| 1. |
Goro Sugiyama, Tomohiro Yamada, Tomoki Sugi, YU Kamata, Kana Ishibashi, Yoshihide Mori, Sarcomatoid carcinoma of the tongue in chronic graft versus host disease: an unusual report., oral science international, 2021.03. |
| 2. |
Goro Sugiyama, Yukiko Ohyama, Tomohiro Yamada, Kotaro Ishii, Wataru Kumamaru, Yuki Sumimoto, Tamotsu Kiyoshima, Hiroaki Niiro and Yoshihide Mori., Other iatrogenic immunodeficiency-associated lymphoproliferative disorders of the oral floor induced by methotrexate and tofacitinib: A case report., Journal of Oral and Maxillofacial Surgery, Medicine, and Pathology, 34, 2, 601-608, 2020.11. |
| 3. |
Kousuke Yasuda, Hiroyuki Nakano, Tomohiro Yamada, Safieh Albougha, Kazuya Inoue, Azusa Nakashima, Yu Kamata, Goro Sugiyama, Shiho Tajiri, Tomoki Sumida, Katsuaki Mishima, Yoshihide Mori, Identifying Differences between a Straight Face and a Posed Smile Using the Homologous Modeling Technique and the Principal Component Analysis, Journal of Craniofacial Surgery, 10.1097/SCS.0000000000005969, 2019.01. |
| 4. |
Tomohiro Yamada, Goro Sugiyama, Ken Higashimoto, Azusa Nakashima, Hiroyuki Nakano, Tomoki Sumida, Hidenobu Soejima, Yoshihide Mori, Beckwith-Wiedemann syndrome with asymmetric mosaic of paternal disomy causing hemihyperplasia, Oral Surgery, Oral Medicine, Oral Pathology and Oral Radiology, 10.1016/j.oooo.2018.07.053, 127, 3, e84-e88, 2019.03. |
| 5. |
Azusa Suzuki, Goro Sugiyama, Yukiko Ohyama, Wataru Kumamaru, Tomohiro Yamada, Yoshihide Mori, Regulation of NF-kB signalling through the PR55β-RelA interaction in osteoblasts, In Vivo, 10.21873/invivo.11813, 34, 2, 601-608, 2020.01. |
| 6. |
Azusa Nakashima, Tomohiro Yamada, Goro Sugiyama, Wataru Mizunoya, Hiroyuki Nakano, Kosuke Yasuda, Ichiro Takahashi, Yoshihide Mori, Masseter muscle properties differ between the left and right sides in mandibular class III patients with asymmetry, Journal of Hard Tissue Biology, 10.2485/jhtb.29.25, 29, 1, 25-30, 2020.01. |
| 7. |
Tomohiro Yamada, Goro Sugiyama, Yoshihide Mori, Masticatory muscle function affects the pathological conditions of dentofacial deformities, Japanese Dental Science Review, 10.1016/j.jdsr.2019.12.001, 56, 1, 56-61, 2020.12. |
| 8. |
Azusa Nakashima, Tomohiro Yamada, Hiroyuki Nakano, Goro Sugiyama, Tomotaka Sugi, Y. U. Kamata, Tomoki Sumida, Yoshihide Mori, Jaw asymmetry may cause bad posture of the head and the spine—A preliminary study, Journal of Oral and Maxillofacial Surgery, Medicine, and Pathology, 10.1016/j.ajoms.2018.01.001, 30, 3, 242-246, 2018.05. |
| 9. |
Mariko Urata, Shoichiro Kokabu, Takuma Matsubara, Goro Sugiyama, Chihiro Nakatomi, Hiroshi Takeuchi, Shizu Hirata-Tsuchiya, Kazuhiro Aoki, Yukihiko Tamura, Yasuko Moriyama, Yasunori Ayukawa, Miho Matsuda, Min Zhang, Kiyoshi Koyano, Chiaki Kitamura, Eijiro Jimi, A peptide that blocks the interaction of NF-κB p65 subunit with Smad4 enhances BMP2-induced osteogenesis, Journal of Cellular Physiology, 10.1002/jcp.26571, 233, 9, 7356-7366, 2018.01, Bone morphogenetic protein (BMP) potentiates bone formation through the Smad signaling pathway in vitro and in vivo. The transcription factor nuclear factor B (NF-B) suppresses BMP-induced osteoblast differentiation. Recently, we identified that the transactivation (TA) 2 domain of p65, a main subunit of NF-B, interacts with the mad homology (MH) 1 domain of Smad4 to inhibit BMP signaling. Therefore, we further attempted to identify the interacting regions of these two molecules at the amino acid level. We identified a region that we term the Smad4-binding domain (SBD), an amino-terminal region of TA2 that associates with the MH1 domain of Smad4. Cell-permeable SBD peptide blocked the association of p65 with Smad4 and enhanced BMP2-induced osteoblast differentiation and mineralization without affecting the phosphorylation of Smad1/5 or the activation of NF-B signaling. SBD peptide enhanced the binding of the BMP2-inudced phosphorylated Smad1/5 on the promoter region of inhibitor of DNA binding 1 (Id-1) compared with control peptide. Although SBD peptide did not affect BMP2-induced chondrogenesis during ectopic bone formation, the peptide enhanced BMP2-induced ectopic bone formation in subcortical bone. Thus, the SBD peptide is useful for enabling BMP2-induced bone regeneration without inhibiting NF-kappa B activity.. |
