PMID:22389496

Citation	Correnti, C and Strong, RK (2012) Mammalian siderophores, siderophore-binding lipocalins, and the labile iron pool. J. Biol. Chem. 287:13524-31
Abstract	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.
Links	PubMed PMC3340207 Online version:10.1074/jbc.R111.311829
Keywords	Animals; Anti-Bacterial Agents/chemistry; Apoptosis; Biological Transport; Carrier Proteins/chemistry; Catechols/chemistry; Chelating Agents/pharmacology; Humans; Hydrogen-Ion Concentration; Immunity, Innate; Iron/chemistry; Kinetics; Lipocalins/chemistry; Models, Biological; Models, Chemical; Siderophores/chemistry
edit table

Significance

You can help EcoliWiki by summarizing why this paper is useful

You can help Ecoliwiki by describing the useful materials (strains, plasmids, antibodies, etc) described in this paper.

Add links to pages that link here (e.g. gene, product, method pages)

See Help:References for how to manage references in EcoliWiki.