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Glycomics: Implications for Metabolic Health and Disease
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Glycomics: Implications for Metabolic Health and Disease

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: closed (31 December 2021) | Viewed by 17345

Special Issue Editors

Prof. Dr. Alexey V. Pshezhetsky

E-Mail Website1 Website2
Guest Editor
Division of Medical Genetics, CHU Ste-Justine Research Centre, Montreal, QC H3T 1C5, Canada
Interests: glycobiology; sialic acids; neuraminidases; sialidases; lysosomal diseases; mucopolysaccharidosis; Sanfilippo disease; sialidosis; synaptic transmission; neurodegeneration; neuroinflammation; mouse models; atherosclerosis; diabetes type 2; inborn errors of metabolism; gene therapy
Prof. Dr. Christopher W. Cairo

E-Mail Website
Guest Editor
Department of Chemistry, Faculty of Science, University of Alberta, Edmonton , AB, Canada
Interests: chemical glycobiology; medicinal glycochemistry; enzyme inhibitors; bioconjugate chemistry; neuraminidases; sialidases cardiovascular disease; cancer; inflammation; leukocyte receptors
Dr. Domenico Garozzo

E-Mail Website
Guest Editor
Head, 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 Issue Information

Dear Colleagues,

Highly ordered interactions between glycans and their receptors are evolutionary conserved and crucial for healthy metabolic responses. Disruptions of these interactions underline the pathogenesis of a wide range of metabolic diseases from those providing a global risk for the contemporary and future public health such as diabetes, cardiovascular and neurodegenerative disorders to rare inborn errors of metabolism.

Glycomics, a targeted approach for the analysis of glycans in biological systems, thus offers a unique opportunity for identification of novel disease mechanisms underlying metabolic diseases as well as potential biomarkers for their prevention and treatment. This special issue focuses on the recent advances in our understanding of the roles of glycans, their receptors, glycosidases, and glycosyltransferases in normal metabolism and its pathological alterations. Authors are invited to submit their original research conducted in both basic and clinical settings and describing the molecular, cellular and biochemical mechanisms by which glycans contribute to metabolic regulation and cellular signaling. We also welcome reviews discussing how this work may eventually lead to promotion of human health and disease control.

Prof. Dr. Alexey V. Pshezhetsky
Prof. Dr. Christopher W. Cairo
Dr. Domenico Garozzo
Guest Editors

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
  • Glycome
  • Glycosydases
  • Glycosyltransferases
  • Sialidases
  • Sialyltransferases
  • Metabolism
  • Diabetes
  • CAD
  • Atherosclerosis
  • Signaling
  • Biomarkers
  • Inflammation
  • Sphingolipids
  • Glycoproteins
  • Inborn errors of metabilism

Published Papers (5 papers)

