@article{oai:nagasaki-u.repo.nii.ac.jp:00001303,
 author = {Ueda, Hiroshi and Matsunaga, Hayato and Matsushita, Yosuke and Maeda, Shiori and Iwamoto, Ryusei and Yokoyama, Shigeyuki and Shirouzu, Mikako},
 issue = {Suppl 1},
 journal = {Expert Opinion on Biological Therapy},
 month = {Jul},
 note = {Objectives: Prothymosin α (ProTα) was reported to inhibit the neuronal necrosis by facilitating the plasma membrane localization of endocytosed glucose transporter 1/4 through an activation of putative Gi-coupled receptor. The present study aims to identify a novel ProTα target, which may lead to an activation of Gi-coupled receptor. Methods: We used Gi-rich lipid rafts fraction of retinal cell line N18-RE-105 cells for affinity cross-linking. The biological confirmation that F0/F1 ATPase is a target protein complex was performed by cell-free experiments using ELISA-based binding assay, surface plasmon resonance assay and quartz crystal microbalance assay, and cell-based experiments to measure extracellular ATP level in the HUVECs culture. Results: From the cross-linking study and above-mentioned protein-protein interaction assays, ATP5A1 and ATP5B, F1 ATPase subunits were found to ProTα binding target proteins. In the culture of HUVEC cells, furthermore, ProTα increased the extracellular ATP levels in a reversible manner by anti-ATP5A1- and ATP5B-antibodies. Conclusion: The present study suggests that ProTα may activate ecto-F0/F1 ATPase and produced ATP. This study leads to next subjects whether produced ATP and its metabolites, ADP or adenosine may activate corresponding Gi-coupled receptors., Expert Opinion on Biological Therapy, 18(suppl 1), pp.89-94; 2018},
 pages = {89--94},
 title = {Ecto-F0/F1 ATPase as a novel candidate of prothymosin α receptor},
 volume = {18},
 year = {2018}
}