Search for Articles:
Title / Keyword
Author / Affiliation / Email
Journal
Article Type
 
 
Advanced Search
 
Section
Special Issue
Volume
Issue
Number
Page
 
7.8
3.9
Journals
Biomedicines
Special Issues
Role of Glycomics in Health and Diseases
share announcement

Role of Glycomics in Health and Diseases

A special issue of Biomedicines (ISSN 2227-9059). This special issue belongs to the section "Molecular and Translational Medicine".

Deadline for manuscript submissions: 30 September 2026 | Viewed by 13669

Special Issue Editor

Dr. Tijl Vermassen

E-Mail Website
Guest Editor
Department Medical Oncology, Ghent University Hospital, 9000 Ghent, Belgium
Interests: glycomics; protein chemistry; immunology; biomarker research
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

The human body and its physiology are characterized by a variety of complex processes and structures. One of these structures is glycans; these are complex carbohydrate molecules that are one of the four primary components of the cell (alongside DNA, proteins, and lipids).

The main functions of glycans are as follows: 1) structural and modulatory roles; 2) extrinsic (interspecies) recognition; 3) intrinsic (intraspecies) recognition; and 4) molecular mimicry of host glycans. Via these functions, carbohydrate structures play a fundamental role in almost every process in our body, e.g., the maintenance of tissue structure, protein trafficking, and ligand binding.

The field of glycome research is gaining more and more attention. The accumulation of aberrant glycan patterns has been demonstrated in various pathological conditions, such as liver diseases, immune-related disorders, nephropathy, and cancer development. Insights into how these changes occur in the glycan machinery remain scarce and further research on the matter is needed.

In this Special Issue, we aim to cover the most recent advances regarding glycomic research in both healthy and diseased states. The main focus will be on, but not limited to, the physiological role of the glycome in the human body, the pathophysiological processes of aberrant glycosylation in disease, the methodological approaches to assess glycan-related biomarkers, and the use of glycan patterns as potential biomarkers for disease diagnosis and risk stratification.

In this Special Issue, we welcome all types of papers (reviews, original papers, or perspective papers) on the aforementioned subject.

Dr. Tijl Vermassen
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 250 words) can be sent to the Editorial Office for assessment.

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. Biomedicines 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 2600 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

  • glycomics
  • protein chemistry
  • immunology
  • biomarker research

Benefits of Publishing in a Special Issue

  • Ease of navigation: Grouping papers by topic helps scholars navigate broad scope journals more efficiently.
  • Greater discoverability: Special Issues support the reach and impact of scientific research. Articles in Special Issues are more discoverable and cited more frequently.
  • Expansion of research network: Special Issues facilitate connections among authors, fostering scientific collaborations.
  • External promotion: Articles in Special Issues are often promoted through the journal's social media, increasing their visibility.
  • Reprint: MDPI Books provides the opportunity to republish successful Special Issues in book format, both online and in print.

Further information on MDPI's Special Issue policies can be found here.

Published Papers (4 papers)

Download All Papers
Order results
Result details
Show export options expand_more Show export options expand_less
Select all
Export citation of selected articles as:

Review

20 pages, 2031 KB  
Review
GalNAc-Transferases in Cancer
by Shruthi C. Iyer, Dinesh Kumar Srinivasan and Rajeev Parameswaran
Biomedicines 2026, 14(1), 5; https://doi.org/10.3390/biomedicines14010005 - 19 Dec 2025
Viewed by 1656
Abstract
Background/Objectives: The polypeptide N-acetylgalactosaminyltransferase (GALNT) family initiates mucin-type O-glycosylation, a post-translational modification that plays a pivotal role in cellular signaling, adhesion, and immune evasion. Dysregulated GALNT expression has been increasingly implicated in carcinogenesis. Methods: We reviewed the literature on the [...] Read more.
Background/Objectives: The polypeptide N-acetylgalactosaminyltransferase (GALNT) family initiates mucin-type O-glycosylation, a post-translational modification that plays a pivotal role in cellular signaling, adhesion, and immune evasion. Dysregulated GALNT expression has been increasingly implicated in carcinogenesis. Methods: We reviewed the literature on the expression, function, and clinical relevance of GALNT isoforms across various cancers, with a focus on their mechanistic roles, biomarker potential, and therapeutic implications. Results: Aberrant GALNT expression is observed in numerous malignancies, including breast, colorectal, gastric, lung, ovarian, and hepatocellular carcinomas. Isoforms such as GALNT1, -T2, -T3, and -T14 contribute to tumorigenesis by modulating the glycosylation of mucins such as Mucin-1 (MUC1), epithelial growth factor receptors (EGFR), and other signaling proteins. These alterations promote cancer cell proliferation, metastasis, epithelial–mesenchymal transition (EMT), and chemoresistance. Deranged GALNT expression is frequently associated with poor prognosis, and certain GALNT genotypes predict treatment response. However, functional redundancy among isoforms poses challenges for selective targeting. Conclusions: Despite their strong potential as modulators of cancer progression, GALNTs face substantial limitations in terms of substrate identification, mechanistic clarity, immune relevance, and therapeutic tractability. Overcoming these challenges requires advanced glycoproteomics, development of isoform-specific tools, and integrated studies across cancer and immunology to fully harness GALNT biology for clinical benefit. Full article
(This article belongs to the Special Issue Role of Glycomics in Health and Diseases)
►▼ Show Figures

