The dynamics of hepcidin-ferroportin internalization and consequences of a novel ferroportin disease mutation

American Journal of Hematology

Volumn 92, Issue 10, 2017, Pages 1052-1061

  Wallace, Daniel F ^a,b   McDonald, Cameron J ^b   Ostini, Lesa ^b   Iser, David ^c   Tuckfield, Annabel ^d   Subramaniam, V Nathan ^a,b  

^a QUEENSLAND UNIVERSITY OF TECHNOLOGY   (Australia)

^b QIMR BERGHOFER MEDICAL RESEARCH INSTITUTE   (Australia)

^c ST VINCENT S HOSPITAL   (Australia)

^d ROYAL MELBOURNE HOSPITAL   (Australia)

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBODY; FERRITIN; FERROPORTIN; HEPCIDIN; CATION TRANSPORT PROTEIN; CELL SURFACE RECEPTOR; HEPCIDIN 25, HUMAN; IRON; METAL TRANSPORTING PROTEIN 1;

ADULT; ARTICLE; CASE REPORT; CELL SURFACE; CLINICAL ARTICLE; DNA SEQUENCE; FEMALE; FERRITIN BLOOD LEVEL; FLOW CYTOMETRY; HEK293 CELL LINE; HISTOGRAM; HUMAN; HUMAN CELL; IMMUNOFLUORESCENCE; INTERNALIZATION; IRON HOMEOSTASIS; IRON METABOLISM; IRON OVERLOAD; IRON TRANSPORT; LIVER CELL; MOLECULAR DYNAMICS; MUTATION; NEXT GENERATION SEQUENCING; PHENOTYPE; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FUNCTION; BIOASSAY; BLOOD; GENETIC TRANSFECTION; GENETICS; IRON METABOLISM DISORDER; KINETICS; METABOLISM; PROTEIN TRANSPORT;

BIOLOGICAL ASSAY; CATION TRANSPORT PROTEINS; FEMALE; FLOW CYTOMETRY; HEK293 CELLS; HEPCIDINS; HUMANS; IRON; IRON METABOLISM DISORDERS; KINETICS; MUTATION; PROTEIN TRANSPORT; RECEPTORS, CELL SURFACE; TRANSFECTION;

EID: 85026447320     PISSN: 03618609     EISSN: 10968652     Source Type: Journal    
DOI: 10.1002/ajh.24844     Document Type: Article

References (30)

