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Glyco-Dynamics and Cell Signaling
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Glyco-Dynamics and Cell Signaling

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

Deadline for manuscript submissions: closed (15 August 2023) | Viewed by 3969

Special Issue Editor

Prof. Dr. Koichi Furukawa

E-Mail Website
Guest Editor
Department of Biomedical Sciences, Chubu University College of Life and Health Sciences, Kasugai 487-8501, Japan
Interests: glycosphingolipids; neuronal cell; glioma cell; cancer; glycosylation; gangliosides; inflammation; neurodegeneration
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Recently, the dynamic actions of sugar chains both on the cell surface and between cells have been elucidated, and their significance has been disclosed. Focusing on the spatiotemporal dynamics of glycoconjugates on the cell membrane, between cell surface and cytoplasm, release from cells and in targeting other cells, a number of challenging studies have been performed, elucidating changes in cell signaling and cell behavior. The findings of those studies should bring about discoveries of novel modes of glycoconjugate behaviors including cluster formations with receptors on the membrane and changes of adapter signaling molecules in the cytoplasm. Furthermore, various glycoconjugates are generated based on the uptake of free glyco-molecules from outside of cells as well as de novo synthetic pathways. Some glycoconjugates are generated from other organisms from the external environment (e.g., microbiota in the intestinal system, food materials). The processes of these dynamic behaviors and modifications of glyco-structures, and the consequent roles of various glycoconjugates are not well-known at this moment.

These topics should be fresh and exciting for many researchers and readers, and will provide deep insights into regulatory mechanisms for generation of novel glycoconjugates and their roles in the nervous system, metabolism, immune system, and cancers.

Prof. Dr. Koichi Furukawa
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

  • cell signaling
  • dynamics
  • glycoconjugate
  • cell membrane
  • molecular cluster
  • extracellular vesicle
  • microbiota
  • glyco-modification
  • neurodegeneration
  • cancer

Published Papers (2 papers)

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Research

12 pages, 3364 KiB  
Article
Reducing Sialylation Enhances Electrotaxis of Corneal Epithelial Cells
by Bryan Le, Kan Zhu, Chelsea Brown, Brian Reid, Amin Cressman, Min Zhao and Fernando A. Fierro
Int. J. Mol. Sci. 2023, 24(18), 14327; https://doi.org/10.3390/ijms241814327 - 20 Sep 2023
Viewed by 786
Abstract
Corneal wound healing is a complex biological process that integrates a host of different signals to coordinate cell behavior. Upon wounding, there is the generation of an endogenous wound electric field that serves as a powerful cue to guide cell migration. Concurrently, the [...] Read more.
Corneal wound healing is a complex biological process that integrates a host of different signals to coordinate cell behavior. Upon wounding, there is the generation of an endogenous wound electric field that serves as a powerful cue to guide cell migration. Concurrently, the corneal epithelium reduces sialylated glycoforms, suggesting that sialylation plays an important role during electrotaxis. Here, we show that pretreating human telomerase-immortalized corneal epithelial (hTCEpi) cells with a sialyltransferase inhibitor, P-3FAX-Neu5Ac (3F-Neu5Ac), improves electrotaxis by enhancing directionality, but not speed. This was recapitulated using Kifunensine, which inhibits cleavage of mannoses and therefore precludes sialylation on N-glycans. We also identified that 3F-Neu5Ac enhanced the responsiveness of the hTCEpi cell population to the electric field and that pretreated hTCEpi cells showed increased directionality even at low voltages. Furthermore, when we increased sialylation using N-azidoacetylmannosamine-tetraacylated (Ac4ManNAz), hTCEpi cells showed a decrease in both speed and directionality. Importantly, pretreating enucleated eyes with 3F-Neu5Ac significantly improved re-epithelialization in an ex vivo model of a corneal injury. Finally, we show that in hTCEpi cells, sialylation is increased by growth factor deprivation and reduced by PDGF-BB. Taken together, our results suggest that during corneal wound healing, reduced sialylated glycoforms enhance electrotaxis and re-epithelialization, potentially opening new avenues to promote corneal wound healing. Full article
(This article belongs to the Special Issue Glyco-Dynamics and Cell Signaling)
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17 pages, 1694 KiB  
Article
In-Depth Analysis of the N-Glycome of Colorectal Cancer Cell Lines
by Di Wang, Valeriia Kuzyk, Katarina Madunić, Tao Zhang, Oleg A. Mayboroda, Manfred Wuhrer and Guinevere S. M. Lageveen-Kammeijer
Int. J. Mol. Sci. 2023, 24(5), 4842; https://doi.org/10.3390/ijms24054842 - 2 Mar 2023
Cited by 1 | Viewed by 2478
Abstract
Colorectal cancer (CRC) is the third most commonly diagnosed cancer and the second leading cause of cancer deaths worldwide. A well-known hallmark of cancer is altered glycosylation. Analyzing the N-glycosylation of CRC cell lines may provide potential therapeutic or diagnostic targets. In [...] Read more.
Colorectal cancer (CRC) is the third most commonly diagnosed cancer and the second leading cause of cancer deaths worldwide. A well-known hallmark of cancer is altered glycosylation. Analyzing the N-glycosylation of CRC cell lines may provide potential therapeutic or diagnostic targets. In this study, an in-depth N-glycomic analysis of 25 CRC cell lines was conducted using porous graphitized carbon nano-liquid chromatography coupled to electrospray ionization mass spectrometry. This method allows for the separation of isomers and performs structural characterization, revealing profound N-glycomic diversity among the studied CRC cell lines with the elucidation of a number of 139 N-glycans. A high degree of similarity between the two N-glycan datasets measured on the two different platforms (porous graphitized carbon nano-liquid chromatography electrospray ionization tandem mass spectrometry (PGC-nano-LC-ESI-MS) and matrix-assisted laser desorption/ionization time of flight-mass spectrometry (MALDI-TOF-MS)) was discovered. Furthermore, we studied the associations between glycosylation features, glycosyltransferases (GTs), and transcription factors (TFs). While no significant correlations between the glycosylation features and GTs were found, the association between TF CDX1 and (s)Le antigen expression and relevant GTs FUT3/6 suggests that CDX1 contributes to the expression of the (s)Le antigen through the regulation of FUT3/6. Our study provides a comprehensive characterization of the N-glycome of CRC cell lines, which may contribute to the future discovery of novel glyco-biomarkers of CRC. Full article
(This article belongs to the Special Issue Glyco-Dynamics and Cell Signaling)
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