Suppression of beta-N-acetylglucosaminidase in the N-glycosylation pathway for complex glycoprotein formation in Drosophila S2 cells.

@article{Kim2009SuppressionOB,
  title={Suppression of beta-N-acetylglucosaminidase in the N-glycosylation pathway for complex glycoprotein formation in Drosophila S2 cells.},
  author={Yeon Kyu Kim and Kyoung Ro Kim and Dong Gyun Kang and So Young Jang and Young Hwan Kim and Hyung Joon Cha},
  journal={Glycobiology},
  year={2009},
  volume={19 3},
  pages={301-8}
}
Most insect cells have a simple N-glycosylation process and consequently paucimannosidic or simple core glycans predominate. Previously, we have shown that paucimannosidic N-glycan structures are dominant in Drosophila S2 cells. It has been proposed that beta-N-acetylglucosaminidase (GlcNAcase), a hexosaminidase in the Golgi membrane which removes a terminal N-acetylglucosamine (GlcNAc), might contribute to simple N-glycosylation in several insects and insect-derived cells except S2 cells. In… CONTINUE READING