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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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Self-citationMicroorganisms pumping iron: anaerobic microbial iron oxidation and reduction
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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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