Polysialic acid: A veteran sugar with a new site of action in the brain

Giza, Joanna; Biederer, Thomas

doi:10.1073/pnas.1005637107

Cited by 8 publications

(4 citation statements)

References 14 publications

(13 reference statements)

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“…In particular, sialylation plays a crucial role in the nervous system. It has been shown that sialoglycoproteins participate neuronal outgrowth, neuroprotective response, synaptic connectivity, and memory formation via mediating cell‐cell interactions and binding to the extracellular matrix . Sialic acids protect cells from membrane proteolysis, and mediate cell adhesion, cell surface interactions and cell differentiation .…”

Section: Introductionmentioning

confidence: 99%

“…It has been shown that sialoglycoproteins participate neuronal outgrowth, neuroprotective response, synaptic connectivity, and memory formation via mediating cell-cell interactions and binding to the extracellular matrix. 24,29,30 Sialic acids protect cells from membrane proteolysis, and mediate cell adhesion, cell surface interactions and cell differentiation. 20,27 Sialylation can affect absorption, serum half-life, and antiinflammatory activity of therapeutic glycoproteins.…”

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confidence: 99%

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Mass spectrometry for protein sialoglycosylation

Zhang

Wang

et al. 2017

Mass Spectrometry Reviews

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Sialic acids are a family of structurally unique and negatively charged nine-carbon sugars, normally found at the terminal positions of glycan chains on glycoproteins and glycolipids. The glycosylation of proteins is a universal post-translational modification in eukaryotic species and regulates essential biological functions, in which the most common sialic acid is N-acetyl-neuraminic acid (2-keto-5-acetamido-3,5-dideoxy-D-glycero-D-galactononulopyranos-1-onic acid) (Neu5NAc). Because of the properties of sialic acids under general mass spectrometry (MS) conditions, such as instability, ionization discrimination, and mixed adducts, the use of MS in the analysis of protein sialoglycosylation is still challenging. The present review is focused on the application of MS related methodologies to the study of both N- and O-linked sialoglycans. We reviewed MS-based strategies for characterizing sialylation by analyzing intact glycoproteins, proteolytic digested glycopeptides, and released glycans. The review concludes with future perspectives in the field.

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Section: Introductionmentioning

confidence: 99%

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confidence: 99%

Mass spectrometry for protein sialoglycosylation

Zhang

Wang

et al. 2017

Mass Spectrometry Reviews

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“…The sialic acid family shares the common feature of a nine-carbon backbone and a carboxylic acid residue. They play a variety of physiologically important roles, including intercellular and intermolecular interactions, neuronal outgrowth and memory formation, function of extracellular matrix, binding of viruses and microorganisms, and cancer development. − Modifications at the C5 position determine the primary sialic acid forms, including N -acetylneuraminic acid (NeuAc), N -glycolylneuraminic acid (NeuGc), and 2-keto-3-deoxynononic acid (KDN) . Further modification with the addition of O -acetyl, O -sulfo, O -lactyl, and/or O -methyl groups is found at the hydroxyl groups at the C4, C7, C8, and/or C9 position .…”

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confidence: 99%

Analysis of O-Acetylated Sialic Acids in Dried Blood Spots

et al. 2019

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Sialic acid is a family of N-and O-substitutions of neuraminic acid. Plasma or serum sialic acid has been established as a potential disease marker. For example, the presence of 9-O-acetyl on the sialic acid of some glycans and glycoconjugates (e.g., 9-O-acetyl GD3 ganglioside) could be related to cancer occurrence. A variety of assays are available to measure serum or plasma sialic acid; however, sample preparation and storage can alter the O-acetylation profile due to the loss of O-acetyl groups and/or the migration of Oacetyl groups. Herein, we report dried blood spot (DBS) sampling, in combination with diamino-4,5-methylenedioxybenzene derivatization, for profiling sialic acids in blood samples with minimal alteration in O-acetylation patterns. The feasibility of the method was first evaluated by analyzing sialic acids in crucian carp blood and comparing with traditional blood/ plasma sample preparation procedures. A total of 19 different sialic acids were identified by using liquid chromatography− Orbitrap mass spectrometry, including four mono-O-acetylated N-acetylneuraminic acids, four mono-O-acetylated Nglycolylneuraminic acids, six di-O-acetylated N-acetylneuraminic acids, and three tri-O-acetylated N-acetylneuraminic acids. The long-term storage study indicated that DBS sampling could effectively preserve the O-acetylation information for at least 6 weeks. Thus, it is demonstrated that this method is a valuable tool for the study of sialic acid diversity, especially for the characterization of isomeric structures.

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“…). Similar to NCAM, the polysialylation of SynCAM 1 is down‐regulated during post‐natal developmental stages (Giza and Biederer ; Rollenhagen et al . ).…”

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confidence: 99%

Polysialic acid as an antigen for monoclonal antibody HIgM12 to treat multiple sclerosis and other neurodegenerative disorders

Watzlawik

Kahoud

et al. 2015

Journal of Neurochemistry

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CNS regeneration is a desirable goal for diseases of brain and spinal cord. Current therapeutic strategies for the treatment of multiple sclerosis (MS) aim to eliminate detrimental effects of the immune system, so far without reversing disability or affecting long-term prognosis in patients. Approachable molecular targets that stimulate CNS repair are not part of the clinical praxis or have not been identified yet. The purpose of this study was to identify the molecular target of the human monoclonal antibody HIgM12. HIgM12 reverses motor deficits in chronically demyelinated mice, a model of MS. Here we identified polysialic acid (PSA) attached to the Neural Cell Adhesion Molecule (NCAM) as the antigen for HIgM12 by using different NCAM knockout strains and through PSA removal from the NCAM protein core. Antibody binding to CNS tissue and primary cells, antibody-mediated cell adhesion and neurite outgrowth on HIgM12-coated nitrocellulose was detected only in the presence of PSA as assessed by Western blotting, immunoprecipitation, immunocytochemistry and histochemistry. We conclude that HIgM12 mediates it's in vivo and in vitro effects through binding to PSA and has the potential to be an effective therapy for MS and neurodegenerative diseases.

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Polysialic acid: A veteran sugar with a new site of action in the brain

Cited by 8 publications

References 14 publications

Mass spectrometry for protein sialoglycosylation

Mass spectrometry for protein sialoglycosylation

Analysis of O-Acetylated Sialic Acids in Dried Blood Spots

Polysialic acid as an antigen for monoclonal antibody HIgM12 to treat multiple sclerosis and other neurodegenerative disorders

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