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Research

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12 pages, 10493 KiB  
Article
Characterization of Sialic Acid Affinity of the Binding Domain of Mistletoe Lectin Isoform One
by Soran Mohammed and Natalie Ferry
Int. J. Mol. Sci. 2021, 22(15), 8284; https://doi.org/10.3390/ijms22158284 - 31 Jul 2021
Cited by 1 | Viewed by 1869
Abstract
Sialic acid (Sia) is considered as one of the most important biomolecules of life since its derivatives and terminal orientations on cell membranes and macromolecules play a major role in many biological and pathological processes. To date, there is only a limited number [...] Read more.
Sialic acid (Sia) is considered as one of the most important biomolecules of life since its derivatives and terminal orientations on cell membranes and macromolecules play a major role in many biological and pathological processes. To date, there is only a limited number of active molecules that can selectively bind to Sia and this limitation has made the study of this glycan challenging. The lectin superfamily is a well-known family of glycan binding proteins, which encompasses many strong glycan binding peptides with diverse glycan affinities. Mistletoe lectin (ML) is considered one of the most active members of lectin family which was initially classified in early studies as a galactose binding lectin; more recent studies have suggested that the peptide can also actively bind to Sia. However, the details with respect to Sia binding of ML and the domain responsible for this binding are left unanswered because no comprehensive studies have been instigated. In this study, we sought to identify the binding domain responsible for the sialic acid affinity of mistletoe lectin isoform I (MLI) in comparison to the binding activity of elderberry lectin isoform I (SNA), which has long been identified as a potent Sia binding lectin. In order to execute this, we performed computational carbohydrate-protein docking for MLB and SNA with Neu5Ac and β-Galactose. We further analyzed the coding sequence of both lectins and identified their glycan binding domains, which were later cloned upstream and downstream to green fluorescent protein (GFP) and expressed in Escherichia coli (E. coli). Finally, the glycan affinity of the expressed fusion proteins was assessed by using different biochemical and cell-based assays and the Sia binding domains were identified. Full article
(This article belongs to the Special Issue Glycomics: Implications for Metabolic Health and Disease)
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14 pages, 2380 KiB  
Article
N-Glycomics of Human Erythrocytes
by Rosaria Ornella Bua, Angela Messina, Luisa Sturiale, Rita Barone, Domenico Garozzo and Angelo Palmigiano
Int. J. Mol. Sci. 2021, 22(15), 8063; https://doi.org/10.3390/ijms22158063 - 28 Jul 2021
Cited by 5 | Viewed by 3239
Abstract
Glycosylation is a complex post-translational modification that conveys functional diversity to glycoconjugates. Cell surface glycosylation mediates several biological activities such as induction of the intracellular signaling pathway and pathogen recognition. Red blood cell (RBC) membrane N-glycans determine blood type and influence cell lifespan. [...] Read more.
Glycosylation is a complex post-translational modification that conveys functional diversity to glycoconjugates. Cell surface glycosylation mediates several biological activities such as induction of the intracellular signaling pathway and pathogen recognition. Red blood cell (RBC) membrane N-glycans determine blood type and influence cell lifespan. Although several proteomic studies have been carried out, the glycosylation of RBC membrane proteins has not been systematically investigated. This work aims at exploring the human RBC N-glycome by high-sensitivity MALDI-MS techniques to outline a fingerprint of RBC N-glycans. To this purpose, the MALDI-TOF spectra of healthy subjects harboring different blood groups were acquired. Results showed the predominant occurrence of neutral and sialylated complex N-glycans with bisected N-acetylglucosamine and core- and/or antennary fucosylation. In the higher mass region, these species presented with multiple N-acetyllactosamine repeating units. Amongst the detected glycoforms, the presence of glycans bearing ABO(H) antigens allowed us to define a distinctive spectrum for each blood group. For the first time, advanced glycomic techniques have been applied to a comprehensive exploration of human RBC N-glycosylation, providing a new tool for the early detection of distinct glycome changes associated with disease conditions as well as for understanding the molecular recognition of pathogens. Full article
(This article belongs to the Special Issue Glycomics: Implications for Metabolic Health and Disease)
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15 pages, 3341 KiB  
Article
Mesenchymal Stromal Cells Regulate Sialylations of N-Glycans, Affecting Cell Migration and Survival
by Kayla Templeton, Meiby Ramos, Jacqueline Rose, Bryan Le, Qingwen Zhou, Amin Cressman, Stephanie Ferreyra, Carlito B. Lebrilla and Fernando Antonio Fierro
Int. J. Mol. Sci. 2021, 22(13), 6868; https://doi.org/10.3390/ijms22136868 - 26 Jun 2021
Cited by 10 | Viewed by 2412
Abstract
N-Glycosylations are an important post-translational modification of proteins that can significantly impact cell function. Terminal sialic acid in hybrid or complex N-glycans has been shown to be relevant in various types of cancer, but its role in non-malignant cells remains poorly understood. We [...] Read more.
N-Glycosylations are an important post-translational modification of proteins that can significantly impact cell function. Terminal sialic acid in hybrid or complex N-glycans has been shown to be relevant in various types of cancer, but its role in non-malignant cells remains poorly understood. We have previously shown that the motility of human bone marrow derived mesenchymal stromal cells (MSCs) can be modified by altering N-glycoforms. The goal of this study was to determine the role of sialylated N-glycans in MSCs. Here, we show that IFN-gamma or exposure to culture media low in fetal bovine serum (FBS) increases sialylated N-glycans, while PDGF-BB reduces them. These stimuli alter mRNA levels of sialyltransferases such as ST3Gal1, ST6Gal1, or ST3Gal4, suggesting that sialylation of N-glycans is regulated by transcriptional control of sialyltransferases. We next show that 2,4,7,8,9-pentaacetyl-3Fax-Neu5Ac-CO2Me (3F-Neu5Ac) effectively inhibits sialylations in MSCs. Supplementation with 3F-Neu5Ac increases adhesion and migration of MSCs, as assessed by both videomicroscopy and wound/scratch assays. Interestingly, pre-treatment with 3F-Neu5Ac also increases the survival of MSCs in an in vitro ischemia model. We also show that pre-treatment or continuous treatment with 3F-Neu5Ac inhibits both osteogenic and adipogenic differentiation of MSCs. Finally, secretion of key trophic factors by MSCs is variably affected upon exposure to 3F-Neu5Ac. Altogether, our experiments suggest that sialylation of N-glycans is tightly regulated in response to environmental cues and that glycoengineering MSCs to reduce sialylated N-glycans could be beneficial to increase both cell migration and survival, which may positively impact the therapeutic potential of the cells. Full article
(This article belongs to the Special Issue Glycomics: Implications for Metabolic Health and Disease)
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24 pages, 3901 KiB  
Article
Novel Insights into Selected Disease-Causing Mutations within the SLC35A1 Gene Encoding the CMP-Sialic Acid Transporter
by Bożena Szulc, Yelyzaveta Zadorozhna, Mariusz Olczak, Wojciech Wiertelak and Dorota Maszczak-Seneczko
Int. J. Mol. Sci. 2021, 22(1), 304; https://doi.org/10.3390/ijms22010304 - 30 Dec 2020
Cited by 8 | Viewed by 2680
Abstract
Congenital disorders of glycosylation (CDG) are a group of rare genetic and metabolic diseases caused by alterations in glycosylation pathways. Five patients bearing CDG-causing mutations in the SLC35A1 gene encoding the CMP-sialic acid transporter (CST) have been reported to date. In this study [...] Read more.
Congenital disorders of glycosylation (CDG) are a group of rare genetic and metabolic diseases caused by alterations in glycosylation pathways. Five patients bearing CDG-causing mutations in the SLC35A1 gene encoding the CMP-sialic acid transporter (CST) have been reported to date. In this study we examined how specific mutations in the SLC35A1 gene affect the protein’s properties in two previously described SLC35A1-CDG cases: one caused by a substitution (Q101H) and another involving a compound heterozygous mutation (T156R/E196K). The effects of single mutations and the combination of T156R and E196K mutations on the CST’s functionality was examined separately in CST-deficient HEK293T cells. As shown by microscopic studies, none of the CDG-causing mutations affected the protein’s proper localization in the Golgi apparatus. Cellular glycophenotypes were characterized using lectins, structural assignment of N- and O-glycans and analysis of glycolipids. Single Q101H, T156R and E196K mutants were able to partially restore sialylation in CST-deficient cells, and the deleterious effect of a single T156R or E196K mutation on the CST functionality was strongly enhanced upon their combination. We also revealed differences in the ability of CST variants to form dimers. The results of this study improve our understanding of the molecular background of SLC35A1-CDG cases. Full article
(This article belongs to the Special Issue Glycomics: Implications for Metabolic Health and Disease)
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Review

