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Glycobiology: The New Discoveries, Approaches, and Technical Developments
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Glycobiology: The New Discoveries, Approaches, and Technical Developments

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

Deadline for manuscript submissions: 31 May 2024 | Viewed by 2534

Special Issue Editor

Dr. Sanja Dabelić

E-Mail Website
Guest Editor
Department of Biochemistry and Molecular Biology, Faculty of Pharmacy and Biochemistry, University of Zagreb, A. Kovacica 1, 10000 Zagreb, Croatia
Interests: glycobiology

Special Issue Information

Dear Colleagues,

Over the last few decades, our understanding of structure and function of carbohydrate has undergone an incredible transformation. From being considered molecules whose role is strictly energetical or structural, glycans are now recognized as complex and diverse structures involved in, and even crucial to, numerous biological processes. Given that the techniques and interest for investigating the structure, presence, and functions of glycans are progressing more and more, it is expected that we will, in the years ahead, discover many more of their roles—some "sweet or desirable", others "bitter or fatal". The growing field of glycobiology has a great impact, not only on our understanding of biological processes, but also on our potential to modulate them. This open access Special Issue will bring together original research and review articles on various aspects of glycobiology, highlighting new discoveries, approaches, and technical developments. The main focus of this issue is sharing significant works that advance our understanding of glycans’ roles and their impact on the structure and function of individual molecules, materials, cells, tissues, and organisms, as well as on the interplay between them.

This Special Issue welcomes original research papers, as well as critical or comprehensive reviews, that demonstrate or summarize significant advances in the glycobiology field. 

Topics include, but are not limited to:

  • Novel tools and strategies for the analysis/synthesis/modulation of glycoconjugates.
  • Glycan structure, function, and biosynthesis.
  • Glycan-recognizing molecules.
  • Glycan structural and functional diversity across biological taxa.
  • Genetic basis of glycobiology.
  • Glycans in physiology, disorders, and diseases.
  • Carbohydrates in pharmacy, medicine, biotechnology, materials sciences and nanotechnology.

Dr. Sanja Dabelić
Guest Editor

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. 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

  • glycans
  • lectins
  • glycoconjugates
  • glycosylation
  • genetic disorders of glycosylation
  • glycomics and glycoproteomics

Published Papers (3 papers)