| 10. |
Kana Ishibashi, kotaro ishii, Goro Sugiyama, Tomoki Sumida, Tsuyoshi Sugiura, Yu Kamata, Katsuhiro Seki, Takahiro Fujinaga, Kumamaru Wataru, Yosuke Kobayashi, Naomi Hiyake, Hiroyuki Nakano, Tomohiro Yamada, Yoshihide Mori, Deregulation of nicotinamide N-methyltransferase and gap junction protein alpha-1 causes metastasis in adenoid cystic carcinoma, Anticancer Research, 10.21873/anticanres.12207, 38, 1, 187-197, 2018.01, BACKGROUND/AIM: Adenoid cystic carcinoma (AdCC) is a malignant tumor that occurs in the salivary glands and frequently metastasizes. The aim of this study was to identify factors mediating AdCC metastasis. MATERIALS AND METHODS: We established three AdCC cell lines by orthotropic transplantation and in vivo selection: parental, highly metastatic (ACCS-M-GFP), and lymph node metastatic (ACCS-LN-GFP) cells. RESULTS: We examined the three cell lines. DNA microarray indicated significantly altered processes in ACCS-LN-GFP cells: particularly, the expression of nicotinamide N-methyltransferase (NNMT) was enhanced the most. NNMT is associated with tumorigenesis and is a potential tumor biomarker. Concomitantly, we found-significant down-regulation of gap junction protein alpha-1. We suggest that ACCS-LN-GFP cells acquire cancer stem cell features involving the up-regulation of NNMT and the loss of gap junction protein alpha-1, leading to epithelial-mesenchymal transition and consequent AdCC metastasis. CONCLUSION: NNMT is a potential biomarker of AdCC.. |
| 11. |
Kana Ishibashi, kotaro ishii, Goro Sugiyama, Yu Kamata, Azusa Suzuki, Kumamaru Wataru, Yukiko Ohyama, Hiroyuki Nakano, Tamotsu Kiyoshima, Tomoki Sumida, Tomohiro Yamada, Yoshihide Mori, Regulation of β-catenin phosphorylation by PR55β in adenoid cystic carcinoma, Cancer Genomics and Proteomics, 10.21873/cgp.20064, 15, 1, 53-60, 2018.01. |
| 12. |
Azusa Nakashima, Hiroyuki Nakano, Tomohiro Yamada, Kazuya Inoue, Goro Sugiyama, Kumamaru Wataru, Yasumichi Nakajima, Tomoki Sumida, Takeshi Yokoyama, Katsuaki Mishiama, Yoshihide Mori, The relationship between lateral displacement of the mandible and scoliosis, Oral and Maxillofacial Surgery, 10.1007/s10006-016-0607-9, 21, 1, 59-63, 2017.03. |
| 13. |
Minami Shibuya, Tatsuya Ikari, Goro Sugiyama, Yukiko Ohyama, Kumamaru Wataru, Koki Nagano, Tsuyoshi Sugiura, Kanemitsu Shirasuna, Yoshihide Mori, Efficient regulation of branching morphogenesis via fibroblast growth factor receptor 2c in early-stage embryonic mouse salivary glands, Differentiation, 10.1016/j.diff.2016.05.005, 92, 4, 216-224, 2016.10, Salivary gland (SG) defects have a wide range of health implications, including xerostomia, bacterial infections, and oral health issues. Branching morphogenesis is critical for SG development. A clear understanding of the mechanisms underlying this process will accelerate SG regeneration studies. Fibroblast growth factor receptor 2 (FGFR2) interacts with multiple fibroblast growth factors (FGFs), which promote development. FGFR2 consists of two isoforms, FGFR2b and FGFR2c. FGFR2b is critical for SG development, but little is known about the expression and function of FGFR2c. We investigated the expression of all FGFR family members in fetal SGs between embryonic day 12.5 (E12.5) and E18.5. Based on RT-PCR, we observed an increase in the expression of not only Fgfr2b, but also Fgfr2c in early-stage embryonic mouse SGs, suggesting that FGFR2c is related to SG development. The branch number decreased in response to exogenous FGF2 stimulation, and this effect was suppressed by a mouse anti-FGFR2c neutralizing antibody (NA) and siRNA targeting FGFR2c, whereas FGFR2b signaling was not inhibited. Moreover, the expression of marker genes related to EMT was induced by FGF2, and this expression was suppressed by the NA. These results suggested that branching morphogenesis in SGs is regulated by FGFR2c, in addition to FGFR2b. Interestingly, FGFR2c signaling also led to increased fgf10 expression, and this increase was suppressed by the NA. FGFR2c signaling regulates branching morphogenesis through the activation of FGFR2b signaling via increased FGF10 autocrine. These results provide new insight into the mechanisms by which crosstalk between FGFR2b and FGFR2c results in efficient branching morphogenesis.. |
