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jing gao Last modified date：2023.11.28

Assistant Professor / Oral Biological Sciences / Department of Dental Science / Faculty of Dental Science


Papers
1. Gao J., Li A., Fujii S., Huang F., Nakatomi C., Nakamura I., Honda H., Kiyoshima T., Jimi E., p130Cas is required for androgen-dependent postnatal development regulation of submandibular glands., Scientific reports, 10.1038/s41598-023-32390-1., 13, 1, 13(1):5144, 2023.03.
2. Gao J, Mizokami A, Takeuchi H, Li A, Huang F, Nagano H, Kanematsu T, Jimi E, Hirata M., Phospholipase C-related but catalytically inactive protein acts as a positive regulator of insulin signalling in adipocytes, Journal of cell science, 10.1242/jcs.258584., 135, 1, 2022.01.
3. Inoue A, Kiyoshima T, Yoshizaki K, Nakatomi C, Nakatomi M, Ohshima H, Shin M, Gao J, Tsuru K, Okabe K, Nakamura I, Honda H, Matsuda M, Takahashi I, Jimi E., Deletion of epithelial cell-specific p130Cas impairs the maturation stage of amelogenesis, Bone, 10.1016/j.bone.2021.116210. , 154, 116210, 2022.01.
4. Gao J, Muroya R, Huang F, Nagata K, Shin M, Nagano R, Tajiri Y, Fujii S, Yamaza T, Aoki K, Tamura Y, Inoue M, Chishaki S, Kukita T, Okabe K, Matsuda M, Mori Y, Kiyoshima T, Jimi E., Bone morphogenetic protein induces bone invasion of melanoma by epithelial-mesenchymal transition via the Smad1/5 signaling pathway, Lab Invest., 10.1038/s41374-021-00661-y., 101, 11, 1475-1483, 2021.10.
5. Mukai S, Mizokami A, Otani T, Sano T, Matsuda M, Chishaki S, Gao J, Kawakubo-Yasukochi T, Tang R, Kanematsu T, Takeuchi H, Jimi E, Hirata M., Adipocyte-specific GPRC6A ablation promotes diet-induced obesity by inhibiting lipolysis , Journal of biological chemistry , doi: 10.1016/j.jbc.2021.100274., 296, 100274, 2021 Jan 8;296:100274., 2021.01.
6. Tatsuki Yaginuma, Jing Gao, Kengo Nagata, Ryusuke Muroya, Huang Fei, Haruki Nagano, Sakura Chishaki, Takuma Matsubara, Shoichiro Kokabu, Kou Matsuo, Tamotsu Kiyoshima, Izumi Yoshioka, Eijiro Jimi, p130Cas Induces Bone Invasion by Oral Squamous Cell Carcinoma by Regulating Tumor Epithelial-Mesenchymal Transition and Cell Proliferation, Carcinogenesis, doi: 10.1093/carcin/bgaa007., 2020.01.
7. Akiko Mizokami, Satoru Mukai, Jing Gao, Tomoyo Kawakubo-Yasukochi, Takahito Otani, Hiroshi Takeuchi, Eijiro Jimi, Masato Hirata, GLP-1 Signaling Is Required for Improvement of Glucose Tolerance by Osteocalcin, the Journal of endocrinology , 10.1530/JOE-19-0288, Vol 244, 2, 2019.11.