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Research

12 pages, 2368 KiB  
Article
Glycosylation and Characterization of Human Transferrin in an End-Stage Kidney Disease
by Goran Miljuš, Ana Penezić, Lucia Pažitná, Nikola Gligorijević, Marko Baralić, Aleksandra Vilotić, Miloš Šunderić, Dragana Robajac, Zorana Dobrijević, Jaroslav Katrlík and Olgica Nedić
Int. J. Mol. Sci. 2024, 25(9), 4625; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms25094625 - 24 Apr 2024
Viewed by 294
Abstract
Chronic kidney disease (CKD) is a global health concern affecting approximately one billion individuals worldwide. End-stage kidney disease (ESKD), the most severe form of CKD, is often accompanied by anemia. Peritoneal dialysis (PD), a common treatment for ESKD, utilizes the peritoneum for solute [...] Read more.
Chronic kidney disease (CKD) is a global health concern affecting approximately one billion individuals worldwide. End-stage kidney disease (ESKD), the most severe form of CKD, is often accompanied by anemia. Peritoneal dialysis (PD), a common treatment for ESKD, utilizes the peritoneum for solute transfer but is associated with complications including protein loss, including transferrin (Tf) a key protein involved in iron transport. This study investigated Tf characteristics in ESKD patients compared to healthy individuals using lectin microarray, spectroscopic techniques and immunocytochemical analysis to assess Tf interaction with transferrin receptors (TfRs). ESKD patients exhibited altered Tf glycosylation patterns, evidenced by significant changes in lectin reactivity compared to healthy controls. However, structural analyses revealed no significant differences in the Tf secondary or tertiary structures between the two groups. A functional analysis demonstrated comparable Tf-TfR interaction in both PD and healthy samples. Despite significant alterations in Tf glycosylation, structural integrity and Tf-TfR interaction remained preserved in PD patients. These findings suggest that while glycosylation changes may influence iron metabolism, they do not impair Tf function. The study highlights the importance of a glucose-free dialysis solutions in managing anemia exacerbation in PD patients with poorly controlled anemia, potentially offering a targeted therapeutic approach to improve patient outcomes. Full article
(This article belongs to the Special Issue Glycobiology: The New Discoveries, Approaches, and Technical Developments)
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14 pages, 1778 KiB  
Article
Label-Free Liquid Chromatography–Mass Spectrometry Quantitation of Relative N- and O-Glycan Concentrations in Human Milk in Japan
by Toshiyuki Yamaguchi, Hirofumi Fukudome, Junichi Higuchi, Tomoki Takahashi, Yuta Tsujimori, Hiroshi M. Ueno, Yasuhiro Toba and Fumihiko Sakai
Int. J. Mol. Sci. 2024, 25(3), 1772; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms25031772 - 01 Feb 2024
Viewed by 781
Abstract
Human milk is abundant in carbohydrates and includes human milk oligosaccharides (HMOs) and N/O-glycans conjugated to proteins. HMO compositions and concentrations vary in individuals according to the maternal secretor status based on the fucosyltransferase 2 genotype; however, the profile of [...] Read more.
Human milk is abundant in carbohydrates and includes human milk oligosaccharides (HMOs) and N/O-glycans conjugated to proteins. HMO compositions and concentrations vary in individuals according to the maternal secretor status based on the fucosyltransferase 2 genotype; however, the profile of N/O-glycans remains uninvestigated because of the analytical complexity. Herein, we applied a label-free chromatography–mass spectrometry (LC–MS) technique to elucidate the variation in the composition and concentration of N/O-glycans in human milk. We used label-free LC–MS to relatively quantify 16 N-glycans and 12 O-glycans in 200 samples of Japanese human milk (1–2 months postpartum) and applied high performance anion exchange chromatography with pulsed amperometric detection to absolutely quantify the concentrations of 11 representative HMOs. Cluster analysis of the quantitative data revealed that O-glycans and several HMOs were classified according to the presence or absence of fucose linked to galactose while N-glycans were classified into a different group from O-glycans and HMOs. O-glycans and HMOs with fucose linked to galactose were more abundant in human milk from secretor mothers than from nonsecretor mothers. Thus, secretor status influenced the composition and concentration of HMOs and O-glycans but not those of N-glycans in human milk. Full article
(This article belongs to the Special Issue Glycobiology: The New Discoveries, Approaches, and Technical Developments)
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16 pages, 6669 KiB  
Article
Sialyltransferase Mutations Alter the Expression of Calcium-Binding Interneurons in Mice Neocortex, Hippocampus and Striatum
by Senka Blažetić, Vinko Krajina, Irena Labak, Barbara Viljetić, Valentina Pavić, Vedrana Ivić, Marta Balog, Ronald L. Schnaar and Marija Heffer
Int. J. Mol. Sci. 2023, 24(24), 17218; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms242417218 - 07 Dec 2023
Viewed by 756
Abstract
Gangliosides are major glycans on vertebrate nerve cells, and their metabolic disruption results in congenital disorders with marked cognitive and motor deficits. The sialyltransferase gene St3gal2 is responsible for terminal sialylation of two prominent brain gangliosides in mammals, GD1a and GT1b. In this [...] Read more.
Gangliosides are major glycans on vertebrate nerve cells, and their metabolic disruption results in congenital disorders with marked cognitive and motor deficits. The sialyltransferase gene St3gal2 is responsible for terminal sialylation of two prominent brain gangliosides in mammals, GD1a and GT1b. In this study, we analyzed the expression of calcium-binding interneurons in primary sensory (somatic, visual, and auditory) and motor areas of the neocortex, hippocampus, and striatum of St3gal2-null mice as well as St3gal3-null and St3gal2/3-double null. Immunohistochemistry with highly specific primary antibodies for GABA, parvalbumin, calretinin, and calbindin were used for interneuron detection. St3gal2-null mice had decreased expression of all three analyzed types of calcium-binding interneurons in all analyzed regions of the neocortex. These results implicate gangliosides GD1a and GT1b in the process of interneuron migration and maturation. Full article
(This article belongs to the Special Issue Glycobiology: The New Discoveries, Approaches, and Technical Developments)
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