Advances in Galectins

A special issue of Biomolecules (ISSN 2218-273X). This special issue belongs to the section "Biomacromolecules: Proteins".

Deadline for manuscript submissions: 31 December 2024 | Viewed by 1544

Special Issue Editors


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Guest Editor
Brigham and Women's Hospital, 77 Avenue Louis Pasteur, New Research Building 652, Boston, MA 02115, USA
Interests: glycoimmunology; galectins; lectin-microbiome interactions

E-Mail Website
Guest Editor
Microbiology, Tumor and Cell Biology, Karolinska Institutet, Biomedicum C8, Solnavägen 9, 171 65 Solna, Sweden
Interests: glycoimmunology; galectins; host-pathogen interaction

Special Issue Information

Dear Colleagues,

Galectins, an ancient family of carbohydrate-binding proteins, have emerged as key players in various biological processes, making this a rapidly evolving field of research. This Special Issue aims to bring together cutting-edge research on recent advances in galectin biology. We invite authors to contribute original research articles, reviews, and perspectives on the multifaceted aspects of galectin research.

Potential topics in the Special Issue include, but are not limited to, the following:

  1. Galectin structure and function.
  2. Galectin-mediated cellular signaling networks.
  3. Immunomodulatory roles of galectins.
  4. Galectins in cancer biology and therapy.
  5. Galectins and their involvement in inflammatory processes.
  6. Neurobiology and galectins.
  7. Galectins as regulators and mediators of metabolic signaling.
  8. Galectins in development, tissue regeneration, and repair.
  9. Galectin–microbe interactions.
  10. Galectins in autoimmune diseases.
  11. Epigenetic regulation of galectins.
  12. Diagnostic and prognostic potential of galectins as biomarkers.
  13. Multidisciplinary approaches that combine galectin biology with other fields such as bioinformatics, genomics, and proteomics.
  14. Evolutionary perspectives on galectins.
  15. Galectin-based interventions in clinical research.

We encourage article submissions from researchers working at the forefront of galectin research. Your contributions will advance our understanding of galectins and their potential applications in improving human health.

Dr. Anu Paul
Dr. Diyoly Ayona
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. Biomolecules is an international peer-reviewed open access monthly 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

  • galectins
  • carbohydrate-binding proteins
  • galectin–microbe

Published Papers (1 paper)

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Research

12 pages, 1545 KiB  
Article
Reduced form of Galectin-1 Suppresses Osteoclastic Differentiation of Human Peripheral Blood Mononuclear Cells and Murine RAW264 Cells In Vitro
by Tomoharu Takeuchi, Midori Oyama, Mayumi Tamura, Yoichiro Arata and Tomomi Hatanaka
Biomolecules 2024, 14(1), 121; https://doi.org/10.3390/biom14010121 - 17 Jan 2024
Viewed by 1160
Abstract
Galectin-1 (Gal-1) is an evolutionarily conserved sugar-binding protein found in intra- and extracellular spaces. Extracellularly, it binds to glycoconjugates with β-galactoside(s) and functions in various biological phenomena, including immunity, cancer, and differentiation. Under extracellular oxidative conditions, Gal-1 undergoes oxidative inactivation, losing its sugar-binding [...] Read more.
Galectin-1 (Gal-1) is an evolutionarily conserved sugar-binding protein found in intra- and extracellular spaces. Extracellularly, it binds to glycoconjugates with β-galactoside(s) and functions in various biological phenomena, including immunity, cancer, and differentiation. Under extracellular oxidative conditions, Gal-1 undergoes oxidative inactivation, losing its sugar-binding ability, although it exhibits sugar-independent functions. An age-related decrease in serum Gal-1 levels correlates with decreasing bone mass, and Gal-1 knockout promotes osteoclastic bone resorption and suppresses bone formation. However, the effect of extracellular Gal-1 on osteoclast differentiation remains unclear. Herein, we investigated the effects of extracellular Gal-1 on osteoclastogenesis in human peripheral blood mononuclear cells (PBMCs) and mouse macrophage RAW264 cells. Recombinant Gal-1 suppressed the macrophage colony-stimulating factor and receptor activator of nuclear factor-κB ligand-dependent osteoclast formation, actin ring formation, and bone-resorption activity of human PBMCs. Similar results were obtained for RAW264 cells. Gal-1 knockdown increased osteoclast-like cell formation, suggesting that it affected differentiation in an autocrine-like manner. Oxidized Gal-1 slightly affected differentiation, and in the presence of lactose, the differentiation inhibitory effect of galectin-1 was not observed. These findings suggest that extracellular Gal-1 inhibits osteoclast differentiation in a β-galactoside-dependent manner, and an age-related decrease in serum Gal-1 levels may contribute to reduced osteoclast activity and decreasing bone mass. Full article
(This article belongs to the Special Issue Advances in Galectins)
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