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Glycobiology in Human Health and Disease
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Glycobiology in Human Health and Disease

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

Deadline for manuscript submissions: 20 February 2025 | Viewed by 3498

Special Issue Editor

Dr. Katrin Mani

E-Mail Website
Guest Editor
Department of Experimental Medical Science, Glycobiology Group, Lund University, Biomedical Center A13, SE-221 84 Lund, Sweden
Interests: glycobiology; glypicans; cancer

Special Issue Information

Dear Colleagues,

Glycobiology, the study of carbohydrates and their interactions with proteins and other molecules, holds immense promise in unraveling the intricate mechanisms underlying human health and disease. Glycoconjugates play pivotal roles in cellular recognition, signaling, and immune response modulation, making these molecules essential players in numerous physiological and pathological processes.

Understanding the complex interplay between glycans, glycoproteins, and glycolipids with other molecules and unraveling their impact on cellular function is crucial for elucidating the molecular basis of various diseases, including cancer, neurodegenerative disorders, infectious diseases, and metabolic disorders, among many other diseases. Glycobiology research offers unique insights into disease mechanisms, biomarker discovery, and therapeutic targeting, paving the way for novel diagnostic and therapeutic strategies.

Moreover, advances in glycobiology have far-reaching implications for personalized medicine, drug development, and precision therapeutics. Deciphering the glycome's intricate language would reveal disease-specific glycan signatures, leading to the development of targeted interventions and precision medicine approaches tailored to individual patients.

This Special Issue on Glycobiology in Human Health and Disease provides a platform to report the latest findings, innovative methodologies, and translational insights in glycobiology. This Special Issue aims to accelerate progress toward unraveling the complexities of glycobiology and translating discoveries into clinical applications for improved human health.

Dr. Katrin Mani
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 and glycoconjugates
  • glycoproteins
  • proteoglycans
  • glycolipids
  • glycosylation including glycosyltransferases and glycosidases
  • carbohydrate and glycan metabolism
  • glycan structure
  • disease biomarkers
  • glycan signaling
  • glycoimmunology
  • glycomics

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Published Papers (3 papers)

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10 pages, 3156 KiB  
Article
Elucidating the Antiglycation Effect of Creatine on Methylglyoxal-Induced Carbonyl Stress In Vitro
by Shin Koike, Haruka Mitsuhashi, Atsushi Kishida and Yuki Ogasawara
Int. J. Mol. Sci. 2024, 25(20), 10880; https://doi.org/10.3390/ijms252010880 - 10 Oct 2024
Viewed by 802
Abstract
Advanced glycation end products (AGEs) with multiple structures are formed at the sites where carbonyl groups of reducing sugars bind to free amino groups of proteins through the Maillard reaction. In recent years, it has been highlighted that the accumulation of AGEs, which [...] Read more.
Advanced glycation end products (AGEs) with multiple structures are formed at the sites where carbonyl groups of reducing sugars bind to free amino groups of proteins through the Maillard reaction. In recent years, it has been highlighted that the accumulation of AGEs, which are generated when carbonyl compounds produced in the process of sugar metabolism react with proteins, is involved in various diseases. Creatine is a biocomponent that is homeostatically present throughout the body and is known to react nonenzymatically with α-dicarbonyl compounds. This study evaluated the antiglycation potential of creatine against methylglyoxal (MGO), a glucose metabolite that induces carbonyl stress with formation of AGEs in vitro. Further, to elucidate the mechanism of the cytoprotective action of creatine, its effect on the accumulation of carbonyl proteins in the cells and the MGO-induced cellular damage were investigated using neuroblastoma cells. The results revealed that creatine significantly inhibits protein carbonylation by directly reacting with MGO, and creatine added to the culture medium suppressed MGO-derived carbonylation of intracellular proteins and exerted a protective effect on MGO-induced cytotoxicity. These findings suggest that endogenous and supplemented creatine may contribute to the attenuation of carbonyl stress in vivo. Full article
(This article belongs to the Special Issue Glycobiology in Human Health and Disease)
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Review

