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Glycome and Nervous System
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Glycome and Nervous System

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

Deadline for manuscript submissions: closed (31 August 2022) | Viewed by 14743

Special Issue Editors

Prof. Dr. Naoyuki Taniguchi

E-Mail Website
Guest Editor
Department of Glyco-Oncology and Medical Biochemistry, Osaka International Cancer Institute, 3-1-69 Otemae, Chuo-ku, Osaka 541-8567, Japan
Interests: glycobiology and disease implication; glycosyltransferases involved in N-linked glycans; reactive oxygen species; glutathione metabolism
Special Issues, Collections and Topics in MDPI journals
Prof. Dr. Shinobu Kitazume

E-Mail Website
Guest Editor
Department of Clinical Laboratory Sciences, School of Health Sciences, Fukushima Medical University, Fukushima 960-8516, Japan
Interests: glycoscience in brain and brain-related diseases; sialic acid biosynthesis; biomarker discovery; Alzheimer’s disease, glioma, platelet biology
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear colleagues,

More than 70 % of proteins are modified with glycans; N-linked glycosylation to Asn residues, and O-linked glycosylation to Ser or Thr residues. In the brain, several adhesion molecules and receptor proteins are modified with specific glycans and these glycans play important roles for high-order brain function. a2,8-Linked polysialic acid (polySia) is found in the N-linked glycans of neural cell adhesion molecule, N-CAM, and is involved in cell-cell interaction during neural development and plasticity. Genome-wide association study shows that genetic variation of the polysialyltransferase gene associates with mental disorder. HNK-1 epitope is predominantly expressed in the brains, modifies the N-linked glycans of several neural proteins, such as myelin-associated glycoprotein (MAG), L1, and glutamate receptor, and has critical role for synaptic plasticity, spatial learning, and memory. Brain-specific b1,6-GlcNAc-branched O-mannosyl glycans decorate protein tyrosine phosphatase Z (PTPRZ), which is expressed in astrocytes and oligodendrocyte precursor cells. PTPRZ expression is markedly increased in brain tumors, and its shedding form in cerebrospinal fluid (CSF) is a promising diagnostic marker for glioma. In this Special Issue, we would explore how Nerve-specific glycans carry out their roles in neural development as well as interaction of nervous system and tumor environment.

Prof. Dr. Naoyuki Taniguchi
Prof. Dr. Shinobu Kitazume
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.

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Keywords

  • Polysialic acid
  • HNK-1
  • O-mannose glycan
  • glycosylatransferases
  • neural activity
  • Alzheimer’s disease
  • neural development
  • psychiatric disease
  • glioma

Published Papers (5 papers)

