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Acknowledgements
We are grateful to Prof. Hidenao Sasaki for helpful comments. We thank Shoko Shimizu for preparation of this manuscript. This work was supported by JSPS KAKENHI Grant number 25893006.
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HY, IY and HT designed and performed experiments, analyzed and interpreted data and drafted the manuscript and figures. MW, TN, TK, MW and SH conceived and designed the study and critically revised the manuscript. All authors have seen and agree with the content of the manuscript. HY and IY contributed equally to this work.
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This study was approved by the Institutional Review Board of Hokkaido University Hospital.
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Written informed consent was obtained from the patient (Protocol number 012-0167).
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415_2018_8785_MOESM1_ESM.eps
Supplementary material 1 (EPS 22285 kb) Supplemental Fig. 1. Immunofluorescence analysis using HeLa cells transfected with the extracellular domain of Sez6l2 (FLAG-Sez6l2(EX)) and the extracellular domain of GluR1 (HA-GluR1(EX)). (A) Immunofluorescence analysis of FLAG-Sez6l2(EX) and HA-GluR1(EX). The cells were fixed and stained with antibodies to FLAG (green), HA (red), and Hoechst33258 (blue). Immunofluorescence analysis using HeLa cells transfected with the extracellular domain of Sez6l2 (FLAG-Sez6l2(EX)) and the extracellular domain of GluR1 (HA-GluR1(EX)) showed co-localization of Sez6l2(EX) and GluR1(EX). (B) Immunofluorescence analysis of FLAG-Sez6l2(FL) and GluR1(FL). The cells were fixed and stained with antibodies to FLAG (green), GluR1 (red), and Hoechst33258 (blue). Immunofluorescence analysis using HeLa cells transfected with the full length of FLAG-Sez6l2 [FLAG-Sez6l2 (FL)] and the full length of GluR1(GluR1(FL)) showed partial co-localization of Sez6l2(FL) and GluR1(FL)
415_2018_8785_MOESM2_ESM.eps
Supplementary material 2 (EPS 2906 kb) Supplemental Fig. 2. Schema of “inhibition assay of direct binding between Sez6l2 and GluR1 using the patient’s serum or control serum”. Pt, patient; Ct, control; PBS, phosphate buffered saline; IP, immunoprecipitation; IB, immunoblot. Using recombinant proteins of FLAG-Sez6l2(EX) and HA-GluR1(EX) and the patient’s serum and healthy control serum, we tried to check inhibition of direct binding between Sez6l2 and GluR1. Proteins of FLAG-Sez6l2(EX) and HA-GluR1(EX) were used at the same amounts as those shown in Fig. 1. We washed each sample with PBS gently three times in every PBS wash
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Yaguchi, H., Yabe, I., Takahashi, H. et al. Anti-Sez6l2 antibody detected in a patient with immune-mediated cerebellar ataxia inhibits complex formation of GluR1 and Sez6l2. J Neurol 265, 962–965 (2018). https://doi.org/10.1007/s00415-018-8785-z
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DOI: https://doi.org/10.1007/s00415-018-8785-z