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Biomolecules
Special Issues
Glycomics in Health, Aging and Disease
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Glycomics in Health, Aging and Disease

A special issue of Biomolecules (ISSN 2218-273X). This special issue belongs to the section "Cellular Biochemistry".

Deadline for manuscript submissions: 30 November 2026 | Viewed by 2975

Editor

Dr. Domenico Garozzo

E-Mail Website
Guest Editor
Institute for Polymers, Composites and Biomaterials (IPCB CNR) of Catania, Catania, Italy
Interests: glycomics; mass spectrometry; polysaccharides; lipopolysaccharides; structural elucidation; congenital glycosylation defects; neurodegenerative diseases
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

The glycome plays an essential role in life, since glycans (glycoproteins, glycolipids, proteoglycans, lipopolysaccharides, free glycans etc.) are vital in cell communication, cell growth, tumors and metastasis, and bacterial and viral infections. It is therefore not surprising that many diseases are linked to abnormalities in the synthesis of glycans, from congenital glycosylation disorders (CDGs) to other illnesses such as autoimmune and inflammatory diseases, neurodegenerative diseases, and cancer.

While the above considerations are well recognized today, the impact of glycome on life was underestimated until relatively recently. The first CDG was described by Jaak Jaeken and collaborators in 1980, with the next case reported only a decade later. The same applies to all other fields of glyco-science, a field that is still relatively young. Today, we are aware of the importance of the glycome in life sciences, and a growing number of scientists are working in this domain. In recent years, we have also seen a proliferation of new analytical and IT tools and new investigation methodologies, and many large projects have been funded by public and private agencies.

With this Special Issue entitled “Glycomics in Health, Aging and Disease”, we aim to provide a dedicated platform for all glyco-scientists to publish their results in the journal of Biomolecules. We welcome all kinds of contributions (reviews, original articles, prospective articles) concerning structural and/or functional studies on glycans and glycoconjugates, as well as on those aspects that can shed light on their physiological roles, their biosynthesis, the pathophysiology of glycosylation disorders, and their role in bacterial and viral infections.

Therefore, we are pleased to invite you to submit your manuscript to this Special Issue.

We look forward to receiving your contributions.

Dr. Domenico Garozzo
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-anonymized 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

  • glycome
  • glycobiology
  • glycochemistry
  • glycans
  • glycoconjugates

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Published Papers (4 papers)