| 14. |
Yasumichi Nakajima, Hiroyuki Nakano, Tomoki Sumida, Tomohiro Yamada, Kazuya Inoue, Goro Sugiyama, Katsuaki Mishima, Yoshihide Mori, High Le Fort I osteotomy for correction of mid-face deformity in Crouzon syndrome, Congenital Anomalies, 10.1111/cga.12168, 56, 5, 240-242, 2016.09, An 18-year-old woman with mild Crouzon syndrome was referred with malocclusion and mandibular protrusion. Examination revealed Class III canine and molar relationships, hypoplastic maxilla, 1-mm overbite, and −2-mm overjet. Analysis showed 69° sella-nasion-A, 73.6° sella-nasion-B, and −4.6° A point-nasion-B point angles. Polysomnography revealed respiratory disturbance and 6.3% oxygen desaturation indices of 5.4/h and 9.0/h. We performed double-jaw surgery using high Le Fort I osteotomy and bilateral sagittal split ramus osteotomy for midfacial deformity correction. Twelve months post-surgery, her measures were 70.8°, 72°, −1.2°, 3.0/h, and 6.1/h, respectively. Esthetics were satisfactory. High Le Fort I osteotomy is effective for midfacial deformity correction in patients with Crouzon syndrome.. |
| 15. |
Kouhei Hayashi, Tatsuya Ikari, Goro Sugiyama, Tsuyoshi Sugiura, Yukiko Ohyama, Kumamaru Wataru, Kanemitsu Shirasuna, Yoshihide Mori, Involvement of the T-box transcription factor Brachyury in early-stage embryonic mouse salivary gland, Biochemical and Biophysical Research Communications, 10.1016/j.bbrc.2016.06.140, 477, 4, 814-819, 2016.09, The mouse submandibular gland (SMG) is important organ for embryonic development, and branching morphogenesis is regulated by many molecules containing transcription factors. Real-time reverse transcriptase polymerase chain reaction revealed that the expression of Brachyury increased in the SMG and peaked between E12.5–E13.5, concomitant with the early stage of branching morphogenesis. The expression of Brachyury in SMG rudiments between E12.5–E13.5 was confirmed by western blotting. In addition, fibronectin and Btbd7 (regulated by fibronectin), which are both essential for cleft formation, were expressed strongly during the same period. The Sox2 and Wnt3a, which regulate cell growth, were also expressed strongly during E12.5–E13.5. On the other hand, cleft formation and branching morphogenesis was suppressed by knockdown of Brachyury gene, suggesting that Brachyury plays a central role in regulating cell growth and cleft formation in early-stage embryonic mouse salivary gland development.. |
| 16. |
Shoichiro Kokabu, Shizu Tsuchiya-Hirata, Hidefumi Fukushima, Goro Sugiyama, Jonathan W. Lowery, Takenobu Katagiri, Eijiro Jimi, Inhibition of bone morphogenetic protein-induced osteoblast differentiation, Journal of Oral Biosciences, 10.1016/j.job.2015.05.005, 57, 4, 179-184, 2015.01, Background Bone morphogenetic proteins (BMPs) induce ectopic bone formation in vivo and osteoblast differentiation of various cells in vitro. Therefore, BMPs are thought to be useful in bone regeneration medicine and for treating bone-related diseases. However, clinical application of BMPs is not widespread. Highlight BMP signal transduction and BMP-induced osteoblast differentiation are negatively regulated at several steps. BMP-3 acts as an antagonist to activin receptor type 2B and suppresses osteoblast differentiation of bone marrow stromal cells (BMSCs). Targeted disruption of Bmp-3 in mice increases trabecular bone formation and bone mass. A selective inhibitor of classical NF-κB pathway enhances BMP-2-induced ectopic bone formation in vivo. NF-κB inhibits BMP-induced osteoblast differentiation by directly targeting SMAD proteins. p65, the main subunit of NF-κB, interacts with SMAD4 and interferes with the DNA binding of SMAD complex, thus suppressing BMP-induced osteoblast differentiation. Transducin-like enhancer of split 3 (TLE3), a member of Groucho/TLE family, represses the transactivation of RUNX2, one of the master regulators of osteoblast differentiation, thus suppressing BMP-induced osteoblast differentiation of BMSCs. Conclusion In addition to BMP-3, NF-κB, and TLE3, numerous inhibitors suppress BMP-induced osteoblast differentiation. Therefore, a precise understanding of mechanisms underlying the inhibition of osteoblast differentiation may help develop novel methods for treating bone-related diseases or for the tissue engineering of the bone.. |
