Changes in N-linked sugar chain patterns induced by moderate-to-high expression of the galactosyltransferase I gene in a brain-derived cell line, CG4
✍ Scribed by Krishnakumar N. Menon; Takeshi Ikeda; Ichiro Fujimoto; Hisashi Narimatsu; Shin-ichi Nakakita; Sumihiro Hase; Kazuhiro Ikenaka
- Publisher
- John Wiley and Sons
- Year
- 2005
- Tongue
- English
- Weight
- 298 KB
- Volume
- 80
- Category
- Article
- ISSN
- 0360-4012
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✦ Synopsis
Oligosaccharides with biantennae and bisecting N-acetyl glucosamine (GlcNAc) residues attached to the mannose in the beta1-4 trimannosyl core (BA2) are enriched in the brain and considered brain-type sugar chains. We investigated the significance of the interplay between galactosyltransferase I (GalTase I) and BA2 formation in a brain-derived cell line, CG4. Increased GalTase expression in different glial- and neuronal-derived cell lines was accompanied by decreased or undetectable levels of BA2, depending on the level of GalTase expression. Forceful expression of GalTase I in CG4 cells expressing high levels of BA2 and low GalTase activity significantly reduced BA2 levels. In addition, a sixfold increase in an abnormal sugar chain A1(6)G1Fo and a moderate increase in A2G2Fo(6)F were evident. The increased levels of A1(6)G1Fo indicate a diversion or abrogation of the N-linked sugar chain biosynthetic pathway from normal. The accumulation of A1(6)G1Fo and increased A2G2Fo(6)F levels were accompanied by decreased levels of the high mannose-type sugar chains, M5A, M6B, M8A, and M9A. Increased GalTase I expression also led to stunted growth and abnormal morphology of CG4 cells, with increased mortality. Even moderate overexpression of GalTase I thus disrupts the normal biosynthetic pathway of N-linked sugar chains, and high overexpression is fatal to CG4 cells.