TY - JOUR
T1 - Establishment of a novel monoclonal antibody SMab-1 specific for IDH1-R132S mutation
AU - Kaneko, Mika Kato
AU - Tian, Wei
AU - Takano, Shingo
AU - Suzuki, Hiroyuki
AU - Sawa, Yoshihiko
AU - Hozumi, Yasukazu
AU - Goto, Kaoru
AU - Yamazaki, Kentaro
AU - Kitanaka, Chifumi
AU - Kato, Yukinari
N1 - Funding Information:
We thank Ryo Yanagiya, Shunpei Morita, and Yoshiko Tsukada for their excellent technical assistance. This study was supported in part by grants from the Global COE Program for Medical Sciences, Japan Society for Promotion of Science, from the Ministry of Education, Culture, Sports, Science and Technology of Japan, and from the Mitsubishi Pharma Research Foundation. T.W. was supported by Experimental and Research Center, North China Coal Medical University.
PY - 2011/3/25
Y1 - 2011/3/25
N2 - Isocitrate dehydrogenase 1 (IDH1) mutations, which are early and frequent genetic alterations in gliomas, are specific to a single codon in the conserved and functionally important Arginine 132 (R132) in IDH1. We earlier established a monoclonal antibody (mAb), IMab-1, which is specific for R132H-containing IDH1 (IDH1-R132H), the most frequent IDH1 mutation in gliomas. To establish IDH1-R132S-specific mAb, we immunized mice with R132S-containing IDH1 (IDH1-R132S) peptide. After cell fusion using Sendai virus envelope, IDH1-R132S-specific mAbs were screened in ELISA. One mAb, SMab-1, reacted with the IDH1-R132S peptide, but not with other IDH1 mutants. Western-blot analysis showed that SMab-1 reacted only with the IDH1-R132S protein, not with IDH1-WT protein or IDH1 mutants, indicating that SMab-1 is IDH1-R132S-specific. Furthermore, SMab-1 specifically stained the IDH1-R132S-expressing glioblastoma cells in immunocytochemistry and immunohistochemistry, but did not react with IDH1-WT or IDH1-R132H-containing glioblastoma cells. We newly established an anti-IDH1-R132S-specific mAb SMab-1 for use in diagnosis of mutation-bearing gliomas.
AB - Isocitrate dehydrogenase 1 (IDH1) mutations, which are early and frequent genetic alterations in gliomas, are specific to a single codon in the conserved and functionally important Arginine 132 (R132) in IDH1. We earlier established a monoclonal antibody (mAb), IMab-1, which is specific for R132H-containing IDH1 (IDH1-R132H), the most frequent IDH1 mutation in gliomas. To establish IDH1-R132S-specific mAb, we immunized mice with R132S-containing IDH1 (IDH1-R132S) peptide. After cell fusion using Sendai virus envelope, IDH1-R132S-specific mAbs were screened in ELISA. One mAb, SMab-1, reacted with the IDH1-R132S peptide, but not with other IDH1 mutants. Western-blot analysis showed that SMab-1 reacted only with the IDH1-R132S protein, not with IDH1-WT protein or IDH1 mutants, indicating that SMab-1 is IDH1-R132S-specific. Furthermore, SMab-1 specifically stained the IDH1-R132S-expressing glioblastoma cells in immunocytochemistry and immunohistochemistry, but did not react with IDH1-WT or IDH1-R132H-containing glioblastoma cells. We newly established an anti-IDH1-R132S-specific mAb SMab-1 for use in diagnosis of mutation-bearing gliomas.
KW - Glioblastoma
KW - IDH1
KW - Monoclonal antibody
KW - Mutation
KW - R132S
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U2 - 10.1016/j.bbrc.2011.02.102
DO - 10.1016/j.bbrc.2011.02.102
M3 - Article
C2 - 21352804
AN - SCOPUS:79953024539
SN - 0006-291X
VL - 406
SP - 608
EP - 613
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 4
ER -