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Special Issue "Glycan–Receptor Interaction 2018"

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

Deadline for manuscript submissions: closed (25 September 2018)

Special Issue Editor

Guest Editor
Prof. Dr. Cheorl-Ho Kim

Molecular and Cellular Glycobiology Unit, Department of Biological Sciences, College of Science, Sungkyukwan University, 2066, Seobu-Ro, Jangan-Gu, Suwon-Si, Gyeong Gi, Korea
Website | E-Mail
Phone: +82-31-290-7002
Fax: +82-31-290-7015
Interests: glycobiology; sialobiology; sialyltransferase; N-glycan; O-glycan; glycolipid; sphingolipid; glycoprotein; surface sugar; ganglioside; sialic acid; sialyl Le antigen; lectin; galectin; siglec; ER-Golgi glyosylation; sugar–receptor interaction; innate immune; xenotransplantation; cell–cell interaction

Special Issue Information

Dear Colleagues,

Cell surface carbohydrates attached to proteins and lipids are major components of the outer surface of mammalian cells. Changes to the surface glycosylation are important means of cell–cell interaction in fertilization, development, differentiation, growth, aging, adhesion, signal transduction, neurotransduction, immune systems, and carcinogenesis, metastasis, and angiogenesis. Therefore, surface glycosylations are mainly located on the borders of cells to communicate through face-to-face recognition or carbohydrate glycan–receptor interaction. Because the glycans communicate with their counterparts, such as specific receptors through purely physical interactions, the synthesis and distribution of these components are under strict genetic control. These glycosylated proteins and lipids have been implicated in multicellular functional expression and society formation, which depends on cell type, tissue type, and organ type. Modifications of cellular glycosylation are also a common phenotypic change in malignancy, with a poor prognosis for the patients. Most of the carbohydrate tumor antigens are sialylated. As examples, the mucin-type Sialyl-Tn, Sialyl-Lewis X, and Sialyl-Lewis A antigens are increased in the N-linked and O-linked oligosaccharides of the carcinoma cell glycoproteins of cancers. In recent viral pandemics, it was recognized that human and avian influenza viruses bind sialic acid-based receptors. For example, a human-type is NeuAcα2-6Gal, while an avian-type is NeuAcα2-3Gal. From the recent human type H3N2 virus, the evolutionary transition has been suggested in sialyl ligand–receptor interaction. Therefore, interaction between the influenza virus and sialic acid receptors is the hot issue of current glycan–receptor interaction. The changed glycans can regulate carbohydrate–carbohydrate, carbohydrate–protein, and carbohydrate–lipid interactions. Therefore, each glycan structure has been implicated as a face or signature of certain biological states in cells and organs. In tumors, the glycosylated antigens can be used as tumor markers for human cancer patients, especially for node-negative patients.

We invite researchers to contribute original and review articles regarding the interactions between glycans and proteins. Potential topics include, but are not limited to:

  • Glycosylation of N-/O-glycoproteins
  • Sialylation of glycoproteins and glycolipids
  • Lectin–glycan interaction
  • Sialyltransferases
  • Glycosylation in malignancy and cancers
  • Xenoantigenic glycosylation in non-human mammals
  • Sphingolipids in membranes
  • ER-specific glycobiology
  • Golgy-specific glycobiology
  • Glycan-based cell differentiation and development
  • Glycan antigens in stem cells
  • Sialyl antigen–Lectin, Galectin, Siglec
  • Sugar–receptor interaction
  • Innate immunity
  • Xenotransplantation
  • Influenza virus and sialic acid receptors
  • Sialic acids mimetics as drug design

Prof. Dr. Cheorl-Ho Kim
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 papers will be 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 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 1800 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

  • Glycobiology
  • N-/O-glycan
  • Glycosphingolipid;
  • Glycoprotein;
  • Ganglioside
  • Surface Glycan
  • Lectin
  • Galectin
  • Siglec
  • ER–Golgi network
  • Glycan–receptor interaction
  • Innate Immunity
  • Xenotransplantation
  • Cell–cell interaction
  • Influenza virus sialic acid receptors

Published Papers (3 papers)

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Research

Open AccessArticle Receptor-Like Kinase LYK9 in Pisum sativum L. Is the CERK1-Like Receptor that Controls Both Plant Immunity and AM Symbiosis Development
Int. J. Mol. Sci. 2018, 19(1), 8; https://doi.org/10.3390/ijms19010008
Received: 28 November 2017 / Revised: 13 December 2017 / Accepted: 16 December 2017 / Published: 21 December 2017
Cited by 4 | PDF Full-text (3160 KB) | HTML Full-text | XML Full-text | Supplementary Files
Abstract
Plants are able to discriminate and respond to structurally related chitooligosaccharide (CO) signals from pathogenic and symbiotic fungi. In model plants Arabidopsis thaliana and Oryza sativa LysM-receptor like kinases (LysM-RLK) AtCERK1 and OsCERK1 (chitin elicitor receptor kinase 1) were shown to be involved
[...] Read more.
Plants are able to discriminate and respond to structurally related chitooligosaccharide (CO) signals from pathogenic and symbiotic fungi. In model plants Arabidopsis thaliana and Oryza sativa LysM-receptor like kinases (LysM-RLK) AtCERK1 and OsCERK1 (chitin elicitor receptor kinase 1) were shown to be involved in response to CO signals. Based on phylogenetic analysis, the pea Pisum sativum L. LysM-RLK PsLYK9 was chosen as a possible candidate given its role on the CERK1-like receptor. The knockdown regulation of the PsLyk9 gene by RNA interference led to increased susceptibility to fungal pathogen Fusarium culmorum. Transcript levels of PsPAL2, PsPR10 defense-response genes were significantly reduced in PsLyk9 RNAi roots. PsLYK9’s involvement in recognizing short-chain COs as most numerous signals of arbuscular mycorrhizal (AM) fungi, was also evaluated. In transgenic roots with PsLyk9 knockdown treated with short-chain CO5, downregulation of AM symbiosis marker genes (PsDELLA3, PsNSP2, PsDWARF27) was observed. These results clearly indicate that PsLYK9 appears to be involved in the perception of COs and subsequent signal transduction in pea roots. It allows us to conclude that PsLYK9 is the most likely CERK1-like receptor in pea to be involved in the control of plant immunity and AM symbiosis formation. Full article
(This article belongs to the Special Issue Glycan–Receptor Interaction 2018)
Figures

