title: Mammalian siderophores, siderophore-binding lipocalins, and the labile iron pool.
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.
authors.affiliation: Division of Basic Sciences, Fred Hutchinson Cancer Research Center, Seattle, Washington 98109, USA.
authors.forename: Colin
authors.initials: C
authors.lastname: Correnti
authors.forename: Roland K
authors.initials: RK
authors.lastname: Strong
mesh_terms: D000818:Animals; D000900:Anti-Bacterial Agents / Q000737:chemistry; D017209:Apoptosis; D001692:Biological Transport; D002352:Carrier Proteins / Q000737:chemistry; D002396:Catechols / Q000737:chemistry; D002614:Chelating Agents / Q000494:pharmacology; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007113:Immunity, Innate; D007501:Iron / Q000737:chemistry*; D007700:Kinetics; D000071068:Lipocalin-2; D054834:Lipocalins / Q000737:chemistry*; D008954:Models, Biological; D008956:Models, Chemical; D017262:Siderophores / Q000737:chemistry*
chemical_list: D000900:Anti-Bacterial Agents; D002352:Carrier Proteins; D002396:Catechols; D002614:Chelating Agents; C489506:LCN2 protein, human; D000071068:Lipocalin-2; D054834:Lipocalins; D017262:Siderophores; D007501:Iron