrient metals at the host–pathogen interface
Murdoch, C. C., & Skaar, E. P. (2022) · Nature Reviews Microbiology · doi:10.1038/s41579-022-00745-6 · Cited by 701
Lipocalin 2: an emerging player in iron homeostasis and inflammation
Xiao, X., Yeoh, B. S., & Vijay-Kumar, M. (2017) · Annual Review of Nutrition · doi:10.1146/annurev-nutr-071816-064559 · Cited by 426
Iron transport and its regulation in plants
Kobayashi, T., Nozoye, T., & Nishizawa, N. K. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.10.439 · Cited by 403
Shared and distinct mechanisms of iron acquisition by bacterial and fungal pathogens of humans
Caza, M., & Kronstad, J. W. (2013) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2013.00080 · Cited by 306
Diverging roles of bacterial siderophores during infection
Holden, V. I., & Bachman, M. A. (2015) · Metallomics · doi:10.1039/c4mt00333k · Cited by 274
Metadata
- Authors
- Correnti, C., & Strong, R. K.
- Affiliations
- Fred Hutch Cancer Center (US)
- Corresponding author
- Strong, Roland K.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2012-04
- Volume
- 287
- Issue
- 17
- Pages
- 13524-13531
- ISSN
- 0021-9258 (ISSN-L)
- PMC
- PMC3340207
- OpenAlex
- W1990262536
- Cited by
- 115
- References
- 88
- Citations by year
- 2025: 3 · 2024: 4 · 2023: 5 · 2022: 7 · 2021: 11 · 2020: 4 · 2019: 12 · 2018: 8 · 2017: 6 · 2016: 10 · 2015: 11 · 2014: 12 · 2013: 12 · 2012: 6
- FWCI
- 2.08
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of Allergy and Infectious Diseases (AI 059432, R01AI059432)
- National Institute of Diabetes and Digestive and Kidney Diseases (R01DK073462, R21DK091729, DK091729, DK073462)
- Topics
- Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Hemoglobin structure and function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Keywords
- siderocalin, labile iron pool, iron acquisition, iron transport, iron storage, transferrin, ferritin, antibacterial proteins
- MeSH terms
- Lipocalin-2, Animals, Anti-Bacterial Agents, Biological Transport, Carrier Proteins, Catechols, Chelating Agents, Humans, Hydrogen-Ion Concentration, Immunity, Innate, Iron, Kinetics, Models, Biological, Models, Chemical, Apoptosis, Siderophores, Lipocalins
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