Homogeneous Human Complex-Type Oligosaccharides in Correctly Folded Intact Glycoproteins: Evaluation of Oligosaccharide Influence On Protein Folding, Stability, and Conformational Properties

2012 ◽  
Vol 18 (19) ◽  
pp. 5944-5953 ◽  
Author(s):  
Yasuhiro Kajihara ◽  
Yasutaka Tanabe ◽  
Shun Sasaoka ◽  
Ryo Okamoto
Keyword(s):  
Protein Folding ◽  
Complex Type ◽  
Conformational Properties ◽  
Human Complex

scholarly journals Cytosolic Free N-Glycans Are Retro-Transported Into the Endoplasmic Reticulum in Plant Cells

2021 ◽  
Vol 11 ◽  
Author(s):  
Makoto Katsube ◽  
Natsuki Ebara ◽  
Megumi Maeda ◽  
Yoshinobu Kimura
Keyword(s):  
Endoplasmic Reticulum ◽  
Protein Folding ◽  
Golgi Apparatus ◽  
Plant Cells ◽  
Complex Type ◽  
Secretion Pathway ◽  
Amyloid Fibril Formation ◽  
Free Oligosaccharides ◽  
Β Amyloid ◽  
Protein Secretion Pathway

During endoplasmic reticulum (ER)-associated degradation, free N-glycans (FNGs) are produced from misfolded nascent glycoproteins via the combination of the cytosolic peptide N-glycanase (cPNGase) and endo-β-N-acetylglucosaminidase (ENGase) in the plant cytosol. The resulting high-mannose type (HMT)-FNGs, which carry one GlcNAc residue at the reducing end (GN1-FNGs), are ubiquitously found in developing plant cells. In a previous study, we found that HMT-FNGs assisted in protein folding and inhibited β-amyloid fibril formation, suggesting a possible biofunction of FNGs involved in the protein folding system. However, whether these HMT-FNGs occur in the ER, an organelle involved in protein folding, remained unclear. On the contrary, we also reported the presence of plant complex type (PCT)-GN1-FNGs, which carry the Lewisa epitope at the non-reducing end, indicating that these FNGs had been fully processed in the Golgi apparatus. Since plant ENGase was active toward HMT-N-glycans but not PCT-N-glycans that carry β1-2xylosyl and/or α1-3 fucosyl residue(s), these PCT-GN1-FNGs did not appear to be produced from fully processed glycoproteins that harbored PCT-N-glycans via ENGase activity. Interestingly, PCT-GN1-FNGs were found in the extracellular space, suggesting that HMT-GN1-FNGs formed in the cytosol might be transported back to the ER and processed in the Golgi apparatus through the protein secretion pathway. As the first step in elucidating the production mechanism of PCT-GN1-FNGs, we analyzed the structures of free oligosaccharides in plant microsomes and proved that HMT-FNGs (Man9-7GlcNAc1 and Man9-8GlcNAc2) could be found in microsomes, which almost consist of the ER compartments.

Effect of Bisecting GlcNAc and Core Fucosylation on Conformational Properties of Biantennary Complex-Type N-Glycans in Solution

2012 ◽  
Vol 116 (29) ◽  
pp. 8504-8512 ◽  
Author(s):  
Wataru Nishima ◽  
Naoyuki Miyashita ◽  
Yoshiki Yamaguchi ◽  
Yuji Sugita ◽  
Suyong Re
Keyword(s):  
Complex Type ◽  
Conformational Properties ◽  
Core Fucosylation ◽  
Bisecting Glcnac

Chemical Synthesis of a Glycoprotein Having an Intact Human Complex-Type Sialyloligosaccharide under the Boc and Fmoc Synthetic Strategies

2008 ◽  
Vol 130 (2) ◽  
pp. 501-510 ◽  
Author(s):  
Naoki Yamamoto ◽  
Yasutaka Tanabe ◽  
Ryo Okamoto ◽  
Philip E. Dawson ◽  
Yasuhiro Kajihara
Keyword(s):  
Chemical Synthesis ◽  
Complex Type ◽  
Human Complex

scholarly journals Constructing a human complex type N-linked glycosylation pathway in Kluyveromyces marxianus

PLoS ONE ◽  
2020 ◽  
Vol 15 (5) ◽  
pp. e0233492
Author(s):  
Ming-Hsuan Lee ◽  
Tsui-Ling Hsu ◽  
Jinn-Jy Lin ◽  
Yu-Ju Lin ◽  
Yi-Ying Kao ◽  
...  
Keyword(s):  
Kluyveromyces Marxianus ◽  
Complex Type ◽  
Glycosylation Pathway ◽  
Human Complex

PROTEINS AND RANDOM HETEROPOLYMERS: AN OVERVIEW

1992 ◽  
Vol 03 (supp01) ◽  
pp. 201-207
Author(s):  
GIULIA IORI
Keyword(s):  
Protein Folding ◽  
External Perturbation ◽  
Experimental Results ◽  
Stable Configuration ◽  
Zero Temperature ◽  
Normal Oscillation ◽  
Oscillation Modes ◽  
Conformational Properties

We present a brief review of the main analytical and experimental results on the problem of protein folding. We will then discuss the conformational properties of the IMP model for an heteropolymeric chain at low and zero temperature. Finally we will analyze the dynamical relaxation of this system subject to the action of an external perturbation and we will discuss the localization of the normal oscillation modes around one stable configuration.

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