8. Kenya Touyama, Masud Khan, Kazuhiro Aoki, Miho Matsuda, Fumitaka Hiura, Nana Takakura, Takuma Matsubara, Yui Harada, Yuna Hirohashi, Yukihiko Tamura, Jing Gao, Kayo Mori, Shoichiro Kokabu, Hisataka Yasuda, Yuko Fujita, Koji Watanabe, Yoshinori Takahashi, Kenshi Maki, Eijiro Jimi, Bif-1/Endophilin B1/SH3GLB1 regulates bone homeostasis, Journal of Cellular Biochemistry, 10.1002/jcb.29193, 120, 11, 18793-18804, 2019.11, Skeletal tissue homeostasis is maintained via the balance of osteoclastic bone resorption and osteoblastic bone formation. Autophagy and apoptosis are essential for the maintenance of homeostasis and normal development in cells and tissues. We found that Bax-interacting factor 1 (Bif-1/Endophillin B1/SH3GLB1), involving in autophagy and apoptosis, was upregulated during osteoclastogenesis. Furthermore, mature osteoclasts expressed Bif-1 in the cytosol, particularly the perinuclear regions and podosome, suggesting that Bif-1 regulates osteoclastic bone resorption. Bif-1-deficient (Bif-1 −/−) mice showed increased trabecular bone volume and trabecular number. Histological analyses indicated that the osteoclast numbers increased in Bif-1 −/− mice. Consistent with the in vivo results, osteoclastogenesis induced by receptor activator of nuclear factor-κB (NF-κB) ligand (RANKL) was accelerated in Bif-1 −/− mice without affecting RANKL-induced activation of RANK downstream signals, such as NF-κB and mitogen-activated protein kinases (MAPKs), CD115/RANK expression in osteoclast precursors, osteoclastic bone-resorbing activity and the survival rate. Unexpectedly, both the bone formation rate and osteoblast surface substantially increased in Bif-1 −/− mice. Treatment with β-glycerophosphate (β-GP) and ascorbic acid (A.A) enhanced osteoblastic differentiation and mineralization in Bif-1 −/− mice. Finally, bone marrow cells from Bif-1 −/− mice showed a significantly higher colony-forming efficacy by the treatment with or without β-GP and A.A than cells from wild-type (WT) mice, suggesting that cells from Bif-1 −/− mice had higher clonogenicity and self-renewal activity than those from WT mice. In summary, Bif-1 might regulate bone homeostasis by controlling the differentiation and function of both osteoclasts and osteoblasts (235 words)..
9. Satoshi Asano, Yuri Taniguchi, Yosuke Yamawaki, Jing Gao, Kae Harada , Hiroshi Takeuchi, Masato Hirata, Takashi Kanematsu, Suppression of cell migration by phospholipase C-related catalytically inactive protein-dependent modulation of PI3K signalling., Scientific Reports, 10.1038/s41598-017-05908-7, 7, 1, 2017.07, [URL], The metabolic processes of phosphatidylinositol 4,5-bisphosphate [PI(4,5)P2] into PI(3,4,5)P3 and the subsequent PI(3,4,5)P3 signalling are involved in cell migration. Dysfunctions in the control of this pathway can cause human cancer cell migration and metastatic growth. Here we investigated whether phospholipase C-related catalytically inactive protein (PRIP), a PI(4,5)P2-binding protein, regulates cancer cell migration. PRIP overexpression in MCF-7 and BT-549 human breast cancer cells inhibited cell migration in vitro and metastasis development in vivo. Overexpression of the PRIP pleckstrin homology domain, a PI(4,5)P2 binding motif, in MCF-7 cells caused significant suppression of cell migration. Consistent with these results, in comparison with wild-type cells, Prip-deficient mouse embryonic fibroblasts exhibited increased cell migration, and this was significantly attenuated upon transfection with a siRNA targeting p110α, a catalytic subunit of class I phosphoinositide 3-kinases (PI3Ks). PI(3,4,5)P3 production was decreased in Prip-overexpressing MCF-7 and BT-549 cells. PI3K binding to PI(4,5)P2 was significantly inhibited by recombinant PRIP in vitro, and thus the activity of PI3K was downregulated. Collectively, PRIP regulates the production of PI(3,4,5)P3 from PI(4,5)P2 by PI3K, and the suppressor activity of PRIP in PI(4,5)P2 metabolism regulates the tumour migration, suggesting PRIP as a promising target for protection against metastatic progression..
