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Glycosignals in Human Health and Diseases
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Glycosignals in Human Health and Diseases

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

Deadline for manuscript submissions: 31 August 2024 | Viewed by 2338

Special Issue Editor

Prof. Dr. Kazunori Hamamura

E-Mail Website
Guest Editor
Department of Pharmacology, School of Dentistry, Aichi Gakuin University, 1-100 Kusumoto-cho, Chikusa-ku, Nagoya 464-8650, Japan
Interests: glycosylation; glycosphingolipids; bone metabolism; malignant properties
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

The most important modification of proteins is glycosylation, which affects the structure of proteins and protein–protein interactions, such as those between protein ligands and their cognate receptor molecules. Many proteins are glycosylated, which impacts their activity when they bind to their receptors. Receptor signaling is regulated via glycosylation, the fucosylation of N-glycans and O-glycans on the receptors in various cells plays an important role in the regulation of cellular signaling.

Glycosphingolipids consist of carbohydrate chains and ceramide, which are not only tumor markers but also enhance the malignant properties of cancer cells. Recently, it was reported that they regulate bone metabolism. As one of the mechanisms, glycosphingolipids in lipid rafts interact with membrane molecules, leading to the enhancement or attenuation of cellular signaling.

This Special Issue, titled “Glycosignals in Human Health and Diseases”, provides up-to-date information on glycoscience and will cover research topics and current review articles in this field.

Prof. Dr. Kazunori Hamamura
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

  • glycosylation
  • glycoconjugates
  • glycolipids
  • gangliosides
  • glycoproteins

Published Papers (3 papers)