Graphical abstract

25 pages, 1216 KB  
Review
Unlocking the Sugar Code: Implications and Consequences of Glycosylation in Alzheimer’s Disease and Other Tauopathies
by Andrei-Cristian Bondar, Marius P. Iordache, Mirela Coroescu, Anca Buliman, Elena Rusu, Magdalena Budișteanu and Cristiana Tanase
Biomedicines 2025, 13(12), 2884; https://doi.org/10.3390/biomedicines13122884 - 26 Nov 2025
Cited by 4 | Viewed by 1394
Abstract
Alzheimer’s disease (AD) is the most prevalent cause of dementia, characterized by progressive cognitive decline, amyloid-β (Aβ) plaques, and neurofibrillary tangles composed of hyperphosphorylated tau protein. Other tauopathies, including frontotemporal lobar degeneration (FTLD), progressive supranuclear palsy (PSP), and corticobasal degeneration (CBD) share pathological [...] Read more.
Alzheimer’s disease (AD) is the most prevalent cause of dementia, characterized by progressive cognitive decline, amyloid-β (Aβ) plaques, and neurofibrillary tangles composed of hyperphosphorylated tau protein. Other tauopathies, including frontotemporal lobar degeneration (FTLD), progressive supranuclear palsy (PSP), and corticobasal degeneration (CBD) share pathological hallmarks centered on abnormal tau biology. Increasing evidence highlights the role of post-translational modifications in modulating these pathogenic processes. Among these, glycosylation, the enzymatic attachment of glycans to proteins or lipids, has emerged as a critical regulator of protein folding, trafficking, aggregation, and clearance. Both N-linked glycosylation (N-glycosylation) and O-linked glycosylation (O-glycosylation) influence tau stability, Aβ processing, receptor signaling, synaptic integrity, and neuroinflammation. Dysregulated glycosylation patterns have been documented in brains and cerebrospinal fluid (CSF) of AD patients, suggesting biomarker potential and novel therapeutic targets. Moreover, glycosyltransferases and glycosidases show altered expression in neurodegeneration, linking metabolic and inflammatory pathways to tauopathy progression. This review synthesizes current evidence on the implications and consequences of glycosylation in AD and other tauopathies, integrating mechanistic, pathological, and clinical findings. We also discuss advances in glycoproteomics, the interplay between glycosylation and phosphorylation, and the translational potential of targeting glycosylation pathways for diagnosis and therapy. Full article
(This article belongs to the Special Issue Role of Glycomics in Health and Diseases)
►▼ Show Figures