1. Nemeth E, Tuttle MS, Powelson J, et al. Hepcidin regulates cellular iron efflux by binding to ferroportin and inducing its internalization. Science. 2004;306:2090–2093.
2. Feder JN, Gnirke A, Thomas W, et al. A novel MHC class I-like gene is mutated in patients with hereditary haemochromatosis. Nat Genet. 1996;13:399–408.
3. Wallace DF, Subramaniam VN. Non-HFE haemochromatosis. World J Gastroenterol. 2007;13:4690–4698.
4. Montosi G, Donovan A, Totaro A, et al. Autosomal-dominant hemochromatosis is associated with a mutation in the ferroportin (SLC11A3) gene. J Clin Invest. 2001;108:619–623.
5. Njajou OT, Vaessen N, Joosse M, et al. A mutation in SLC11A3 is associated with autosomal dominant hemochromatosis. Nat Genet. 2001;28:213–214.
6. Mayr R, Janecke AR, Schranz M, et al. Ferroportin disease: a systematic meta-analysis of clinical and molecular findings. J Hepatol. 2010;53:941–949.
7. McDonald CJ, Wallace DF, Ostini L, et al. G80S-linked ferroportin disease: classical ferroportin disease in an Asian family and reclassification of the mutant as iron transport defective. J Hepatol. 2011;54:538–544.
8. Taniguchi R, Kato HE, Font J, et al. Outward- and inward-facing structures of a putative bacterial transition-metal transporter with homology to ferroportin. Nat Commun. 2015;6:8545.
9. McDonald CJ, Ostini L, Wallace DF, et al. Next-generation sequencing: application of a novel platform to the analysis of atypical iron disorders. J Hepatol. 2015;63:1288–1293.
10. Wallace DF, Pedersen P, Dixon JL, et al. Novel mutation in ferroportin1 is associated with autosomal dominant hemochromatosis. Blood. 2002;100:692–694.
11. Wallace DF, Harris JM, Subramaniam VN. Functional analysis and theoretical modeling of ferroportin reveals clustering of mutations according to phenotype. Am J Physiol, Cell Physiol. 2010;298:C75–C84.
12. Ross SL, Tran L, Winters A, et al. Molecular mechanism of hepcidin-mediated ferroportin internalization requires ferroportin lysines, not tyrosines or JAK-STAT. Cell Metab. 2012;15:905–917.
13. Wallace DF, Jones MD, Pedersen P, et al. Purification and partial characterisation of recombinant human hepcidin. Biochimie. 2006;88:31–37.
14. Wallace DF, Summerville L, Lusby PE, et al. Prohepcidin localises to the Golgi compartment and secretory pathway in hepatocytes. J Hepatol. 2005;43:720–728.
15. Liu XB, Yang F, Haile DJ. Functional consequences of ferroportin 1 mutations. Blood Cells Mol Dis. 2005;35:33–46.
16. Rice AE, Mendez MJ, Hokanson CA, et al. Investigation of the biophysical and cell biological properties of ferroportin, a multipass integral membrane protein iron exporter. J Mol Biol. 2009;386:717–732.
17. Daher R, Kannengiesser C, Houamel D, et al. Heterozygous mutations in BMP6 Pro-peptide lead to inappropriate hepcidin synthesis and moderate iron overload in humans. Gastroenterology. 2016;150:672–683.
18. Le Gac G, Gourlaouen I, Ka C, et al. The p.Leu96Pro missense mutation in the BMP6 gene is repeatedly associated with hyperferritinemia in patients of French origin. Gastroenterology. 2016;151:769–770.
19. McDonald CJ, Rishi G, Wallace DF, et al. Genetic variants in the BMP6 pro-peptide may not cause iron loading and should be interpreted with caution. Gastroenterology. 2016;151:770–771.
20. Wallace DF, Dixon JL, Ramm GA, et al. A novel mutation in ferroportin implicated in iron overload. J Hepatol. 2007;46:921–926.
21. De Domenico I, Ward DM, Nemeth E, et al. The molecular basis of ferroportin-linked hemochromatosis. Proc Natl Acad Sci USA U S A. 2005;102:8955–8960.
22. Callebaut I, Joubrel R, Pissard S, et al. Comprehensive functional annotation of 18 missense mutations found in suspected hemochromatosis type 4 patients. Hum Mol Genet. 2014;23:4479–4490.
23. Drakesmith H, Schimanski LM, Ormerod E, et al. Resistance to hepcidin is conferred by hemochromatosis-associated mutations of ferroportin. Blood. 2005;106:1092–1097.
24. Schimanski LM, Drakesmith H, Merryweather-Clarke AT, et al. In vitro functional analysis of human ferroportin (FPN) and hemochromatosis-associated FPN mutations. Blood. 2005;105:4096–4102.
25. Yeh KY, Yeh M, Glass J. Interactions between ferroportin and hephaestin in rat enterocytes are reduced after iron ingestion. Gastroenterology. 2011;141:292–299, 299 e291.
26. Praschberger R, Schranz M, Griffiths WJ, et al. Impact of D181V and A69T on the function of ferroportin as an iron export pump and hepcidin receptor. Biochim Biophys Acta. 2014;1842:1406–1412.
27. Goncalves AS, Muzeau F, Blaybel R, et al. Wild-type and mutant ferroportins do not form oligomers in transfected cells. Biochem J. 2006;396:265–275.
28. Le Gac G, Ka C, Joubrel R, et al. Structure-function analysis of the human ferroportin iron exporter (SLC40A1): effect of hemochromatosis type 4 disease mutations and identification of critical residues. Hum Mutat. 2013;34:1371–1380.
29. Mayr R, Griffiths WJ, Hermann M, et al. Identification of mutations in SLC40A1 that affect ferroportin function and phenotype of human ferroportin iron overload. Gastroenterology. 2011;140:2056–2063, 2063 e2051.
30. Kroot JJ, van Herwaarden AE, Tjalsma H, et al. Second round robin for plasma hepcidin methods: first steps toward harmonization. Am J Hematol. 2012;87:977–983.