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Research

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15 pages, 3091 KiB  
Article
Polysialylation in a DISC1 Mutant Mouse
by Yuka Takahashi, Chikara Abe, Masaya Hane, Di Wu, Ken Kitajima and Chihiro Sato
Int. J. Mol. Sci. 2022, 23(9), 5207; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms23095207 - 06 May 2022
Cited by 3 | Viewed by 1920
Abstract
Schizophrenia is a serious psychiatric disorder that affects the social life of patients. Psychiatric disorders are caused by a complex combination of genetic (G) and environmental (E) factors. Polysialylation represents a unique posttranslational modification of a protein, and such changes in neural cell [...] Read more.
Schizophrenia is a serious psychiatric disorder that affects the social life of patients. Psychiatric disorders are caused by a complex combination of genetic (G) and environmental (E) factors. Polysialylation represents a unique posttranslational modification of a protein, and such changes in neural cell adhesion molecules (NCAMs) have been reported in postmortem brains from patients with psychiatric disorders. To understand the G × E effect on polysialylated NCAM expression, in this study, we performed precise measurements of polySia and NCAM using a disrupted-in-schizophrenia 1 (DISC1)-mutant mouse (G), a mouse model of schizophrenia, under acute stress conditions (E). This is the first study to reveal a lower number and smaller length of polySia in the suprachiasmatic nucleus of DISC1 mutants relative to those in wild-type (WT) mice. In addition, an analysis of polySia and NCAM responses to acute stress in five brain regions (olfactory bulb, prefrontal cortex, suprachiasmatic nucleus, amygdala, and hippocampus) revealed that the pattern of changes in these responses in WT mice and DISC1 mutants differed by region. These differences could indicate the vulnerability of DISC1 mutants to stress. Full article
(This article belongs to the Special Issue Glycome and Nervous System)
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16 pages, 2835 KiB  
Article
Peptide Sequence Mapping around Bisecting GlcNAc-Bearing N-Glycans in Mouse Brain
by Yuki Ohkawa, Yasuhiko Kizuka, Misaki Takata, Miyako Nakano, Emi Ito, Sushil K. Mishra, Haruna Akatsuka, Yoichiro Harada and Naoyuki Taniguchi
Int. J. Mol. Sci. 2021, 22(16), 8579; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms22168579 - 09 Aug 2021
Cited by 4 | Viewed by 3175
Abstract
N-glycosylation is essential for many biological processes in mammals. A variety of N-glycan structures exist, of which, the formation of bisecting N-acetylglucosamine (GlcNAc) is catalyzed by N-acetylglucosaminyltransferase-III (GnT-III, encoded by the Mgat3 gene). We previously identified various bisecting GlcNAc-modified [...] Read more.
N-glycosylation is essential for many biological processes in mammals. A variety of N-glycan structures exist, of which, the formation of bisecting N-acetylglucosamine (GlcNAc) is catalyzed by N-acetylglucosaminyltransferase-III (GnT-III, encoded by the Mgat3 gene). We previously identified various bisecting GlcNAc-modified proteins involved in Alzheimer’s disease and cancer. However, the mechanisms by which GnT-III acts on the target proteins are unknown. Here, we performed comparative glycoproteomic analyses using brain membranes of wild type (WT) and Mgat3-deficient mice. Target glycoproteins of GnT-III were enriched with E4-phytohemagglutinin (PHA) lectin, which recognizes bisecting GlcNAc, and analyzed by liquid chromatograph-mass spectrometry. We identified 32 N-glycosylation sites (Asn-Xaa-Ser/Thr, Xaa ≠ Pro) that were modified with bisecting GlcNAc. Sequence alignment of identified N-glycosylation sites that displayed bisecting GlcNAc suggested that GnT-III does not recognize a specific primary amino acid sequence. The molecular modeling of GluA1 as one of the good cell surface substrates for GnT-III in the brain, indicated that GnT-III acts on N-glycosylation sites located in a highly flexible and mobile loop of GluA1. These results suggest that the action of GnT-III is partially affected by the tertiary structure of target proteins, which can accommodate bisecting GlcNAc that generates a bulky flipped-back conformation of the modified glycans. Full article
(This article belongs to the Special Issue Glycome and Nervous System)
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Review