10. Akiko Mizokami, Daguang Wang, Mitsuru Tanaka, Jing Gao, Hiroshi Takeuchi, Toshiro Matsui, Masato Hirata, An extract from pork bones containing osteocalcin improves glucose metabolism in mice by oral administration, Bioscience, Biotechnology, and Biochemistry, 10.1080/09168451.2016.1214530, 27, 1-8, 2016.06, Osteocalcin (OC) is a bone-derived hormone that regulates energy metabolism. OC exists in two forms, carboxylated (GlaOC) and uncaboxylated (GluOC), but only the latter appears to have an endocrine function. In this study, we prepared an extract containing both Gla- and GluOC from boiled pork bone using 0.2 M carbonate buffer at pH 9.5, and tested whether the extract had beneficial effects on improving metabolic parameters in obese mice. The extract equivalent of 1.2 μg of GluOC/mouse was orally administrated to C57BL/6 female mice fed a high-fat, high-sucrose diet. Daily oral administration of the extract for four weeks decreased blood glucose levels and promoted glucose tolerance as well as insulin sensitivity. Our study shows for the first time that boiled pork bones are a source material for osteocalcin in the large-scale production of supplements designed to improve glucose metabolism..
11. Jing Gao, Makiko Hirata, Akiko Mizokami, 髙橋 一郎, 竹内 弘, 平田 雅人, Differential role of SNAP-25 phosphorylation by protein kinases A and C in the regulation of SNARE complex formation and exocytosis in PC12 cells, CELLULAR SIGNALLING, 10.1016/j.cellsig.2015.12.014, 28, 5, 425-437, 2016.05.
12. Koki Nagano, Hiroshi Takeuchi, Jing Gao, Yoshihide Mori, Takahito Otani, Daguang Wang, Hirata Masato, Tomosyn is a novel Akt substrate mediating insulin-dependent GLUT4 exocytosis, INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY, 10.1016/j.biocel.2015.02.013, 62, 62-71, 2015.05.
13. Takahito Otani, Akiko Mizokami, Yoshikazu Hayashi, Jing Gao, Yoshihide Mori, Seiji Nakamura, Hiroshi Takeuchi, Masato Hirata, Signaling pathway for adiponectin expression in adipocytes by osteocalcin, CELLULAR SIGNALLING, 10.1016/j.cellsig.2014.12.018, 27, 3, 533-544, 27(3), 2015.03.
14. Daguang Wang, Hiroshi Takeuchi, Jing Gao, Zhao Zhang, Masato Hirata, Hetero-oligomerization of C2 domains of phospholipase C-related but catalytically inactive protein and synaptotagmin-1, Advances in Biological Regulation, 10.1016/j.jbior.2014.09.001., 2015.01, The C2 domain is a protein module often found in molecules that regulate exocytosis. C2 domains mediate interactions between the parental molecule and Ca2+, phospholipids, and proteins. Although various molecules have been shown to interact with several C2 domains, no interactions between the C2 domains from different molecules have yet been reported. In the present study, we identified direct interactions between the C2 domain of PRIP (phospholipase C-related but catalytically inactive protein) and the C2 domains of other molecules. Among the C2 domains examined, those of synaptotagmin-1 (Syt1-C2A and Syt1-C2B) and phospholipase C δ-1 bound to the C2 domain of PRIP. We investigated the interactions between the C2 domain of PRIP (PRIP-C2) with Syt1-C2A and Syt1-C2B, and the mode of binding of each was Ca2+-dependent and -independent, respectively. We further demonstrated that the Ca2+ dependence of the interaction between PRIP-C2 and Syt1-C2A was attributed to Ca2+ binding with Syt1-C2A, but not PRIP-C2, using a series of mutants prepared from both C2 domains. We previously reported that the interaction between PRIP-C2 and the membrane fusion machinery suggested a critical role for PRIP in exocytosis; therefore, the results of the present study further support the importance of PRIP-C2 in the inhibitory function of PRIP in regulating exocytosis..
15. Goro Sugiyama, Hiroshi Takeuchi, Takashi Kanematsu, Jing Gao, Miho Matsuda, Masato Hirata, Phospholipase C-related but catalytically inactive protein, PRIP as a scaffolding protein for phospho-regulation, Advanced in Biological Regulation, 10.1016/j.jbior.2013.07.001, 53, 3, 331-340, 2013.07.