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Research

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22 pages, 16217 KB  
Article
Revitalizing Muscle Repair: Hyaluronan Preserves Mitochondrial Architecture and Promotes Myogenesis Under Pro-Inflammatory Conditions
by Fabio Ferrini, Giosuè Annibalini, Michela Battistelli, SeyedehMahboobeh Moosavi, Osman Riham, Fabiana Fanelli, Italo Capparucci, Piero Sestili and Elena Barbieri
Biomolecules 2026, 16(6), 913; https://doi.org/10.3390/biom16060913 - 19 Jun 2026
Viewed by 320
Abstract
Hyaluronic acid (HA), a major component of the glycome and a non-sulfated glycosaminoglycan, plays a crucial role in regulating stem cell behavior and function, thereby supporting skeletal muscle repair under inflammatory conditions. In this study, we investigated the effects of a mixture of [...] Read more.
Hyaluronic acid (HA), a major component of the glycome and a non-sulfated glycosaminoglycan, plays a crucial role in regulating stem cell behavior and function, thereby supporting skeletal muscle repair under inflammatory conditions. In this study, we investigated the effects of a mixture of HA fractions with different molecular weights (M-HA; 2–1000 kDa) on the repair capacity and myogenic potential of C2C12 murine myoblasts exposed to inflammatory stimuli. C2C12 cells were cultured, induced to differentiate, and treated with M-HA (1 mg/mL) under either physiological or inflammatory conditions (LPS, 10 µg/mL; IL-1β, 20 ng/mL). M-HA exhibited no cytotoxic effects, even at the highest concentration tested (1.0 mg/mL), and significantly enhanced scratch wound closure. Moreover, M-HA improved the myogenic index at day 5 of differentiation, promoted the expression of myogenic markers, preserved myosin heavy chain (MHC) levels under inflammatory stress, and reduced the expression of autophagy-related genes. Ultrastructural analyses revealed that untreated myotubes displayed swollen mitochondria, disrupted cristae architecture, and numerous autophagic vacuoles, whereas M-HA-treated cells exhibited well-preserved mitochondrial morphology, intact cristae organization, reduced cytoplasmic damage, and maintained myofibrillar structure. Taken together, the functional, molecular, and ultrastructural findings demonstrate that M-HA protects myoblasts from inflammation-induced cellular damage and supports their regenerative capacity. These results underscore the potential of glycomics-based strategies to enhance myogenic differentiation and promote skeletal muscle regeneration in inflammatory microenvironments. Full article
(This article belongs to the Special Issue Glycomics in Health, Aging and Disease)
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13 pages, 3375 KB  
Article
IgG Glycosylation Analysis in Patients with Ring14 Syndrome Unveils Novel Pathomechanisms and New Therapy Perspectives
by Angela Messina, Angelo Palmigiano, Donata Agata Romeo, Luisa Sturiale, Enrico Parano, Marco Crimi, Annunziata Carrese Cirillo, Alessandro Vaisfeld, Rita Barone and Domenico Garozzo
Biomolecules 2026, 16(6), 760; https://doi.org/10.3390/biom16060760 - 22 May 2026
Viewed by 728
Abstract
Ring chromosome 14 (RC14) syndrome is an ultra-rare disorder characterized by drug-resistant epilepsy, intellectual disabilities, autism, and recurrent infections, suggesting a possible underlying immune dysregulation. We analyzed immunoglobulin G (IgG) N-glycosylation profiles in six RC14 patients and compared them with age-matched healthy controls [...] Read more.
Ring chromosome 14 (RC14) syndrome is an ultra-rare disorder characterized by drug-resistant epilepsy, intellectual disabilities, autism, and recurrent infections, suggesting a possible underlying immune dysregulation. We analyzed immunoglobulin G (IgG) N-glycosylation profiles in six RC14 patients and compared them with age-matched healthy controls using ultra-high-performance liquid chromatography (UHPLC) coupled with fluorescence detection (FLR) and high-resolution electrospray ionization mass spectrometry (ESI-MS). Patients showed decreased galactosylation and sialylation, resembling pro-inflammatory patterns observed in autoimmune diseases. These alterations were not observed in total serum glycoproteins, indicating a selective effect on IgG. One patient treated with intravenous immunoglobulin (IVIG) showed clinical improvement, which led us to investigate causality. Full article
(This article belongs to the Special Issue Glycomics in Health, Aging and Disease)
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13 pages, 518 KB  
Article
Expanded Clinical Spectrum of Autosomal-Dominant STT3A-CDG
by Hamdan Al-Shahrani, Evelin Szabó, Caroline Staccone, Georgia MacDonald, Yutaka Furuta, Daniel Schecter, Andrew C. Edmondson, Anne McRae, Josh Baker, Eva Morava and Rory J. Tinker
Biomolecules 2026, 16(3), 418; https://doi.org/10.3390/biom16030418 - 12 Mar 2026
Viewed by 894
Abstract
STT3A encodes the catalytic subunit of the oligosaccharyltransferase A (OST-A) complex and is classically linked to severe autosomal-recessive congenital disorder of glycosylation (CDG). To define the distinct autosomal-dominant disorder, we reviewed all published cases and integrated three previously unpublished individuals from the CDG [...] Read more.
STT3A encodes the catalytic subunit of the oligosaccharyltransferase A (OST-A) complex and is classically linked to severe autosomal-recessive congenital disorder of glycosylation (CDG). To define the distinct autosomal-dominant disorder, we reviewed all published cases and integrated three previously unpublished individuals from the CDG natural history study. Across 21 individuals, abnormal transferrin glycosylation was present in nearly all individuals (20/21), and subtle facial dysmorphism was common (18/21). Neurodevelopmental involvement was frequent, including motor delay (13/21), learning difficulties (13/21), speech delay (12/21), and intellectual disability (10/21). Musculoskeletal manifestations were also common, including skeletal abnormalities (12/21), short stature (11/21), muscle cramps (8/21), and early-onset osteoarthritis in adults (6/21). Less frequent features included congenital heart defects (5/21) and coagulation factor deficiency (5/21). Importantly, the newly reported individuals expand dominant STT3A-CDG with previously unreported features, including anorectal malformation, morbid obesity, and clinically significant bleeding diathesis with von Willebrand factor and factor VIII deficiency. Biochemical signatures ranged from classic type I transferrin patterns to subtle or atypical abnormalities, emphasizing that near-normal transferrin testing does not exclude the diagnosis. Variants clustered in conserved catalytic regions, with recurrent p.Arg405 across de novo, inherited, and mosaic cases supporting a mutational hotspot and likely dominant-negative mechanism. Full article
(This article belongs to the Special Issue Glycomics in Health, Aging and Disease)
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Review

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17 pages, 2757 KB  
Review
Glycogen and Glycosylation: Friends or Foes?
by Rohit Sai Reddy Konada, James Osborn and Sharmistha Mitra
Biomolecules 2026, 16(6), 885; https://doi.org/10.3390/biom16060885 - 16 Jun 2026
Viewed by 461
Abstract
Glycosylation, glycogen metabolism, and ubiquitination represent three fundamental cellular processes that are traditionally studied as distinct aspects of biology. Glycosylation and glycogen metabolism are unique carbohydrate-based pathways. The process of glycosylation generates structurally diverse glycans that regulate protein folding, cell signaling, and host–pathogen [...] Read more.
Glycosylation, glycogen metabolism, and ubiquitination represent three fundamental cellular processes that are traditionally studied as distinct aspects of biology. Glycosylation and glycogen metabolism are unique carbohydrate-based pathways. The process of glycosylation generates structurally diverse glycans that regulate protein folding, cell signaling, and host–pathogen interactions, while glycogen serves as a glucose reserve essential for energy homeostasis. Emerging evidence reveals a deep mechanistic connection between these pathways, particularly in the context of brain biology and inherited metabolic diseases. Here, we present recent research linking glycosylation defects with glycogen metabolism, highlighting how changes in the shared metabolites and enzymatic pathways contribute to human health and disease. We then discuss the overlapping disease symptoms of congenital disorders of glycosylation and glycogen storage diseases, with particular emphasis on polyglucosan body-forming diseases. We also highlight the role of non-canonical ubiquitin ligase complexes such as laforin–malin and LUBAC and present emerging evidence for their potential role in the glycogen quality-control mechanism. Finally, we review current therapeutic strategies for CDGs and GSDs, including monosaccharide supplementation, glycogen synthase modulation, and gene therapy. Together, this review underscores glycogen as more than an energy store—as a key contributor to glycosylation homeostasis and cellular regulation in health and disease. Full article
(This article belongs to the Special Issue Glycomics in Health, Aging and Disease)
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