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39 pages, 2342 KiB  
Review
Glycosylation Biomarkers Associated with Age-Related Diseases and Current Methods for Glycan Analysis
by Beatrix Paton, Manuel Suarez, Pol Herrero and Núria Canela
Int. J. Mol. Sci. 2021, 22(11), 5788; https://doi.org/10.3390/ijms22115788 - 28 May 2021
Cited by 22 | Viewed by 6051
Abstract
Ageing is a complex process which implies the accumulation of molecular, cellular and organ damage, leading to an increased vulnerability to disease. In Western societies, the increase in the elderly population, which is accompanied by ageing-associated pathologies such as cardiovascular and mental diseases, [...] Read more.
Ageing is a complex process which implies the accumulation of molecular, cellular and organ damage, leading to an increased vulnerability to disease. In Western societies, the increase in the elderly population, which is accompanied by ageing-associated pathologies such as cardiovascular and mental diseases, is becoming an increasing economic and social burden for governments. In order to prevent, treat and determine which subjects are more likely to develop these age-related diseases, predictive biomarkers are required. In this sense, some studies suggest that glycans have a potential role as disease biomarkers, as they modify the functions of proteins and take part in intra- and intercellular biological processes. As the glycome reflects the real-time status of these interactions, its characterisation can provide potential diagnostic and prognostic biomarkers for multifactorial diseases. This review gathers the alterations in protein glycosylation profiles that are associated with ageing and age-related diseases, such as cancer, type 2 diabetes mellitus, metabolic syndrome and several chronic inflammatory diseases. Furthermore, the review includes the available techniques for the determination and characterisation of glycans, such as liquid chromatography, electrophoresis, nuclear magnetic resonance and mass spectrometry. Full article
(This article belongs to the Special Issue Glycomics: Implications for Metabolic Health and Disease)
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