Kyushu University Academic Staff Educational and Research Activities Database
List of Presentations
jing gao Last modified date:2022.06.24

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


Presentations
1. #李傲男、高靖、藤井慎介、清島保、自見英治郎 , p130Cas はマウス顎下腺の顆粒性導管の発達に関与する, 第63回歯科基礎医学会学術大会, 2021.10.
2. 黄菲、高靖、自見英治郎, NF-κB,p65 の 534 番目のリン酸化は閉経後骨粗鬆症と体重増加に関与する, 第63回歯科基礎医学会学術大会, 2021.10.
3. Jing Gao, Akiko Mizokami, Hiroshi Takeuchi, Ejiro Jimi and Masato Hirata, A novel molecule involved in the regulation of insulin signaling mediated by internalization of insulin receptor in adipocyte, 第91回日本生化学会大会, 2018.09, Insulin resistance is strongly associated with obesity and other symptoms related to the metabolic syndrome (MS). Numerous studies using insulin-resistant animal models and humans have consistently demonstrated a reduced activity of insulin signaling via the insulin receptor substrate (IRS-1)/ Akt pathway, but the molecular mechanism of triggering events remains incompletely understood. We previously reported that PRIP (phospholipase C-related but catalytically inactive protein) interacts with Akt, the center molecule of insulin signaling pathway. In the present study, we investigated whether PRIP is involved in the regulation of insulin signaling. We found that the phosphorylation of of Akt and even upstream molecules, IR (insulin receptor) and IRS-1 (insulin receptor substrate) were inhibited in PRIP-KO (Knockout) MEFs (mouse embryonic fibroblasts), and that glucose uptake was inhibited in adipocytes differentiated from PRIP-KO MEF, indicating insulin insensitivity in PRIP-KO cells. Furthermore, ablation of PRIP diminished the plasma membrane localization of IR in mouse adipocyte. Overexpression of PRIP1 in HepG2 cell blocked the insulin-reduced IR internalization into the cell. PRIP directly interacted with IR and Clathrin Heavy Chain (CLTC) in adipocyte. Silencing of CLTC using siRNA retrieved the plasma membrane localization of IR which was diminished in PRIP-KO adipocyte to the same level of WT cells. These results suggest that PRIP is involved in the regulation of insulin signaling in adipocyte, likely through modulating the internalization of IR..
4. Jing Gao, Akiko Mizokami, Masato Hirata, Phospholipase C-related but Catalytically Inactive Protein, PRIP is involved in the regulation of insulin signaling via IRS-1/Akt pathway by modulating serine phosphorylation of IRS-1, 2016 American Society for Cell Biology Annual Meeting, 2016.12, Insulin resistance is strongly associated with obesity and other symptoms related to the metabolic syndrome (MS). Numerous studies using insulin-resistant animal models and humans have consistently demonstrated a reduced activity of insulin signaling via the insulin receptor substrate (IRS-1)/phosphatidylinositol (PI) 3-kinase/Akt pathway, but the molecular mechanism of triggering events remains incompletely understood. We previously reported that PRIP (phospholipase C-related but catalytically inactive protein) interacts with Akt, the center molecule of insulin signaling pathway. In the present study, we investigated whether PRIP is involved in the regulation of insulin signaling using mouse embryonic fibroblasts (MEF) from wild type (WT) and PRIP-Knockout (KO) mice. We found that the phosphorylation of Thr308 and Ser473 of Akt and tyrosine phosphorylation of even upstream molecules, IR (insulin receptor) and IRS-1 (insulin receptor substrate-1) were inhibited in MEF cells from PRIP-KO mice, and that glucose uptake was also inhibited in adipocytes differentiated from PRIP-KO MEF, indicating insulin insensitivity in PRIP-KO cells. We then investigated how the insulin signaling via the IR/IRS-1/Akt pathway was inhibited in PRIP-KO MEF cells. Since serine phosphorylation of IRS proteins inhibits insulin signaling, we further examined the serine phosphorylation of IRS-1 using MEF cells. We found that stimulation of PRIP-KO MEF with insulin for 30 min triggered more phosphorylation of Ser1101 of IRS-1 than WT, and that the dephosphorylation process of Ser1101 of IRS-1 after insulin stimulation in MEF cells from WT mice was blocked by calyculin A, an inhibitor for the protein phosphatase 1 (PP1) and protein phosphatase 2A (PP2A). Furthermore, we detected the interaction of IRS-1 and protein phosphatase 2A catalytic subunit (PP2Ac), but not PP1 and PP2A subunit A using in situ Proximity Ligation Assay (PLA) in WT MEF cells, whereas PLA signals was dramatically diminished in PRIP-KO cells. Based on these results and our previous finding that PRIP binds with PP2Ac, we speculated that serine phosphorylation of IRS-1 was enhanced due to the decreased dephosphorylation process in PRIP-KO MEF cells compared to WT cells, which in turn inhibited the IRS-1/PI3K/Akt insulin signaling. Collectively, these results suggest that PRIP is involved in the regulation of insulin signaling, likely through modulating the serine phosphorylation of IRS-1.
