Analyses of chicken sialyltransferases related to N-glycosylation

Kojima, Yoshitane; Mizutani, Akifumi; Okuzaki, Yuya; Nishijima, Ken ichi; Kaneoka, Hidenori; Sasamoto, Takako; Miyake, Katsuhide; Iijima, Shinji

doi:10.1016/j.jbiosc.2014.11.009

Cited by 5 publications

(1 citation statement)

References 22 publications

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“…Each family catalyzes the formation of different glycosidic linkages, α2–3, or α2–6 to the terminal Gal residue in N - or O -glycans, α2–6 to the terminal GalNAc residue in O -glycans and glycolipids and α2–8 to terminal SA residues in N - or O -glycans or glycolipids). The ST enzymatic activities have been documented mainly in mouse and human tissues and more recently in chicken [46,47], and to a lesser extent in the invertebrates like the fly D. melanogaster [48], the silkworm Bombyx mori [49], the amphioxus Branchiostoma floridae [1] and the tunicate C. intestinalis [5]. Each member of the mammalian ST3Gal and ST6Gal families shows exquisite acceptor specificities (for reviews, see [41,50,51].…”

Section: Introductionmentioning

confidence: 99%

Phylogenetic-Derived Insights into the Evolution of Sialylation in Eukaryotes: Comprehensive Analysis of Vertebrate β-Galactoside α2,3/6-Sialyltransferases (ST3Gal and ST6Gal)

Teppa

Petit

Plechakova

et al. 2016

IJMS

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Cell surface of eukaryotic cells is covered with a wide variety of sialylated molecules involved in diverse biological processes and taking part in cell–cell interactions. Although the physiological relevance of these sialylated glycoconjugates in vertebrates begins to be deciphered, the origin and evolution of the genetic machinery implicated in their biosynthetic pathway are poorly understood. Among the variety of actors involved in the sialylation machinery, sialyltransferases are key enzymes for the biosynthesis of sialylated molecules. This review focus on β-galactoside α2,3/6-sialyltransferases belonging to the ST3Gal and ST6Gal families. We propose here an outline of the evolutionary history of these two major ST families. Comparative genomics, molecular phylogeny and structural bioinformatics provided insights into the functional innovations in sialic acid metabolism and enabled to explore how ST-gene function evolved in vertebrates.

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Section: Introductionmentioning

confidence: 99%

Phylogenetic-Derived Insights into the Evolution of Sialylation in Eukaryotes: Comprehensive Analysis of Vertebrate β-Galactoside α2,3/6-Sialyltransferases (ST3Gal and ST6Gal)

Teppa

Petit

Plechakova

et al. 2016

IJMS

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Establishment and Characterization of a Novel Tissue-specific DNA Construct and Culture System with Potential for Avian Bioreactor Generation

Sáez

Bussmann

2019

Mol Biotechnol

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Analyses of chicken sialyltransferases related to O-glycosylation

Kidani

Kaneoka

Okuzaki

et al. 2016

Journal of Bioscience and Bioengineering

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The chicken β-galactoside α2,3-sialyltransferase 1, 2, and 5 (ST3Gal1, 2, and 5) genes were cloned, and their enzymes were expressed in 293FT cells. ST3Gal1 and 2 exhibited enzymatic activities toward galactose-β1,3-N-acetylgalactosamine and galactose-β1,3-N-acetylglucosamine. ST3Gal5 only exhibited activity toward lactosylceramide. ST3Gal1 and 2 and previously cloned ST3Gal3 and 6 transferred CMP-sialic acid to asialofetuin. Reverse-transcription-quantitative PCR indicated that ST3Gal1 was expressed at higher levels in the trachea, lung, spleen, and magnum, and the strong expression of ST3Gal5 was observed in the spleen, magnum, and small and large intestines. ST3Gal1, 5, and 6 were also expressed in the tubular gland cells of the magnum, which secretes egg-white proteins. ST3Gal1, 5, and 6 were expressed in the egg chorioallantoic membrane, in which influenza viruses are propagated for the production of vaccines.

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Analyses of chicken sialyltransferases related to N-glycosylation

Cited by 5 publications

References 22 publications

Phylogenetic-Derived Insights into the Evolution of Sialylation in Eukaryotes: Comprehensive Analysis of Vertebrate β-Galactoside α2,3/6-Sialyltransferases (ST3Gal and ST6Gal)

Phylogenetic-Derived Insights into the Evolution of Sialylation in Eukaryotes: Comprehensive Analysis of Vertebrate β-Galactoside α2,3/6-Sialyltransferases (ST3Gal and ST6Gal)

Establishment and Characterization of a Novel Tissue-specific DNA Construct and Culture System with Potential for Avian Bioreactor Generation

Analyses of chicken sialyltransferases related to O-glycosylation

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