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18 results on '"GAO Xiao-dong"'

5. Maca extracts regulate glucose and lipid metabolism in insulin‐resistant HepG2 cells via the PI3K/AKT signalling pathway

Author

Li, Aimin, primary, Liu, Jia, additional, Ding, Fangli, additional, Wu, Xiaolei, additional, Pan, Cong, additional, Wang, Qing, additional, Gao, Ming, additional, Duan, Shenglin, additional, Han, Xiaofeng, additional, Xia, Kai, additional, Liu, Shiwei, additional, Wu, Yimin, additional, Zhou, Zhiqiao, additional, Zhang, Xi, additional, and Gao, Xiao‐Dong, additional

Published
2021
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13. A Strategy for Neuraminidase Inhibitors Using Mechanism‐Based Labeling Information

Author

Hinou, Hiroshi, primary, Miyoshi, Risho, additional, Takasu, Yasuaki, additional, Kai, Hirokazu, additional, Kurogochi, Masaki, additional, Arioka, Shingo, additional, Gao, Xiao‐Dong, additional, Miura, Nobuaki, additional, Fujitani, Naoki, additional, Omoto, Shinya, additional, Yoshinaga, Tomokazu, additional, Fujiwara, Tamio, additional, Noshi, Takeshi, additional, Togame, Hiroko, additional, Takemoto, Hiroshi, additional, and Nishimura, Shin‐Ichiro, additional

Published
2011
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14. An Efficient Approach for the Characterization of Mucin-Type Glycopeptides: The Effect of O-Glycosylation on the Conformation of Synthetic Mucin Peptides

Author

Hashimoto, Ryo, primary, Fujitani, Naoki, additional, Takegawa, Yasuhiro, additional, Kurogochi, Masaki, additional, Matsushita, Takahiko, additional, Naruchi, Kentaro, additional, Ohyabu, Naoki, additional, Hinou, Hiroshi, additional, Gao, Xiao Dong, additional, Manri, Naomi, additional, Satake, Hiroyuki, additional, Kaneko, Akihito, additional, Sakamoto, Takeshi, additional, and Nishimura, Shin-Ichiro, additional

Published
2011
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17. PER1, GUP1 and CWH43 of methylotrophic yeast Ogataea minuta are involved in cell wall integrity.

Author

Xu XX, Komatsuzaki A, Chiba Y, Gao XD, and Yoko-O T

Subjects
Amino Acid Sequence, Cell Wall chemistry, Fungal Proteins genetics, Gene Expression Regulation, Fungal, Cell Wall metabolism, Fungal Proteins metabolism, Yeasts metabolism
Abstract

In eukaryotes, the glycosylphosphatidylinositol (GPI) modification of many glycoproteins on the cell surface is highly conserved. The lipid moieties of GPI-anchored proteins undergo remodelling processes during their maturation. To date, the products of the PER1, GUP1 and CWH43 genes of the yeast Saccharomyces cerevisiae have been shown to be involved in the lipid remodelling. Here, we focus on the putative GPI remodelling pathway in the methylotrophic yeast Ogataea minuta. We found that the O. minuta homologues of PER1, GUP1 and CWH43 are functionally compatible with those of S. cerevisiae. Disruption of GUP1 or CWH43 in O. minuta caused a growth defect under non-permissive conditions. The O. minuta per1Δ mutant exhibited a more fragile phenotype than the gup1Δ or cwh43Δ mutants. To address the role of GPI modification in O. minuta, we assessed the effect of these mutations on the processing and localization of the O. minuta homologues of the Gas1 protein; in S. cerevisiae, Gas1p is an abundant and well-characterized GPI-anchored protein. We found that O. minuta possesses two copies of the GAS1 gene, which we designate GAS1A and GAS1B. Microscopy and western blotting analysis showed mislocalization and/or lower retention of Gas1Ap and Gas1Bp within the membrane fraction in per1Δ or gup1Δ mutant cells, suggesting the significance of lipid remodelling for GPI-anchored proteins in O. minuta. Localization behaviour of Gas1Bp differed from that of Gas1Ap. Our data reveals, for the first time (to our knowledge), the existence of genes related to GPI anchor remodelling in O. minuta cells., (Copyright © 2017 John Wiley & Sons, Ltd.)

Published
2018
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18. β-1,6-glucan synthesis-associated genes are required for proper spore wall formation in Saccharomyces cerevisiae.

Author

Pan HP, Wang N, Tachikawa H, Nakanishi H, and Gao XD

Subjects
Cell Wall metabolism, Chitin Synthase genetics, Chitin Synthase metabolism, Chitin Synthase physiology, Glycoproteins genetics, Glycoproteins metabolism, Glycoproteins physiology, Membrane Glycoproteins genetics, Membrane Glycoproteins metabolism, Membrane Glycoproteins physiology, Membrane Proteins genetics, Membrane Proteins metabolism, Membrane Proteins physiology, Mutation, Saccharomyces cerevisiae physiology, Saccharomyces cerevisiae ultrastructure, Saccharomyces cerevisiae Proteins genetics, Saccharomyces cerevisiae Proteins metabolism, Spores, Fungal metabolism, Spores, Fungal ultrastructure, Cell Wall genetics, Saccharomyces cerevisiae genetics, Saccharomyces cerevisiae Proteins physiology, beta-Glucans metabolism
Abstract

The yeast spore wall is an excellent model to study the assembly of an extracellular macromolecule structure. In the present study, mutants defective in β-1,6-glucan synthesis, including kre1∆, kre6∆, kre9∆ and big1∆, were sporulated to analyse the effect of β-1,6-glucan defects on the spore wall. Except for kre6∆, these mutant spores were sensitive to treatment with ether, suggesting that the mutations perturb the integrity of the spore wall. Morphologically, the mutant spores were indistinguishable from wild-type spores. They lacked significant sporulation defects partly because the chitosan layer, which covers the glucan layer, compensated for the damage. The proof for this model was obtained from the effect of the additional deletion of CHS3 that resulted in the absence of the chitosan layer. Among the double mutants, the most severe spore wall deficiency was observed in big1∆ spores. The majority of the big1∆chs3∆ mutants failed to form visible spores at a higher temperature. Given that the big1∆ mutation caused a failure to attach a GPI-anchored reporter, Cwp2-GFP, to the spore wall, β-1,6-glucan is involved in tethering of GPI-anchored proteins in the spore wall as well as in the vegetative cell wall. Thus, β-1,6-glucan is required for proper organization of the spore wall. Copyright © 2017 John Wiley & Sons, Ltd., (Copyright © 2017 John Wiley & Sons, Ltd.)

Published
2017
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