Graphical abstract

Open AccessArticle Glycoprotein 90K Promotes E-Cadherin Degradation in a Cell Density-Dependent Manner via Dissociation of E-Cadherin–p120-Catenin Complex
Int. J. Mol. Sci. 2017, 18(12), 2601; https://doi.org/10.3390/ijms18122601
Received: 14 October 2017 / Revised: 23 November 2017 / Accepted: 28 November 2017 / Published: 2 December 2017
Cited by 3 | PDF Full-text (5935 KB) | HTML Full-text | XML Full-text | Supplementary Files
Abstract
Glycoprotein 90K (also known as LGALS3BP or Mac-2BP) is a tumor-associated protein, and high 90K levels are associated with poor prognosis in some cancers. To clarify the role of 90K as an indicator for poor prognosis and metastasis in epithelial cancers, the present
[...] Read more.
Glycoprotein 90K (also known as LGALS3BP or Mac-2BP) is a tumor-associated protein, and high 90K levels are associated with poor prognosis in some cancers. To clarify the role of 90K as an indicator for poor prognosis and metastasis in epithelial cancers, the present study investigated the effect of 90K on an adherens junctional protein, E-cadherin, which is frequently absent or downregulated in human epithelial cancers. Treatment of certain cancer cells with 90K significantly reduced E-cadherin levels in a cell-population-dependent manner, and these cells showed decreases in cell adhesion and increases in invasive cell motility. Mechanistically, 90K-induced E-cadherin downregulation occurred via ubiquitination-mediated proteasomal degradation. 90K interacted with the E-cadherin–p120-catenin complex and induced its dissociation, altering the phosphorylation status of p120-catenin, whereas it did not associate with β-catenin. In subconfluent cells, 90K decreased membrane-localized p120-catenin and the membrane fraction of the p120-catenin. Particularly, 90K-induced E-cadherin downregulation was diminished in p120-catenin knocked-down cells. Taken together, 90K upregulation promotes the dissociation of the E-cadherin–p120-catenin complex, leading to E-cadherin proteasomal degradation, and thereby destabilizing adherens junctions in less confluent tumor cells. Our results provide a potential mechanism to explain the poor prognosis of cancer patients with high serum 90K levels. Full article
(This article belongs to the Special Issue Glycan–Receptor Interaction 2018)
Figures

Figure 1

Open AccessArticle Conditioned Medium from Malignant Breast Cancer Cells Induces an EMT-Like Phenotype and an Altered N-Glycan Profile in Normal Epithelial MCF10A Cells
Int. J. Mol. Sci. 2017, 18(8), 1528; https://doi.org/10.3390/ijms18081528
Received: 24 May 2017 / Revised: 11 July 2017 / Accepted: 12 July 2017 / Published: 1 August 2017
Cited by 4 | PDF Full-text (9290 KB) | HTML Full-text | XML Full-text | Supplementary Files
Abstract
Epithelial-mesenchymal transition (EMT) is a key process in cancer development and progression. Communication (crosstalk) between cancer cells and normal (nonmalignant) cells may facilitate cancer progression. Conditioned medium (CM) obtained from cultured cancer cells contains secreted factors capable of affecting phenotypes and the behaviors
[...] Read more.
Epithelial-mesenchymal transition (EMT) is a key process in cancer development and progression. Communication (crosstalk) between cancer cells and normal (nonmalignant) cells may facilitate cancer progression. Conditioned medium (CM) obtained from cultured cancer cells contains secreted factors capable of affecting phenotypes and the behaviors of normal cells. In this study, a culture of normal breast epithelial MCF10A cells with CM from malignant breast cancer cells (termed 231-CM and 453-CM) resulted in an alteration of morphology. CM-treated MCF10A, in comparison with control cells, showed a reduced expression of the epithelial marker E-cadherin, increased expression of the mesenchymal markers fibronectin, vimentin, N-cadherin, and TWIST1, meanwhile cell proliferation and migration were enhanced while cell apoptosis was decreased. N-glycan profiles of 231-CM-treated and control MCF10A cells were compared by MALDI-TOF/TOF-MS (Matrix-Assisted Laser Desorption/ Ionization Time of Flight Mass Spectrometry) and a lectin microarray analysis. The treated cells showed lower levels of high-mannose-type N-glycan structures, and higher levels of complex-type and hybrid-type structures. Altered N-glycan profiles were also detected in 453-CM-treated and non-treated MCF10A cells by MALDI-TOF/TOF-MS, and we found that the expression of five fucosylated N-glycan structures (m/z 1406.663, 1590.471, 1668.782, 2421.141, and 2988.342) and one high-mannose structure m/z 1743.722 have the same pattern as 231-CM-treated MCF10A cells. Our findings, taken together, show that CM derived from breast cancer cells induced an EMT-like process in normal epithelial cells and altered their N-glycan profile. Full article
(This article belongs to the Special Issue Glycan–Receptor Interaction 2018)
Figures

Graphical abstract

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