Disposal of iron by a mutant form of lipocalin 2

Barasch, Jonathan; Hollmen, Maria; Deng, Rong; Hod, Eldad A.; Rupert, Peter B.; Abergel, Rebecca J.; Allred, Benjamin E.; Xu, Katherine; Darrah, Shaun F.; Tekabe, Yared; Perlstein, Alan; Wax, Rebecca; Bruck, Efrat; Stauber, Jacob; Corbin, Kaitlyn A.; Buchen, Charles; Slavkovich, Vesna; Graziano, Joseph; Spitalnik, Steven L.; Bao, Guanhu; Strong, Roland K.; Qiu, Andong

doi:10.1038/ncomms12973

Title: Disposal of iron by a mutant form of lipocalin 2

Journal Article · Mon Oct 31 00:00:00 EDT 2016 · Nature Communications

DOI:https://doi.org/10.1038/ncomms12973· OSTI ID:1458480

Barasch, Jonathan ^[1]; Hollmen, Maria ^[1]; Deng, Rong ^[1]; Hod, Eldad A. ^[1]; Rupert, Peter B. ^[2]; Abergel, Rebecca J. ^[3]; Allred, Benjamin E. ^[3]; Xu, Katherine ^[1]; Darrah, Shaun F. ^[1]; Tekabe, Yared ^[1]; Perlstein, Alan ^[1]; Wax, Rebecca ^[1]; Bruck, Efrat ^[1]; Stauber, Jacob ^[1]; Corbin, Kaitlyn A. ^[1]; Buchen, Charles ^[1]; Slavkovich, Vesna ^[1]; Graziano, Joseph ^[1]; Spitalnik, Steven L. ^[1]; Bao, Guanhu ^[4] more »

Columbia Univ., New York, NY (United States)
Fred Hutchinson Cancer Research Center, Seattle, WA (United States). Basic Sciences Division; Univ. of Washington, Seattle, WA (United States). School of Medicine and Dept. of Biochemistry and Immunology
Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States). Chemical Sciences Division and BioActinide Chemistry Group
Anhui Agricultural Univ., Hefei (China). State Key Lab. of Tea Plant Biology and Utilization and School of Tea and Food Sciences
Columbia Univ., New York, NY (United States); Tongji Univ., Shanghai (China). School of Life Sciences and Technology

Iron overload damages many organs. Unfortunately, therapeutic iron chelators also have undesired toxicity and may deliver iron to microbes. In this work, we show that a mutant form (K3Cys) of endogenous lipocalin 2 (LCN2) is filtered by the kidney but can bypass sites of megalin-dependent recapture, resulting in urinary excretion. Because K3Cys maintains recognition of its cognate ligand, the iron siderophore enterochelin, this protein can capture and transport iron even in the acidic conditions of urine. Mutant LCN2 strips iron from transferrin and citrate, and delivers it into the urine. In addition, it removes iron from iron overloaded mice, including models of acquired (iron-dextran or stored red blood cells) and primary (Hfe^-/-) iron overload. In each case, the mutants reduce redox activity typical of non-transferrin-bound iron. In summary, we present a non-toxic strategy for iron chelation and urinary elimination, based on manipulating an endogenous protein:siderophore:iron clearance pathway.

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Research Organization:: Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States)

Sponsoring Organization:: USDOE Office of Science (SC), Basic Energy Sciences (BES). Chemical Sciences, Geosciences, and Biosciences Division; March of Dimes, White Plains, NY (United States); American Heart Association (AHA); National Natural Science Foundation of China (NSFC)

Contributing Organization:: Max Delbruck Center for Molecular Medicine in the Helmholtz Association, Berlin (Germany)

Grant/Contract Number:: AC02-05CH11231; R21 DK091729; R01DK073462; R01DK092684; 14GRNT18840098; 81170654/H0507

OSTI ID:: 1458480

Journal Information:: Nature Communications, Vol. 7; Related Information: © The Author(s) 2016.; ISSN 2041-1723

Publisher:: Nature Publishing GroupCopyright Statement

Country of Publication:: United States

Language:: English

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Cited by: 26 works

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