ArticleGlycoconjugate journal2014
The in situ distribution of glycoprotein-bound 4-O-Acetylated sialic acids in vertebrates.
Article in Glycoconjugate journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 23 citations in OpenAlex.
- The Sialome of the Retina, Alteration in Age-Related Macular Degeneration Pathology, and Potential Impacts on Complement Factor H.Investigative ophthalmology & visual science · 2025Article
- Extended receptor repertoire of an adenovirus associated with human obesity.PLoS pathogens · 2025Article
- Sialic acid O-acetylation patterns and glycosidic linkage type determination by ion mobility-mass spectrometry.Nature communications · 2023Article
- Changes in the levels of free sialic acid during ex vivo lung perfusion do not correlate with pulmonary function. Experimental model.BMC pulmonary medicine · 2023Article
- Article
- Endothelial Cells in Emerging Viral Infections.Frontiers in cardiovascular medicine · 2021Review
- SARS-CoV-2 Evolutionary Adaptation toward Host Entry and Recognition of Receptor O-Acetyl Sialylation in Virus-Host Interaction.International journal of molecular sciences · 2020Review
- Modified Sialic Acids on Mucus and Erythrocytes Inhibit Influenza A Virus Hemagglutinin and Neuraminidase Functions.Journal of virology · 2020Article
- Review
- Sialic acids regulate microvessel permeability, revealed by novel in vivo studies of endothelial glycocalyx structure and function.The Journal of physiology · 2017Article
- Effects of Sialic Acid Modifications on Virus Binding and Infection.Trends in microbiology · 2016Review
- Complexity and Diversity of the Mammalian Sialome Revealed by Nidovirus Virolectins.Cell reports · 2015Article
- Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Sialic acids are located at the terminal branches of the cell glycocalyx and secreted glycan molecules. O-Acetylation is an important modification of the sialic acids, however very few studies have demonstrated the in situ distribution of the O-Acetylated sialic acids. Here the distribution of glycoprotein bound 4-O-Acetylated sialic acids (4-O-Ac sias) in vertebrates was determined using a novel virus histochemistry assay. The 4-O-Ac sias were found in the circulatory system, i.e. on the surface of endothelial cells and RBCs, of several vertebrate species, though most frequently in the cartilaginous fish (class Chondrichthyes) and the bony fish (class Osteichthyes). The O-Acetylated sialic acid was detected in 64 % of the examined fish species. Even though the sialic acid was found less commonly in higher vertebrates, it was found at the same location in the positive species. The general significance of this endothelial labelling pattern distribution is discussed. The seemingly conserved local position through the evolution of the vertebrates, suggests an evolutionary advantage of this sialic acid modification.
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