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The in situ distribution of glycoprotein-bound 4-O-Acetylated sialic acids in vertebrates

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 glyco...

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Autores principales: Aamelfot, Maria, Dale, Ole Bendik, Weli, Simon Chioma, Koppang, Erling Olaf, Falk, Knut
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer US 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7088174/
https://www.ncbi.nlm.nih.gov/pubmed/24833039
http://dx.doi.org/10.1007/s10719-014-9529-7
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author Aamelfot, Maria
Dale, Ole Bendik
Weli, Simon Chioma
Koppang, Erling Olaf
Falk, Knut
author_facet Aamelfot, Maria
Dale, Ole Bendik
Weli, Simon Chioma
Koppang, Erling Olaf
Falk, Knut
author_sort Aamelfot, Maria
collection PubMed
description 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. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1007/s10719-014-9529-7) contains supplementary material, which is available to authorized users.
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spelling pubmed-70881742020-03-23 The in situ distribution of glycoprotein-bound 4-O-Acetylated sialic acids in vertebrates Aamelfot, Maria Dale, Ole Bendik Weli, Simon Chioma Koppang, Erling Olaf Falk, Knut Glycoconj J Article 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. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1007/s10719-014-9529-7) contains supplementary material, which is available to authorized users. Springer US 2014-05-16 2014 /pmc/articles/PMC7088174/ /pubmed/24833039 http://dx.doi.org/10.1007/s10719-014-9529-7 Text en © Springer Science+Business Media New York 2014 This article is made available via the PMC Open Access Subset for unrestricted research re-use and secondary analysis in any form or by any means with acknowledgement of the original source. These permissions are granted for the duration of the World Health Organization (WHO) declaration of COVID-19 as a global pandemic.
spellingShingle Article
Aamelfot, Maria
Dale, Ole Bendik
Weli, Simon Chioma
Koppang, Erling Olaf
Falk, Knut
The in situ distribution of glycoprotein-bound 4-O-Acetylated sialic acids in vertebrates
title The in situ distribution of glycoprotein-bound 4-O-Acetylated sialic acids in vertebrates
title_full The in situ distribution of glycoprotein-bound 4-O-Acetylated sialic acids in vertebrates
title_fullStr The in situ distribution of glycoprotein-bound 4-O-Acetylated sialic acids in vertebrates
title_full_unstemmed The in situ distribution of glycoprotein-bound 4-O-Acetylated sialic acids in vertebrates
title_short The in situ distribution of glycoprotein-bound 4-O-Acetylated sialic acids in vertebrates
title_sort in situ distribution of glycoprotein-bound 4-o-acetylated sialic acids in vertebrates
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7088174/
https://www.ncbi.nlm.nih.gov/pubmed/24833039
http://dx.doi.org/10.1007/s10719-014-9529-7
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