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Cells
Special Issues
Hemoglobin and Other Globin Types: Structure, Function and Evolution
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Hemoglobin and Other Globin Types: Structure, Function and Evolution

A special issue of Cells (ISSN 2073-4409). This special issue belongs to the section "Cellular Biophysics".

Deadline for manuscript submissions: closed (10 April 2024) | Viewed by 3806

Special Issue Editors

Prof. Dr. David Hoogewijs

E-Mail Website
Guest Editor
Section of Medicine, Department of Endocrinology, Metabolism and Cardiovascular System, University of Fribourg, Fribourg, Switzerland
Interests: hemoglobin; cytoglobin; androglobin; oxygen; hypoxia; gene regulation; HIF; EPO
Dr. Luc Moens

E-Mail Website
Guest Editor
Department of Biomedical Sciences, University of Antwerp, Antwerp, Belgium
Interests: hemoglobin; neuroglobin; globin evolution

Special Issue Information

Dear Colleagues,

Globins are indisputably among the most studied proteins. Globins are heme-proteins, involved in different cellular functions via their reversible binding capacity to gaseous ligands and their storage, transport, and detoxification. Historically, the familiar vertebrate O2-binding hemoglobin and myoglobin were among the first proteins whose sequences and structures were determined over 60 years ago. Most known globins fulfil respiratory functions, supplying the cell with adequate amounts of O2 for aerobic energy production via the respiratory chain in the mitochondria. However, over the last two decades, evidence has accrued indicating that globins exhibit further novel functions as enzymes, sensors, and signalling molecules. In parallel, the post-genomic era also revealed the existence of several additional globin types including chimeric variants.

In this Special Issue, we welcome original research and review articles demonstrating the functional diversity of globins throughout all taxa. We specifically solicit contributions on novel functional, evolutionary, and structural aspects of globins, illustrating the physiological versatility of this protein superfamily.

Prof. Dr. David Hoogewijs
Dr. Luc Moens
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 submissions that pass pre-check are 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. Cells is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2700 CHF (Swiss Francs). 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

  • hemoglobin
  • myoglobin
  • cytoglobin
  • neuroglobin
  • androglobin
  • globin-coupled sensor
  • truncated globin
  • flavohemoglobin
  • oxygen

Published Papers (3 papers)