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5. Jing Gao, Akiko Mizokami, Hiroshi Takeuchi, Masato Hirata, Differential role of SNAP-25 phosphorylation by Protein Kinase A and C in the regulation of SNARE complex formation and exocytosis, The 23rd General Meeting of the Japanese Association for Dental Science, 2016.10, We studied the functional consequences of SNAP-25 phosphorylation by protein kinase A (PKA) and protein kinase C (PKC). Phosphorylation of SNAP-25 at Thr138 by PKA inhibited SNARE complex formation and functional exocytosis in PC12 cells. Phosphorylation of SNAP-25 at Ser187 by PKC enhanced SNARE complex formation and functional exocytosis in PC12 cells.
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6. Aya Nishikawa, Jing Gao, Akiko Mizokami, Makiko Hirata, Masato Hirata, Involvement of Phospholipase C-related but Catalytically Inactive Protein, PRIP in the Regulation of Insulin Signaling
, The 9th KOREA-JAPAN Conference on Cellular Signaling for Young Scientists , 2016.07.
7. Jing Gao, Makiko Hirata, 溝上 顕子, 髙橋 一郎, 竹内 弘, 平田 雅人, Differential roles of SNAP-25 phosphorylation by protein kinase A and C in the regulation of SNARE complex formation and exocytosis in PC12 cells, 第38回日本分子生物学会年会・第88回日本生化学会大会合同大会, 2015.12.
8. Masato Hirata, Goro Sugiyama, Jing Gao, Hiroshi Takeuchi, Phopholipase C-related but catalytically inactive protein, PRIP as a scaffolding protein for phospho-regulation. , The 39th European Symposium on Hormones and Cell Regulation., 2014.10.
9. Jing Gao, Hiroshi Takeuchi, Daguang Wang, Masato Hirata, Phosphorylation of SNAP-25 by protein kinase-A is negatively involved in calcium-dependent exocytosis in PC12 cells , 第87回日本生化学会大会, 2014.10.
10. Jing Gao, Hiroshi Takeuchi, Daguang Wang, Masato Hirata, Differential Role of SNAP-25 phosphorylation by protein kinase-A and –C in SNARE complex formation, 第86回日本生化学大会, 2013.09.
11. Jing Gao, Hiroshi Takeuchi, Masato Hirata, Phospho-dependent Regulation of Exocytosis, 先端歯学スクール2013, 2013.09.
12. Koki Nagano, Hiroshi Takeuchi, Jing Gao, Takahito Otani, Masato Hirata, Phosphorylation of tomosyn by Akt is implicated in the regulation of GLUT4 translocation, The 8th Japan-Korea Conference on Cellular Signaling for Young Scientists, 2013.11.
13. Akiko Mizokami, Yu Yasutake, Jing Gao, Hiroshi Takeuchi, Masato Hirata, Osteocalcin induces release of glucagon-like peptide-1 and improves metabolic state in mice, The 8th Japan-Korea Conference on Cellular Signaling for Young Scientists, 2013.11.
14. Masato Hirata, Goro Sugiyama, Jing Gao, Hiroshi Takeuchi, Phospholipase C-related but catalytically inactive protein, PRIP as a scaffolding protein for phospho-regulation., International Symposium on PI-PLC Activity and Signaling , 2013.07.
15. Jing Gao, Hiroshi Takeuchi, Zhao Zhang, Daguang Wang, Masato Hirata, SNAP-25 phosphorylation causes down-regulation of SNARE complex formation., 第85回日本生化学会大会, 2012.12.
16. Jing Gao, Hiroshi Takeuchi, zhao zhang, Daguang Wang, Masato Hirata, Role of SNAP-25 phosphorylation by protein kinase A in SNARE complex formation., The 22nd IUBMB & 37th FEBS Congress, 2012.09.
17. Roles of PRIP in phospho-regulation of exocytosis through the interaction with protein phosphatases.
18. Phospho-dependent modulation of exocytosis by PRIP, [URL].
19. The 84th Annual Meeting of the Japanese Biochemical Society , [URL].
20. The 33rd Annual Meeting of the molecular Biology Society of Japan
The 83rd Annual Meeting of the Japanese Biochemical Society.