16. Zhao Zhang, Hiroshi Takeuchi, Jing Gao, Daguang Wang, DeclanJ. James, Thomas F.J.Martin, Masato Hirata, PRIP (Phospholipase C-related but Catalytically Inactive Protein) inhibits exocytosis by direct interactions with Syntaxin 1 and SNAP-25 through its C2 domain, The Journal of Biological Chemistry, 10.1074/jbc.M112.419317, 288, 11, 7769-7780, 2013.03.
17. Akiko Mizokami, Yu Yasutake, JingGao, Miho Matsuda, Ichiro Takahashi, Hiroshi Takeuchi, Masato Hirata, Osteocalcin induces release of glucagon-like peptide-1 and thereby stimulates insulin secretion in mice, Plos One, 10.1371/journal.pone.0057375, 8, 2, e57375, 2013.02.
18. Goro Sugiyama, Hiroshi Takeuchi, Koki Nagano, Jing Gao, Yukiko Ohyama, Yoshihide Mori, Masato Hirata, Regulated interaction of protein phosphatase 1 and protein phophatase 2A with phospholipase C-related but catalytically inactive protein, Biochemistry, 10.1021/bi2018128, 51, 16, 3394-3403, 2012.04.
19. Jing Gao, Hiroshi Takeuchi, Zhao Zhang, Mitsunori Fukuda, Masato Hirata, Phospholipase C-related but catalytically inactive protein (PRIP) modulates synaptosomal-associated protein 25 (SNAP-25) phosphorylation and exocytosis., The Journal of Biological Chemistry, 10.1074/jbc.M111.294645, 287, 13, 10565-10578, 2012.03, [URL], Exocytosis is one of the most fundamental cellular events. The basic mechanism of the final step, membrane fusion, is mediated by the formation of the SNARE complex, which is modulated by the phosphorylation of proteins controlled by the concerted actions of protein kinases and phosphatases. We have previously shown that a protein phosphatase-1 (PP1) anchoring protein, phospholipase C-related but catalytically inactive protein (PRIP), has an inhibitory role in regulated exocytosis. The current study investigated the involvement of PRIP in the phospho-dependent modulation of exocytosis. Dephosphorylation of synaptosome-associated protein of 25 kDa (SNAP-25) was mainly catalyzed by PP1, and the process was modulated by wild-type PRIP but not by the mutant (F97A) lacking PP1 binding ability in in vitro studies.We then examined the role of PRIP in phospho-dependent regulation of exocytosis in cell-based studies using pheochromocytoma cell line PC12 cells, which secrete noradrenalin. Exogenous expression of PRIP accelerated the dephosphorylation process of phosphorylated SNAP-25 after for-skolin or phorbol ester treatment of the cells. The phospho-states of SNAP-25 were correlated with noradrenalin secretion, which was enhanced by forskolin or phorbol ester treatment and modulated by PRIP expression in PC12 cells. Both SNAP-25 and PP1 were co-precipitated in anti-PRIP immunocomplex isolated from PC12 cells expressing PRIP. Collectively, together with our previous observation regarding the roles of PRIP in PP1 regulation, these results suggest that PRIP is involved in the regulation of the phospho-states ofSNAP-25by modulating the activity of PP1, thus regulating exocytosis..
20. Hiroshi Takeuchi , Zhao Zhang, Jing Gao, Goro Sugiyama, Takako Takeuchi, Masato Hirata, Second basic pockets contribute to the localization of PX domains by binding to phosphatidic acid, Advances in Biological Regulation , 52, 1, 183-194, 2012.01, [URL].
21. Gao, J., Takeuchi, H., Umebayashi, H., Zhang, Z., Matsuda, M. and Hirata, M., Assay of dense-core vesicle exocytosis in permeabilized PC12 cells, Andvances in Enzyme Regulation, 50, 237-246, 2010.01.
