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Special Issue "Ferroportin and Ceruloplasmin: Structure and Function in Health and Disease"

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Pathology, Diagnostics, and Therapeutics".

Deadline for manuscript submissions: 31 December 2020.

Special Issue Editors

Dr. Giovanni Musci
Website
Guest Editor
Dipartimento di Bioscienze e Territorio, Università del Molise, Pesche (IS), Italy
Interests: iron homeostasis; ceruloplasmin; ferroportin; copper; metalloproteins; lactoferrin; inflammation; structural biology
Dr. Maria Carmela Bonaccorsi Di Patti
Website
Guest Editor
Dipartimento di Scienze biochimiche ‘A. Rossi Fanelli’ Università degli Studi di Roma La Sapienza, Rome, Italy
Interests: iron; copper; multicopper oxidase; ceruloplasmin; ferroportin; lactoferrin; neurodegeneration; oxidative stress; yeast; membrane proteins

Special Issue Information

Dear Colleagues,

In the last years, our understanding of the role of proteins involved in the handling of iron in health and disease had tremendously advanced  due to the efforts of many research groups around the world. Two proteins playing a key role in the cellular management of iron are ferroportin, the only known cellular iron exporter in mammals, and ceruloplasmin, a multifunctional enzyme with ferroxidase activity. A strong connection between ferroportin and ceruloplasmin was uncovered and they can be viewed as a system of functionally interacting partners. The importance of both proteins is underscored by the finding that mutations in each cause iron imbalance leading to pathological states, particularly severe in the case of aceruloplasminemia which belongs to the neurodegeneration with brain iron accumulation (NBIA) group.

This Special Issue of IJMS will focus on recent advances regarding different aspects of ferroportin and ceruloplasmin biology in health and disease: molecular structure and mechanism of action, regulation of expression, interactions with other proteins, exploitation as drug targets, and roles in other pathological states where iron status is altered (e.g., infection and inflammation, cancer, etc.). Original papers and review articles on these and related topics are welcome.

Dr. Giovanni Musci
Dr. Maria Carmela Bonaccorsi Di Patti
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All papers will be peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. There is an Article Processing Charge (APC) for publication in this open access journal. For details about the APC please see here. Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • ferroportin
  • ceruloplasmin
  • iron
  • copper
  • neurodegeneration

Published Papers (1 paper)

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Research

Open AccessArticle
Dynamical Behavior of the Human Ferroportin Homologue from Bdellovibrio bacteriovorus: Insight into the Ligand Recognition Mechanism
Int. J. Mol. Sci. 2020, 21(18), 6785; https://doi.org/10.3390/ijms21186785 - 16 Sep 2020
Abstract
Members of the major facilitator superfamily of transporters (MFS) play an essential role in many physiological processes such as development, neurotransmission, and signaling. Aberrant functions of MFS proteins are associated with several diseases, including cancer, schizophrenia, epilepsy, amyotrophic lateral sclerosis and Alzheimer’s disease. [...] Read more.
Members of the major facilitator superfamily of transporters (MFS) play an essential role in many physiological processes such as development, neurotransmission, and signaling. Aberrant functions of MFS proteins are associated with several diseases, including cancer, schizophrenia, epilepsy, amyotrophic lateral sclerosis and Alzheimer’s disease. MFS transporters are also involved in multidrug resistance in bacteria and fungi. The structures of most MFS members, especially those of members with significant physiological relevance, are yet to be solved. The lack of structural and functional information impedes our detailed understanding, and thus the pharmacological targeting, of these transporters. To improve our knowledge on the mechanistic principles governing the function of MSF members, molecular dynamics (MD) simulations were performed on the inward-facing and outward-facing crystal structures of the human ferroportin homologue from the Gram-negative bacterium Bdellovibrio bacteriovorus (BdFpn). Several simulations with an excess of iron ions were also performed to explore the relationship between the protein’s dynamics and the ligand recognition mechanism. The results reinforce the existence of the alternating-access mechanism already described for other MFS members. In addition, the reorganization of salt bridges, some of which are conserved in several MFS members, appears to be a key molecular event facilitating the conformational change of the transporter. Full article
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Planned Papers

The below list represents only planned manuscripts. Some of these manuscripts have not been received by the Editorial Office yet. Papers submitted to MDPI journals are subject to peer-review.

Title: Hepcidin-ferroportin interaction controls systemic iron homeostasis
Authors: Elizabeta N.;Tomas G.


Title: Role of the hepcidin-ferroportin axis in the control of local iron availability in the tissue microenvironment

Authors: Gaetano C. et.al.

Abstract: Body iron levels are regulated by hepcidin, a liver-derived peptide that exerts its function by controlling the presence on the cell surface of ferroportin (FPN), the sole cellular iron exporter. Hepcidin  binding leads to FPN internalization and degradation, thereby inhibiting iron release, in particular from iron absorbing duodenal cells and macrophages involved in iron recycling. Disruption in this regulatory  mechanism results in a variety of disorders associated with iron-deficiency or overload. Over recent years, increasing evidence has emerged to indicate that, in addition to its role in systemic iron  metabolism, FPN may play an important function in local iron control, so that its dysregulation may lead to tissue damage despite unaltered systemic iron homeostasis.

Title:Oral ferroportin inhibitor improves erythropiesis without interfering with iron chelation therapy in a model of b-thalassemia

Authors: Franz D. et.al

 

 
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