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Research

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16 pages, 2390 KiB  
Article
Ectopic MYBL2-Mediated Regulation of Androglobin Gene Expression
by Antonia Herwig, Carina Osterhof, Anna Keppner, Darko Maric, Teng Wei Koay, Ambre Mbemba-Nsungi and David Hoogewijs
Cells 2024, 13(10), 826; https://doi.org/10.3390/cells13100826 - 11 May 2024
Viewed by 783
Abstract
Androglobin (ADGB) is a highly conserved and recently identified member of the globin superfamily. Although previous studies revealed a link to ciliogenesis and an involvement in murine spermatogenesis, its physiological function remains mostly unknown. Apart from FOXJ1-dependent regulation, the transcriptional landscape of the [...] Read more.
Androglobin (ADGB) is a highly conserved and recently identified member of the globin superfamily. Although previous studies revealed a link to ciliogenesis and an involvement in murine spermatogenesis, its physiological function remains mostly unknown. Apart from FOXJ1-dependent regulation, the transcriptional landscape of the ADGB gene remains unexplored. We, therefore, aimed to obtain further insights into regulatory mechanisms governing ADGB expression. To this end, changes in ADGB promoter activity were examined using luciferase reporter gene assays in the presence of a set of more than 475 different exogenous transcription factors. MYBL2 and PITX2 resulted in the most pronounced increase in ADGB promoter-dependent luciferase activity. Subsequent truncation strategies of the ADGB promoter fragment narrowed down the potential MYBL2 and PITX2 binding sites within the proximal ADGB promoter. Furthermore, MYBL2 binding sites on the ADGB promoter were further validated via a guide RNA-mediated interference strategy using reporter assays. Chromatin immunoprecipitation (ChIP)-qPCR experiments illustrated enrichment of the endogenous ADGB promoter region upon MYBL2 and PITX2 overexpression. Consistently, ectopic MYBL2 expression induced endogenous ADGB mRNA levels. Collectively, our data indicate that ADGB is strongly regulated at the transcriptional level and might have functions beyond ciliogenesis. Full article
(This article belongs to the Special Issue Hemoglobin and Other Globin Types: Structure, Function and Evolution)
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12 pages, 2922 KiB  
Article
Change in Osmotic Pressure Influences the Absorption Spectrum of Hemoglobin inside Red Blood Cells
by Miroslav Karabaliev, Bilyana Tacheva, Boyana Paarvanova and Radostina Georgieva
Cells 2024, 13(7), 589; https://doi.org/10.3390/cells13070589 - 28 Mar 2024
Viewed by 880
Abstract
Absorption spectra of red blood cell (RBC) suspensions are investigated in an osmolarity range in the medium from 200 mOsm to 900 mOsm. Three spectral parameters are used to characterize the process of swelling or shrinkage of RBC—the absorbance at 700 nm, the [...] Read more.
Absorption spectra of red blood cell (RBC) suspensions are investigated in an osmolarity range in the medium from 200 mOsm to 900 mOsm. Three spectral parameters are used to characterize the process of swelling or shrinkage of RBC—the absorbance at 700 nm, the Soret peak height relative to the spectrum background, and the Soret peak wavelength. We show that with an increase in the osmolarity, the absorbance at 700 nm increases and the Soret peak relative height decreases. These changes are related to the changes in the RBC volume and the resulting increase in the hemoglobin intracellular concentration and index of refraction. Confocal microscopy and flow cytometry measurements supported these conclusions. The maximum wavelength of the Soret peak increases with increasing osmolarity due to changes in the oxygenation state of hemoglobin. Using these spectrum parameters, the process of osmosis in RBCs can be followed in real time, but it can also be applied to various processes, leading to changes in the volume and shape of RBCs. Therefore, we conclude that UV–Vis absorption spectrophotometry offers a convenient, easily accessible, and cost-effective method to monitor changes in RBC, which can find applications in the field of drug discovery and diagnostics of RBC and hemoglobin disorders. Full article
(This article belongs to the Special Issue Hemoglobin and Other Globin Types: Structure, Function and Evolution)
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Review

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28 pages, 2332 KiB  
Review
Myoglobin in Brown Adipose Tissue: A Multifaceted Player in Thermogenesis
by Mostafa A. Aboouf, Thomas A. Gorr, Nadia M. Hamdy, Max Gassmann and Markus Thiersch
Cells 2023, 12(18), 2240; https://doi.org/10.3390/cells12182240 - 8 Sep 2023
Cited by 4 | Viewed by 1645
Abstract
Brown adipose tissue (BAT) plays an important role in energy homeostasis by generating heat from chemical energy via uncoupled oxidative phosphorylation. Besides its high mitochondrial content and its exclusive expression of the uncoupling protein 1, another key feature of BAT is the high [...] Read more.
Brown adipose tissue (BAT) plays an important role in energy homeostasis by generating heat from chemical energy via uncoupled oxidative phosphorylation. Besides its high mitochondrial content and its exclusive expression of the uncoupling protein 1, another key feature of BAT is the high expression of myoglobin (MB), a heme-containing protein that typically binds oxygen, thereby facilitating the diffusion of the gas from cell membranes to mitochondria of muscle cells. In addition, MB also modulates nitric oxide (NO•) pools and can bind C16 and C18 fatty acids, which indicates a role in lipid metabolism. Recent studies in humans and mice implicated MB present in BAT in the regulation of lipid droplet morphology and fatty acid shuttling and composition, as well as mitochondrial oxidative metabolism. These functions suggest that MB plays an essential role in BAT energy metabolism and thermogenesis. In this review, we will discuss in detail the possible physiological roles played by MB in BAT thermogenesis along with the potential underlying molecular mechanisms and focus on the question of how BAT–MB expression is regulated and, in turn, how this globin regulates mitochondrial, lipid, and NO• metabolism. Finally, we present potential MB-mediated approaches to augment energy metabolism, which ultimately could help tackle different metabolic disorders. Full article
(This article belongs to the Special Issue Hemoglobin and Other Globin Types: Structure, Function and Evolution)
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