“Three sources and three component parts” of free oligosaccharides

Pismenetskaya, I. U.; Butters, Terry D.

doi:10.15407/ubj86.06.005

Ukr.Biochem.J.

2014

DOI: 10.15407/ubj86.06.005

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“Three sources and three component parts” of free oligosaccharides

I. U. Pismenetskaya¹,

Terry D. Butters²

Abstract: abbreviations: BiP -immunoglobulin heavy-chain-binding protein; Derlin -degradation in endoplasmic reticulum protein; DnaJ -heat shock proteins with J-domain; EDEM -ER-degradation enhancing alpha-mannosidase like protein; ENGase -endo-β-N-acetylglucosaminidase; ERAD (ER-associated degradation) -endoplasmic reticulum-associated degradation; ERp57, ERp59, ERp72, ERp44 -disulfide-isomerase like proteins in ER; α-GII -α-glycosidase II; GM1, GM2 -monosialotetrahexosyl-gangliosides; GRP78 -glucose regulated protein;… Show more

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Cited by 2 publications

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“…The details of their formation in cells and precise structures from each source are well-known. FOS are also indentified in biological fluids [13]. Investigations of FOS in biological fluids have shown that their fractions specifically change in different diseases [14][15][16].…”

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Serum glycomarkers of endoplasmic reticulum and lysosomal-endosomal system stress in human healthy aging and diseases

Pismenetskaya¹,

Butters²

2017

Ukr.Biochem.J.

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To verify the idea that extracellular free oligosaccharides might be able to reflect the functional status of the endoplasmic reticulum (ER) and lysosomal-endosomal system, HPLC-profiles of serum-derived free oligosaccharides (FOS) in human healthyT he multilayered protein quality assurance system encompasses almost all cellular organelles, a network of biochemical processes and a multiplex of intracellular and extracellular signaling cascades [1][2][3][4][5]. At the centre of this wide cellular landscape there are two main hubs -the endoplasmic reticulum (ER) and lysosomal-endosomal system. The former is responsible for quality-reliable guarantee of newly synthesized proteins, the latterfor effective degradation of mature proteins, incorrectly folded proteins and their adducts.The endoplasmic reticulum provides an interconnected space for translation, co-translational and post-translational modifications, folding and assembling of secreted, organelle-targeted and membrane proteins. Only properly folded and assembled proteins can be transported out of the ER via the Golgi apparatus and cytosol to the endpoint of their functional actions -cellular organelles, plasma membrane and extracellular space. Native protein conformation is achieved due to unique environment of the ER lumen and a specific co-translational modification of proteins -N-glycosylation. The oxidation/ reductive conditions of the ER lumen ensure the formation of disulfide bonds maintaining the tertiary and quaternary structure of proteins. The high level of functional chaperone proteins in the ER facilitates protein folding. The high Ca 2+ concentration in the lumen is essential for Ca 2+ -dependent chaperonesprotein interactions. Any disturbance of these three determinants can lead to protein unfolding or misfolding [6].Cells monitor protein folding by a protein quali ty control (QC) system is inbuilt in the ER and

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Serum glycomarkers of endoplasmic reticulum and lysosomal-endosomal system stress in human healthy aging and diseases

Pismenetskaya¹,

Butters²

2017

Ukr.Biochem.J.

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Occurrence of free sialyl oligosaccharides related toN-glycans (sialyl freeN-glycans) in animal sera

et al. 2016

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Free oligosaccharides that are structurally related to N-glycans [free N-glycans (FNGs)] are widely distributed in the cytosol of animal cells. The diverse molecular mechanisms responsible for the formation of these FNGs have been well clarified. In this study we demonstrate the wide occurrence of sialylated FNGs in sera of various animals. The features of these extracellular FNGs are quite distinct from the cytosolic FNGs, as they are Gn2-type glycans, bearing an N,N'-diacetylchitobiose unit at their reducing termini, while the cytosolic FNGs are predominantly Gn1-type, with a single GlcNAc at their reducing termini. The major structures observed varied from species to species, and the structures of the FNGs appear to be correlated with the major sialyl N-glycans on serum glycoproteins, suggesting that the serum FNGs are produced by hepatocytes. Interestingly, glycan-profiles of the FNGs indicated that they are altered in a developmental stage-dependent manner. Sialyl FNGs in the sera may not only be of biological relevance, in that they might reflect the functionality of the liver, but also can be attractive sources for obtaining uniform sialyl FNGs in the chemoenzymatic synthesis of glycoproteins.

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“Three sources and three component parts” of free oligosaccharides

Cited by 2 publications

References 62 publications

Serum glycomarkers of endoplasmic reticulum and lysosomal-endosomal system stress in human healthy aging and diseases

Serum glycomarkers of endoplasmic reticulum and lysosomal-endosomal system stress in human healthy aging and diseases

Occurrence of free sialyl oligosaccharides related toN-glycans (sialyl freeN-glycans) in animal sera

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