TY - JOUR
T1 - Anti-GM1 antibodies affect the integrity of lipid rafts
AU - Ueda, Akihiro
AU - Shima, Sayuri
AU - Miyashita, Tadayuki
AU - Ito, Shinji
AU - Ueda, Masami
AU - Kusunoki, Susumu
AU - Asakura, Kunihiko
AU - Mutoh, Tatsuro
N1 - Funding Information:
The present work was supported partly by the Grant-In-Aid from the Ministry of Education, Culture, Sports, Science and Technology of Japan and the Grant-In-Aid from the Ministry of Labor, Health, and Welfare of Japan to T.M. and the High-Tech Research, COE program, and the research grant on Priority area (Functional Glycomics) from the Ministry of Education, Culture, Sports, Science and Technology of Japan to T.M.
PY - 2010/12
Y1 - 2010/12
N2 - Previous studies have shown that patients with the axonal form of Guillain-Barré syndrome (GBS) develop autoantibodies against GM1 ganglioside (GM1). Nerve growth factor (NGF) is essential for neuronal survival in vivo and its functional receptor is Trk-tyrosine kinase. Here, we examined the biological effects of sera from patients with the axonal form of GBS on the morphology and the phosphorylation state of Trk-tyrosine kinase in PC12 cells. Furthermore, we examined the effect of the sera on the integrity of membrane lipid rafts biochemically. The data show that anti-GM1 antibodies found in patients' sera but not control sera inhibit NGF-induced Trk autophosphorylation. Most intriguingly, the autoantibodies alter the distribution of Trk in lipid rafts without shifting the distribution of a rafts marker protein. These data strongly suggest that anti-GM1 antibodies directly influence the integrity of the signaling platform, lipid rafts, implicating the importance of lipid rafts in the development of this disorder.
AB - Previous studies have shown that patients with the axonal form of Guillain-Barré syndrome (GBS) develop autoantibodies against GM1 ganglioside (GM1). Nerve growth factor (NGF) is essential for neuronal survival in vivo and its functional receptor is Trk-tyrosine kinase. Here, we examined the biological effects of sera from patients with the axonal form of GBS on the morphology and the phosphorylation state of Trk-tyrosine kinase in PC12 cells. Furthermore, we examined the effect of the sera on the integrity of membrane lipid rafts biochemically. The data show that anti-GM1 antibodies found in patients' sera but not control sera inhibit NGF-induced Trk autophosphorylation. Most intriguingly, the autoantibodies alter the distribution of Trk in lipid rafts without shifting the distribution of a rafts marker protein. These data strongly suggest that anti-GM1 antibodies directly influence the integrity of the signaling platform, lipid rafts, implicating the importance of lipid rafts in the development of this disorder.
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U2 - 10.1016/j.mcn.2010.07.008
DO - 10.1016/j.mcn.2010.07.008
M3 - Article
C2 - 20659560
AN - SCOPUS:77957955083
VL - 45
SP - 355
EP - 362
JO - Molecular and Cellular Neurosciences
JF - Molecular and Cellular Neurosciences
SN - 1044-7431
IS - 4
ER -