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Vitamin D and Vitamin D Binding Protein in Health and Disease 3.0

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Macromolecules".

Deadline for manuscript submissions: 10 June 2024 | Viewed by 1386

Special Issue Editor

Special Issue Information

Dear Colleagues,

Vitamin D functions in the human body through both an endocrine and an autocrine mechanism. Nearly all circulating vitamin D (~85–90%) circulates bound to vitamin D-binding protein (DBP), with a smaller proportion bound to albumin, leaving <5% circulating freely. DBP is a multifunctional protein that has attracted increasing interest in recent years. DBP may also play roles beyond vitamin D binding, with potential roles in the immune system and elsewhere. The consequences of low 25(OH)D status include increased risk of various chronic diseases, ranging from hypertension to diabetes to cancer and infections. Also, the DBP polymorphism with more than 120 variants has been linked to several diseases. Despite the enormous progress in the deciphering of the structure of DBP and its function, there remains an impressive list of major research questions. In this special issue, we welcome original papers and review articles, which focus on the role of vitamin and DBP in health and disease.

More published papers can be found in the closed special issue:
Vitamin D and Vitamin D Binding Protein in Health and Disease;
Vitamin D and Vitamin D Binding Protein in Health and Disease 2.0.

Prof. Dr. Marijn Speeckaert
Guest Editor

Manuscript Submission Information

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Keywords

  • vitamin D
  • vitamin D binding protein (gc-globulin)
  • vitamin D receptor
  • vitamin D deficiency
  • immunomodulation
  • chronic inflammatory diseases
  • osteoporosis
  • vitamin D deficiency

Published Papers (1 paper)

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Research

37 pages, 8919 KiB  
Article
The Molecular Aspects of Functional Activity of Macrophage-Activating Factor GcMAF
by Svetlana S. Kirikovich, Evgeniy V. Levites, Anastasia S. Proskurina, Genrikh S. Ritter, Sergey E. Peltek, Asya R. Vasilieva, Vera S. Ruzanova, Evgeniya V. Dolgova, Sofya G. Oshihmina, Alexandr V. Sysoev, Danil I. Koleno, Elena D. Danilenko, Oleg S. Taranov, Alexandr A. Ostanin, Elena R. Chernykh, Nikolay A. Kolchanov and Sergey S. Bogachev
Int. J. Mol. Sci. 2023, 24(24), 17396; https://doi.org/10.3390/ijms242417396 - 12 Dec 2023
Cited by 1 | Viewed by 900
Abstract
Group-specific component macrophage-activating factor (GcMAF) is the vitamin D3-binding protein (DBP) deglycosylated at Thr420. The protein is believed to exhibit a wide range of therapeutic properties associated with the activation of macrophagal immunity. An original method for GcMAF production, [...] Read more.
Group-specific component macrophage-activating factor (GcMAF) is the vitamin D3-binding protein (DBP) deglycosylated at Thr420. The protein is believed to exhibit a wide range of therapeutic properties associated with the activation of macrophagal immunity. An original method for GcMAF production, DBP conversion to GcMAF, and the analysis of the activating potency of GcMAF was developed in this study. Data unveiling the molecular causes of macrophage activation were obtained. GcMAF was found to interact with three CLEC10A derivatives having molecular weights of 29 kDa, 63 kDa, and 65 kDa. GcMAF interacts with high-molecular-weight derivatives via Ca2+-dependent receptor engagement. Binding to the 65 kDa or 63 kDa derivative determines the pro- and anti-inflammatory direction of cytokine mRNA expression: 65 kDa—pro-inflammatory (TNF-α, IL-1β) and 63 kDa—anti-inflammatory (TGF-β, IL-10). No Ca2+ ions are required for the interaction with the canonical 29 kDa CLEC10A. Both forms, DBP protein and GcMAF, bind to the 29 kDa CLEC10A. This interaction is characterized by the stochastic mRNA synthesis of the analyzed cytokines. Ex vivo experiments have demonstrated that when there is an excess of GcMAF ligand, CLEC10A forms aggregate, and the mRNA synthesis of analyzed cytokines is inhibited. A schematic diagram of the presumable mechanism of interaction between the CLEC10A derivatives and GcMAF is provided. The principles and elements of standardizing the GcMAF preparation are elaborated. Full article
(This article belongs to the Special Issue Vitamin D and Vitamin D Binding Protein in Health and Disease 3.0)
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