Figure 1

56 pages, 4337 KB  
Review
Glycomics in Human Diseases and Its Emerging Role in Biomarker Discovery
by Sherifdeen Onigbinde, Moyinoluwa Adeniyi, Oluwatosin Daramola, Favour Chukwubueze, Md Mostofa Al Amin Bhuiyan, Judith Nwaiwu, Tuli Bhattacharjee and Yehia Mechref
Biomedicines 2025, 13(8), 2034; https://doi.org/10.3390/biomedicines13082034 - 21 Aug 2025
Cited by 12 | Viewed by 7400
Abstract
Glycosylation, the enzymatic addition of glycans to proteins and lipids, is a critical post-translational modification that influences protein folding, stability, trafficking, immune modulation, and cell signaling. The vast structural diversity of glycans arising from differences in monosaccharide composition, branching, and terminal modifications such [...] Read more.
Glycosylation, the enzymatic addition of glycans to proteins and lipids, is a critical post-translational modification that influences protein folding, stability, trafficking, immune modulation, and cell signaling. The vast structural diversity of glycans arising from differences in monosaccharide composition, branching, and terminal modifications such as sialylation, fucosylation, and sulfation underpins their functional specificity and regulatory capacity. This review provides a comprehensive overview of glycan biosynthesis, with a focus on N-glycans, O-glycans, glycosaminoglycans (GAGs), and glycolipids. It explores their essential roles in maintaining cellular homeostasis, development, and immune surveillance. In health, glycans mediate cell–cell communication, protein interactions, and immune responses. In disease, however, aberrant glycosylation is increasingly recognized as a hallmark of numerous pathological conditions, including cancer, neurodegenerative disorders, autoimmune diseases, and a wide range of infectious diseases. Glycomic alterations contribute to tumor progression, immune evasion, therapy resistance, neuroinflammation, and synaptic dysfunction. Tumor-associated carbohydrate antigens (TACAs) and disease-specific glycoforms present novel opportunities for biomarker discovery and therapeutic targeting. Moreover, glycan-mediated host–pathogen interactions are central to microbial adhesion, immune escape, and virulence. This review highlights current advances in glycomics technologies, including mass spectrometry, lectin microarrays, and glycoengineering, which have enabled the high-resolution profiling of the glycome. It also highlights the emerging potential of single-cell glycomics and multi-omics integration in precision medicine. Understanding glycome and its dynamic regulation is essential for uncovering the molecular mechanisms of disease and translating glycomic insights into innovative diagnostic and therapeutic strategies. Full article
(This article belongs to the Special Issue Role of Glycomics in Health and Diseases)
►▼ Show Figures

Figure 1

18 pages, 1885 KB  
Review
Advancement in Clinical Glycomics and Glycoproteomics for Congenital Disorders of Glycosylation: Progress and Challenges Ahead
by Nurulamin Abu Bakar and Nurul Izzati Hamzan
Biomedicines 2025, 13(8), 1964; https://doi.org/10.3390/biomedicines13081964 - 13 Aug 2025
Cited by 4 | Viewed by 2407
Abstract
Congenital disorders of glycosylation (CDG) are a group of rare, multisystemic genetic diseases caused by defects in glycan biosynthesis and protein glycosylation. Their broad clinical and genetic heterogeneity often require advanced diagnostic strategies. Clinical glycomics and glycoproteomics have emerged as powerful tools for [...] Read more.
Congenital disorders of glycosylation (CDG) are a group of rare, multisystemic genetic diseases caused by defects in glycan biosynthesis and protein glycosylation. Their broad clinical and genetic heterogeneity often require advanced diagnostic strategies. Clinical glycomics and glycoproteomics have emerged as powerful tools for understanding and diagnosing CDG by enabling high-resolution analysis of glycan structures and glycoproteins. Advancements in high-throughput mass spectrometry (MS) and site-specific glycoproteomics have led to the identification of disease-relevant biomarkers, providing insight into underlying glycosylation defects. These technologies enable detailed analysis of glycan structures and glycoproteins, improving early diagnosis, supporting biomarker discovery, and facilitating therapy monitoring. Integration with genomic and clinical data, including the use of dried blood spot testing and isotopic tracing, further enhances diagnostic precision and reveals the functional consequences of pathogenic variants. While challenges remain in standardizing methods, ensuring accessibility, and implementing bioinformatics tools, global collaborations and harmonized guidelines are beginning to address these gaps. Future directions include the use of artificial intelligence in data analysis, the development of comprehensive diagnostic frameworks, and international efforts to standardize glycomic methods. Collectively, these advances reinforce the growing clinical value of glycomics and glycoproteomics in the diagnosis and management of CDG. Full article
(This article belongs to the Special Issue Role of Glycomics in Health and Diseases)
►▼ Show Figures

Figure 1

Show export options expand_more Show export options expand_less
Select all
Export citation of selected articles as:
 
Displaying articles 1-4
Back to TopTop