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11 pages, 931 KiB  
Review
Ganglioside GM3 Synthase Deficiency in Mouse Models and Human Patients
by Kei-ichiro Inamori and Jin-ichi Inokuchi
Int. J. Mol. Sci. 2022, 23(10), 5368; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms23105368 - 11 May 2022
Cited by 5 | Viewed by 2578
Abstract
Gangliosides (glycosphingolipids containing one or more sialic acids) are highly expressed in neural tissues in vertebrates, and four species (GM1a, GD1a, GD1b, GT1b) are predominant in mammalian brains. GM3 is the precursor of each of these four species and is the major ganglioside [...] Read more.
Gangliosides (glycosphingolipids containing one or more sialic acids) are highly expressed in neural tissues in vertebrates, and four species (GM1a, GD1a, GD1b, GT1b) are predominant in mammalian brains. GM3 is the precursor of each of these four species and is the major ganglioside in many nonneural tissues. GM3 synthase (GM3S), encoded by ST3GAL5 gene in humans, is a sialyltransferase responsible for synthesis of GM3 from its precursor, lactosylceramide. ST3GAL5 mutations cause an autosomal recessive form of severe infantile-onset neurological disease characterized by progressive microcephaly, intellectual disability, dyskinetic movements, blindness, deafness, intractable seizures, and pigment changes. Some of these clinical features are consistently present in patients with ST3GAL5 mutations, whereas others have variable expression. GM3S knockout (KO) mice have deafness and enhanced insulin sensitivity, but otherwise do not display the above-described neurological defects reported in ST3GAL5 patients. The authors present an overview of physiological functions and pathological aspects of gangliosides based on findings from studies of GM3S KO mice and discuss differential phenotypes of GM3S KO mice versus human GM3S-deficiency patients. Full article
(This article belongs to the Special Issue Glycome and Nervous System)
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11 pages, 1314 KiB  
Review
Protein Tyrosine Phosphatase Receptor Type Z in Central Nervous System Disease
by Kenichiro Nagai, Masazumi Fujii and Shinobu Kitazume
Int. J. Mol. Sci. 2022, 23(8), 4414; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms23084414 - 16 Apr 2022
Cited by 8 | Viewed by 2895
Abstract
Gliomas are among the most common tumors of the central nervous system and include highly malignant subtypes, such as glioblastoma, which are associated with poor prognosis. Effective treatments are therefore urgently needed. Despite the recent advances in neuroimaging technologies, differentiating gliomas from other [...] Read more.
Gliomas are among the most common tumors of the central nervous system and include highly malignant subtypes, such as glioblastoma, which are associated with poor prognosis. Effective treatments are therefore urgently needed. Despite the recent advances in neuroimaging technologies, differentiating gliomas from other brain diseases such as multiple sclerosis remains challenging in some patients, and often requires invasive brain biopsy. Protein tyrosine phosphatase receptor type Z (PTPRZ) is a heavily glycosylated membrane protein that is highly expressed in the central nervous system. Several reports analyzing mouse tumor models suggest that PTPRZ may have potential as a therapeutic target for gliomas. A soluble cleaved form of PTPRZ (sPTPRZ) in the cerebrospinal fluid is markedly upregulated in glioma patients, making it another promising diagnostic biomarker. Intriguingly, PTPRZ is also involved in the process of remyelination in multiple sclerosis. Indeed, lowered PTPRZ glycosylation by deletion of the glycosyltransferase gene leads to reduced astrogliosis and enhanced remyelination in mouse models of demyelination. Here, we review the expression, molecular structure, and biological roles of PTPRZ. We also discuss glioma and demyelinating diseases, as well as the pathological role of PTPRZ and its application as a diagnostic marker and therapeutic target. Full article
(This article belongs to the Special Issue Glycome and Nervous System)
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21 pages, 1145 KiB  
Review
Galectins as Emerging Glyco-Checkpoints and Therapeutic Targets in Glioblastoma
by Guillermo A. Videla-Richardson, Olivia Morris-Hanon, Nicolás I. Torres, Myrian I. Esquivel, Mariana B. Vera, Luisina B. Ripari, Diego O. Croci, Gustavo E. Sevlever and Gabriel A. Rabinovich
Int. J. Mol. Sci. 2022, 23(1), 316; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms23010316 - 28 Dec 2021
Cited by 11 | Viewed by 3272
Abstract
Despite recent advances in diagnosis and treatment, glioblastoma (GBM) represents the most common and aggressive brain tumor in the adult population, urging identification of new rational therapeutic targets. Galectins, a family of glycan-binding proteins, are highly expressed in the tumor microenvironment (TME) and [...] Read more.
Despite recent advances in diagnosis and treatment, glioblastoma (GBM) represents the most common and aggressive brain tumor in the adult population, urging identification of new rational therapeutic targets. Galectins, a family of glycan-binding proteins, are highly expressed in the tumor microenvironment (TME) and delineate prognosis and clinical outcome in patients with GBM. These endogenous lectins play key roles in different hallmarks of cancer by modulating tumor cell proliferation, oncogenic signaling, migration, vascularization and immunity. Additionally, they have emerged as mediators of resistance to different anticancer treatments, including chemotherapy, radiotherapy, immunotherapy, and antiangiogenic therapy. Particularly in GBM, galectins control tumor cell transformation and proliferation, reprogram tumor cell migration and invasion, promote vascularization, modulate cell death pathways, and shape the tumor-immune landscape by targeting myeloid, natural killer (NK), and CD8+ T cell compartments. Here, we discuss the role of galectins, particularly galectin-1, -3, -8, and -9, as emerging glyco-checkpoints that control different mechanisms associated with GBM progression, and discuss possible therapeutic opportunities based on inhibition of galectin-driven circuits, either alone or in combination with other treatment modalities. Full article
(This article belongs to the Special Issue Glycome and Nervous System)
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