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19 pages, 1020 KiB  
Review
Fucosidosis: A Review of a Rare Disease
by Burcu Pekdemir, Mikhael Bechelany and Sercan Karav
Int. J. Mol. Sci. 2025, 26(1), 353; https://doi.org/10.3390/ijms26010353 - 3 Jan 2025
Viewed by 394
Abstract
Fucosidosis is a rare lysosomal storage disease caused by α-L-fucosidase deficiency following a mutation in the FUCA1 gene. This enzyme is responsible for breaking down fucose-containing glycoproteins, glycolipids, and oligosaccharides within the lysosome. Mutations in FUCA1 result in either reduced enzyme activity or [...] Read more.
Fucosidosis is a rare lysosomal storage disease caused by α-L-fucosidase deficiency following a mutation in the FUCA1 gene. This enzyme is responsible for breaking down fucose-containing glycoproteins, glycolipids, and oligosaccharides within the lysosome. Mutations in FUCA1 result in either reduced enzyme activity or complete loss of function, leading to the accumulation of fucose-rich substrates in lysosomes. Lysosomes become engorged with undigested substrates, which leads to secondary storage defects affecting other metabolic pathways. The central nervous system is particularly vulnerable, with lysosomal dysfunction causing microglial activation, inflammation, and neuronal loss, leading to the neurodegenerative symptoms of fucosidosis. Neuroinflammation contributes to secondary damage, including neuronal apoptosis, axonal degeneration, and synaptic dysfunction, exacerbating the disease process. Chronic neuroinflammation impairs synaptic plasticity and neuronal survival, leading to progressive intellectual disability, learning difficulties, and loss of previously acquired skills. Inflammatory cytokines and lysosomal burden in motor neurons and associated pathways contribute to ataxia, spasticity, and hypotonia, which are common motor symptoms in fucosidosis. Elevated neuroinflammatory markers can increase neuronal excitability, leading to the frequent occurrence of epilepsy in affected individuals. So, fucosidosis is characterized by rapid mental and motor loss, along with growth retardation, coarse facial features, hepatosplenomegaly, telangiectasis or angiokeratomas, epilepsy, inguinal hernia, and dysostosis multiplex. Patients usually die at an early age. Treatment of fucosidosis is a great challenge, and there is currently no definitive effective treatment. Hematopoietic cell transplantation studies are ongoing in the treatment of fucosidosis. However, early diagnosis of this disease and treatment can be effective. In addition, the body’s immune system decreases due to chemotherapy applied after transplantation, leaving the body vulnerable to microbes and infections, and the risk of death is high with this treatment. In another treatment method, gene therapy, the use of retroviral vectors, is promising due to their easy integration, high cell efficiency, and safety. In another treatment approach, enzyme replacement therapy, preclinical studies are ongoing for fucosidosis, but the blood–brain barrier is a major obstacle in lysosomal storage diseases affecting the central nervous system. Early diagnosis is important in fucosidosis, a rare disease, due to the delay in the diagnosis of patients identified so far and the rapid progression of the disease. In addition, enzyme replacement therapy, which carries fewer risks, is promising. Full article
(This article belongs to the Special Issue Glycobiology in Human Health and Disease)
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35 pages, 5001 KiB  
Review
Mechanistic and Therapeutic Implications of Protein and Lipid Sialylation in Human Diseases
by Xiaotian Zhong, Aaron M. D’Antona and Jason C. Rouse
Int. J. Mol. Sci. 2024, 25(22), 11962; https://doi.org/10.3390/ijms252211962 - 7 Nov 2024
Viewed by 1695
Abstract
Glycan structures of glycoproteins and glycolipids on the surface glycocalyx and luminal sugar layers of intracellular membrane compartments in human cells constitute a key interface between intracellular biological processes and external environments. Sialic acids, a class of alpha-keto acid sugars with a nine-carbon [...] Read more.
Glycan structures of glycoproteins and glycolipids on the surface glycocalyx and luminal sugar layers of intracellular membrane compartments in human cells constitute a key interface between intracellular biological processes and external environments. Sialic acids, a class of alpha-keto acid sugars with a nine-carbon backbone, are frequently found as the terminal residues of these glycoconjugates, forming the critical components of these sugar layers. Changes in the status and content of cellular sialic acids are closely linked to many human diseases such as cancer, cardiovascular, neurological, inflammatory, infectious, and lysosomal storage diseases. The molecular machineries responsible for the biosynthesis of the sialylated glycans, along with their biological interacting partners, are important therapeutic strategies and targets for drug development. The purpose of this article is to comprehensively review the recent literature and provide new scientific insights into the mechanisms and therapeutic implications of sialylation in glycoproteins and glycolipids across various human diseases. Recent advances in the clinical developments of sialic acid-related therapies are also summarized and discussed. Full article
(This article belongs to the Special Issue Glycobiology in Human Health and Disease)
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