22. Takeuchi, H., Takeuchi, T., Gao, J., Cantley, LC. and Hirata, M., Characterization of PXK as a protein involved in epidermal growth factor receptor trafficking., Molecular and Cellular Biology, 30, 7, 1689-1702, 2010.04, The phox homology (PX) domain is a phosphoinositide-binding module that typically binds phosphatidylinositol 3-phosphate. Out of 47 mammalian proteins containing PX domains, more than 30 are denoted sorting nexins and several of these have been implicated in internalization of cell surface proteins to the endosome, where phosphatidylinositol-3-phosphate is concentrated. Here we investigated a multimodular protein termed PXK, composed of a PX domain, a protein kinase-like domain, and a WASP homology 2 domain. We show that the PX domain of PXK localizes this protein to the endosomal membrane via binding to phosphatidylinositol 3-phosphate. PXK expression in COS7 cells accelerated the ligand-induced internalization and degradation of epidermal growth factor receptors by a mechanism requiring phosphatidylinositol 3-phosphate binding but not involving the WASP homology 2 domain. Conversely, depletion of PXK using RNA interference decreased the rate of epidermal growth factor receptor internalization and degradation. Ubiquitination of epidermal growth factor receptor by the ligand stimulation was enhanced in PXK-expressing cells. These results indicate that PXK plays a critical role in epidermal growth factor receptor trafficking through modulating ligand-induced ubiquitination of the receptor..
23. Gao, J., Takeuchi, H., Zhang, Z., Fujii, M., Kanematsu, T. and Hirata, M., Binding of phospholipase C-related but catalytically inactive protein to phosphatidylinositol 4,5-bisphosphate via the PH domain., Cellular Signalling, 21, 1180-1186, 2009.03, A well-known protein module regulating molecular interactions is the pleckstrin homology (PH) domain whose best-characterised ligand is phosphoinositide. In the present study, we analysed the PH domain from PRIP (phospholipase C-related but catalytically inactive protein, comprising types 1 and 2) regarding phosphatidylinositol 4,5-bisphosphate [PtdIns(4,5)P2] binding employing a variety of binding assays. The PH domains prepared from PRIP-1 and -2 showed similar binding profiles to soluble ligands in vitro and showed similar plasma membrane localisation to that of PLC-δ1; however, the PH domain with the N-terminal extension of PRIP-1 but not PRIP-2 showed even distribution throughout the cytoplasm, indicating that the N-terminal extension of PRIP-1 inhibited binding to PtdIns(4,5)P2 present in the plasma membrane. A chimeric molecule of PLC-δ1 PH domain with the N-terminal extension of PRIP-1 exhibited similar localisation to PRIP-1 PH domain with the N-terminal extension. Binding assay to liposomes containing various concentrations of PtdIns(4,5)P2 revealed that the PH domain of PLC-δ1 bound steeply to the maximum, even at a concentration of 1.2 mol%, whereas the PH domains from PRIP-1 and -2 bound depending on the concentration up to 5 mol%. We also performed binding experiments using saponin-permeabilised PC12 cells. PH domains from PRIP increased the binding to cells preincubated with the brain cytosol extract in the presence of ATP, during which PtdIns(4,5)P2 were probably synthesised. The binding of PH domain with the following EF hand motifs showed Ca2+-dependent binding. These results indicate that the PH domain of PRIP binds to PtdIns(4,5)P2 present in the plasma membrane, depending on the concentrations of the lipid ligand and Ca2+, suggesting that PRIP might play physiological roles in events involved in the changes of these parameters, probably including Ins(1,4,5)P3..
24. Inoue, R., Matsuki, N., Gao, J., Kanematsu, T. and Hirata, M., The inhibitory effect of alendronate, a nitrogen-containing bisphosphonate on the PI3K/Akt/NFB pathway in osteosarcoma cells., British Journal of Pharmacology, 10.1038/sj.bjp.0706373, 146, 5, 633-641, 2005.11.


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