Wolfgang Vogel

Innsbruck Medical University

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Heinz Zoller

Innsbruck Medical University

Melanie Schranz

Ospedale Papa Giovanni XXIII

Timothy M. Cox

University of Cambridge

Martin Hermann

Krankenanstalt Rudolfstiftung der Stadt Wien

William J. Griffiths

Cambridge University Hospitals NHS Foundation Trust

Roman Praschberger

VIB-KU Leuven Center for Brain & Disease Research

Roman Mayr

University of Regensburg

Martin P. Schulman

University of Illinois Chicago

Robert J. Simpson

Hull Royal Infirmary

Javier Díaz‐Castro

Universidad de Granada

Cooperative Institutions

Innsbruck Medical University

Universität Innsbruck

University of Cambridge

University Hospital Innsbruck

Cambridge University Hospitals NHS Foundation Trust

Addenbrooke's Hospital

University College London

National Health Service

University of Birmingham

University Hospitals Birmingham NHS Foundation Trust

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Identification of Mutations in SLC40A1 That Affect Ferroportin Function and Phenotype of Human Ferroportin Iron Overload

Gastroenterology (2011)

Roman Mayr William J. Griffiths Martin Hermann Ian G. McFarlane David Halsall

Ferroportin

Transferrin saturation

HAMP

Transport protein

Transferrin receptor

10.1053/j.gastro.2011.02.064

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Citations (58)

Pathways for the regulation of DMT-1 and FP-1 expression by iron in human intestine

Gastroenterology (2001)

Heinz Zoller Igor Theurl R. M. Koch Wolfgang Vogel Günter Weiß

Expression (computer science)

10.1016/s0016-5085(08)83385-9

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Citations (0)

Activation and inactivation of the iron hormone hepcidin: Biochemical characterization of prohepcidin cleavage and sequential degradation to N-terminally truncated hepcidin isoforms

Blood Cells Molecules and Diseases (2009)

Melanie Schranz Rania Bakry Marc Creus Günther K. Bonn Wolfgang Vogel

Furin

Proprotein Convertases

Prohormone convertase

Proprotein Convertases

Protein precursor

Cleavage (geology)

Proteolysis

10.1016/j.bcmd.2009.03.008

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Citations (26)

Heme Synthesis in Iron-deficient Duck Blood

Journal of Biological Chemistry (1960)

Wolfgang Vogel Dan A. Richert Burnett Q. Pixley Martin P. Schulman

10.1016/s0021-9258(19)76879-3

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Citations (38)

Characterization of the transition-metal-binding properties of hepcidin

Biochemical Journal (2010)

Chris Tselepis Samuel Ford Andrew T. McKie Wolfgang Vogel Heinz Zoller

Accumulating evidence suggests that hepcidin, a 25-residue peptide hormone, is the master regulator of iron metabolism. Further evidence suggests that the five N-terminal amino acids are crucial for mediating its biological function. With a histidine residue at position 3, this region also has the potential to bind bivalent metal ions. To characterize this hepcidin-metal interaction in detail, the present study utilizes electrospray MS to measure the binding of a range of metal ions to wild-type and mutant human and murine hepcidins. In addition, the biological effects of these point mutations were tested on Caco-2 and HEK-293T human cell lines and in mice. Our results show that hepcidin-25 can form complexes with copper, nickel and zinc; however, we failed to detect any hepcidin-25 binding to either ferric or ferrous ions. The greatest affinity observed was between hepcidin-25 and copper with a dissociation constant <<1 microM. Substituting the histidine residue at position 3 in human hepcidin-25 and comparably the asparagine residue at position 3 in murine hepcidin-25 with an alanine residue markedly diminished the affinity for copper. The amino acid substitutions also decreased the biological activity of hepcidin-25; namely repression of ferroportin protein levels and hypoferraemia. In summary, the high affinity of hepcidin for copper suggests that hepcidin could bind copper in vivo and this may be of biological relevance.

Ferroportin

Alanine

Metalloprotein

Residue (chemistry)

10.1042/bj20091521

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Citations (42)

A novel binding site for the native hepatic acute‐phase protein α1‐antitrypsin expressed on the human hepatoma cell line HepG 2 and intestinal cell line Caco 2

Liver International (2000)

Ivo Graziadei Wolfgang Vogel Adrian Bomford

Abstract: Aims/Background: α1‐antitrypsin (α1‐AT) is a hepatic acute phase protein which predominantly inhibits neutrophil elastase. Besides this major function, we have also previously shown that α1‐AT markedly increased H‐ferritin mRNA expression and ferritin synthesis in the human hepatoma cell line HepG 2. These actions suggest that α1‐AT might interact with HepG 2 cells via a specific cell surface binding site. Methods and Results: Using radio‐labelled native α1‐AT, we observed saturable binding to HepG 2 cells with a dissociation constant (Kd) of 63.3±6.9 nM and a maximal density of binding sites (Bmax) of 0.34 ±0.05 pmol/10 6 cells equivalent to 195800±29200 sites/cell. The binding of [ 125 I]α1‐AT was time dependent with a calculated association rate constant of 9.22±1.84×10 4 ×M −1 ×min −1 . Binding was highly specific since other acute phase proteins or protease inhibitors failed to block binding. Although α1‐AT‐trypsin, α1‐AT‐elastase and the pentapeptide FVYLI, the minimal binding sequence for the SEC receptor, increased [ 125 I]α1‐AT binding, in long term experiments these complexes failed to influence the number of α1‐AT binding sites. Specific, saturable binding of [ 125 I]α1‐AT was also found on the human intestinal epithelial Caco 2 cells, but not on fibroblast or leukaemic cell lines. Conclusion: These experiments demonstrate a specific, high affinity binding site for native α1‐AT on HepG 2 and Caco 2 cells, cell lines derived from tissues involved in the acute phase response.

Pancreatic elastase

Dissociation constant

10.1034/j.1600-0676.2000.020003240.x

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Citations (1)

Impact of D181V and A69T on the function of ferroportin as an iron export pump and hepcidin receptor

Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease (2014)

Roman Praschberger Melanie Schranz William J. Griffiths Nadja Baumgartner Martin Hermann

Ferroportin

Transferrin receptor

Loss function

10.1016/j.bbadis.2014.05.011

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Citations (20)