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Research

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16 pages, 625 KiB  
Article
Apolipoprotein-CIII O-Glycosylation Is Associated with Micro- and Macrovascular Complications of Type 2 Diabetes
by Annemieke Naber, Daniel Demus, Roderick C. Slieker, Simone Nicolardi, Joline W. J. Beulens, Petra J. M. Elders, Aloysius G. Lieverse, Eric J. G. Sijbrands, Leen M. ‘t Hart, Manfred Wuhrer and Mandy van Hoek
Int. J. Mol. Sci. 2024, 25(10), 5365; https://doi.org/10.3390/ijms25105365 - 14 May 2024
Viewed by 218
Abstract
Apolipoprotein-CIII (apo-CIII) inhibits the clearance of triglycerides from circulation and is associated with an increased risk of diabetes complications. It exists in four main proteoforms: O-glycosylated variants containing either zero, one, or two sialic acids and a non-glycosylated variant. O-glycosylation may affect the [...] Read more.
Apolipoprotein-CIII (apo-CIII) inhibits the clearance of triglycerides from circulation and is associated with an increased risk of diabetes complications. It exists in four main proteoforms: O-glycosylated variants containing either zero, one, or two sialic acids and a non-glycosylated variant. O-glycosylation may affect the metabolic functions of apo-CIII. We investigated the associations of apo-CIII glycosylation in blood plasma, measured by mass spectrometry of the intact protein, and genetic variants with micro- and macrovascular complications (retinopathy, nephropathy, neuropathy, cardiovascular disease) of type 2 diabetes in a DiaGene study (n = 1571) and the Hoorn DCS cohort (n = 5409). Mono-sialylated apolipoprotein-CIII (apo-CIII1) was associated with a reduced risk of retinopathy (β = −7.215, 95% CI −11.137 to −3.294) whereas disialylated apolipoprotein-CIII (apo-CIII2) was associated with an increased risk (β = 5.309, 95% CI 2.279 to 8.339). A variant of the GALNT2-gene (rs4846913), previously linked to lower apo-CIII0a, was associated with a decreased prevalence of retinopathy (OR = 0.739, 95% CI 0.575 to 0.951). Higher apo-CIII1 levels were associated with neuropathy (β = 7.706, 95% CI 2.317 to 13.095) and lower apo-CIII0a with macrovascular complications (β = −9.195, 95% CI −15.847 to −2.543). In conclusion, apo-CIII glycosylation was associated with the prevalence of micro- and macrovascular complications of diabetes. Moreover, a variant in the GALNT2-gene was associated with apo-CIII glycosylation and retinopathy, suggesting a causal effect. The findings facilitate a molecular understanding of the pathophysiology of diabetes complications and warrant consideration of apo-CIII glycosylation as a potential target in the prevention of diabetes complications. Full article
(This article belongs to the Special Issue Glycosignals in Human Health and Diseases)
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14 pages, 1184 KiB  
Article
Serum Clusterin Concentration and Its Glycosylation Changes as Potential New Diagnostic Markers of SARS-CoV-2 Infection and Recovery Process
by Katarzyna Sołkiewicz, Izabela Kokot, Monika Kacperczyk, Violetta Dymicka-Piekarska, Justyna Dorf and Ewa Maria Kratz
Int. J. Mol. Sci. 2024, 25(8), 4198; https://doi.org/10.3390/ijms25084198 - 10 Apr 2024
Viewed by 536
Abstract
COVID-19 is an infectious disease caused by the SARS-CoV-2 virus. Glycoprotein clusterin (CLU) has many functions such as phagocyte recruitment, complement system inhibition, apoptosis inhibition, hormone and lipid transport, as well as in the immune response. The study aimed to assess the changes [...] Read more.
COVID-19 is an infectious disease caused by the SARS-CoV-2 virus. Glycoprotein clusterin (CLU) has many functions such as phagocyte recruitment, complement system inhibition, apoptosis inhibition, hormone and lipid transport, as well as in the immune response. The study aimed to assess the changes in CLU concentrations and the profile and degree of CLU glycosylation between patients with severe COVID-19, convalescents, and healthy subjects (control). The profile and degree of serum CLU N-glycosylation were analyzed using lectin-ELISA with specific lectins. CLU concentrations were significantly lower and relative reactivities of CLU glycans with SNA (Sambucus nigra agglutinin) were significantly higher in severe COVID-19 patients in comparison to convalescents and the control group. The relative reactivities of CLU glycans with MAA (Maackia amurensis agglutinin), together with relative reactivity with LCA (Lens culinaris agglutinin), were also significantly higher in patients with severe COVID-19 than in convalescents and the control group, but they also significantly differed between convalescents and control. The development of acute inflammation in the course of severe COVID-19 is associated with a decrease in CLU concentration, accompanied by an increase in the expression of α2,3-linked sialic acid, and core fucose. Both of these parameters can be included as useful glycomarkers differentiating patients with severe COVID-19 from convalescents and the control group, as well as convalescents and healthy subjects. Full article
(This article belongs to the Special Issue Glycosignals in Human Health and Diseases)
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Review

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14 pages, 2755 KiB  
Review
Regulation of Glycosylation in Bone Metabolism
by Kazunori Hamamura, Mayu Nagao and Koichi Furukawa
Int. J. Mol. Sci. 2024, 25(7), 3568; https://doi.org/10.3390/ijms25073568 - 22 Mar 2024
Viewed by 942
Abstract
Glycosylation plays a crucial role in the maintenance of homeostasis in the body and at the onset of diseases such as inflammation, neurodegeneration, infection, diabetes, and cancer. It is also involved in bone metabolism. N- and O-glycans have been shown to [...] Read more.
Glycosylation plays a crucial role in the maintenance of homeostasis in the body and at the onset of diseases such as inflammation, neurodegeneration, infection, diabetes, and cancer. It is also involved in bone metabolism. N- and O-glycans have been shown to regulate osteoblast and osteoclast differentiation. We recently demonstrated that ganglio-series and globo-series glycosphingolipids were essential for regulating the proliferation and differentiation of osteoblasts and osteoclasts in glycosyltransferase-knockout mice. Herein, we reviewed the importance of the regulation of bone metabolism by glycoconjugates, such as glycolipids and glycoproteins, including our recent results. Full article
(This article belongs to the Special Issue Glycosignals in Human Health and Diseases)
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