Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 466, Issue 4, Pages 733-739Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2015.09.070
Keywords
IDH1; IDH1 mutation; R132H; Monoclonal antibody; HMab-2
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Funding
- Practical Research for Innovative Cancer Control from Japan Agency for Medical Research and Development, AMED
- JSPS KAKENHI Grant [25462242]
- Platform for Drug Discovery, Informatics, and Structural Life Science (PDIS) from AMED
- Basic Science and Platform Technology Program for Innovative Biological Medicine from AMED
- Regional Innovation Strategy Support Program from the Ministry of Education, Culture, Sports, Science and Technology (MEXT) of Japan
- Grants-in-Aid for Scientific Research [25462242, 24390339] Funding Source: KAKEN
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Isocitrate dehydrogenase 1 (IDH1) mutations have been detected in gliomas and other tumors. Although IDH1 catalyzes the oxidative carboxylation of isocitrate to alpha-ketoglutarate (alpha-KG) in cytosol, mutated IDH1 proteins possess the ability to change alpha-KG into the oncometabolite D-2-hydroxyglutarate (D-2HG). Several monoclonal antibodies (mAbs) specific for IDH1 mutations have been established, such as H09, IMab-1, and HMab-1 against IDH1-R132H, which is the most frequent IDH1 mutation in gliomas. In this study, we established a novel high-sensitive mAb HMab-2, which reacts with IDH1-R132H but not with wild type IDH1 in ELISA. HMab-2 reacted only with IDH1-R132H, not with wild type IDH1/2 and other IDH1/2 mutants in Western-blot analysis. Furthermore, HMab-2 recognized IDH1-R132H more sensitively compared with our previously established HMab-1. HMab-2 detected endogenous IDH1-R132H protein expressed in glioblastoma in immunohistochemical analysis. HMab-2 is expected to be useful for the diagnosis of IDH1-R132H-bearing tumors. (C) 2015 Elsevier Inc. All rights reserved.
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