| 17. |
Min Zhang, Shoichiro Kokabu, Chihiro Nakatomi, Goro Sugiyama, Kou Matsuo, Eijiro Jimi, The Distinct Distributions of Immunocompetent Cells in Rat Dentin Pulp After Pulpotomy, Anatomical Record, 10.1002/ar.23087, 298, 4, 741-749, 2015.01, Pulpotomy involves the removal of the coronal portion of pulp, including the diseased tissue, with the intent of maintaining the vitality of the remaining pulpal tissue via a therapeutic dressing. Once odontoblasts suffer injuries, the differentiation of mesenchymal cells is induced from the precursor cell population in the dental pulp, and these cells are recruited to the injured site to differentiate into odontoblasts. However, the involvement of immunocompetent cells during pulpal regeneration remains unclear. Thus, the purpose of this study was to investigate the properties of macrophages that infiltrated wound healing sites in rats between 1 and 28 days after pulpotomy (dap). During the inflammatory phase, ED1+ (CD68+) macrophages significantly increased throughout root pulp, especially apical to the demarcation zone, and this population persisted until 3 dap before decreasing gradually until 28 dap. OX6+ macrophages expressing class II MHC also increased in the apical pulp at 1 dap and declined thereafter. However, OX6+ cells appeared prior to dentin bridge formation at 3 dap and appeared again apical to the dentin bridge during the healing stage at 14 dap. The shift from ED1+ cells in the inflammation phase to OX6+ cells during dentin bridge formation might contribute to wound healing. Anat Rec, 298:741-749, 2015.. |
| 18. |
Shizu Hirata-Tsuchiya, Hidefumi Fukushima, Takenobu Katagiri, Satoshi Ohte, Masashi Shin, Kenichi Nagano, Kazuhiro Aoki, Takahiko Morotomi, Goro Sugiyama, Chihiro Nakatomi, Shoichiro Kokabu, Takahiro Doi, Hiroshi Takeuchi, Keiichi Ohya, Masamichi Terashita, Masato Hirata, Chiaki Kitamura, Eijiro Jimi, Inhibition of BMP2-induced bone formation by the p65 subunit of NF-κB via an interaction with Smad4, Molecular Endocrinology, 10.1210/me.2014-1094, 28, 9, 1460-1470, 2014.09, Bone morphogenic proteins (BMPs) stimulate bone formation in vivo and osteoblast differentiation in vitro via a Smad signaling pathway. Recent findings revealed that the activation of nuclear factor-κB (NF-κB) inhibits BMP-induced osteoblast differentiation. Here, we show that NF-κB inhibits BMP signaling by directly targeting the Smad pathway. A selective inhibitor of the classic NF-κB pathway, BAY11-770682, enhanced BMP2-induced ectopic bone formation in vivo. In mouse embryonic fibroblasts (MEFs) prepared from mice deficient in p65, the main subunit of NF-κB, BMP2, induced osteoblastic differentiation via the Smad complex to a greater extent than that in wild-type MEFs. In p65(-/-) MEFs, the BMP2-activated Smad complex bound much more stably to the target element than that in wild-type MEFs without affecting the phosphorylation levels of Smad1/5/8. Overexpression of p65 inhibited BMP2 activity by decreasing the DNA binding of the Smad complex. The C-terminal region, including the TA2 domain, of p65 was essential for inhibiting the BMP-Smad pathway. The C-terminal TA2 domain of p65 associated with the MH1 domain of Smad4 but not Smad1. Taken together, our results suggest that p65 inhibits BMP signaling by blocking the DNA binding of the Smad complex via an interaction with Smad4. Our study also suggests that targeting the association between p65 and Smad4 may help to promote bone regeneration in the treatment of bone diseases.. |
| 19. |
Goro Sugiyama, Yukiko Ohyama, Tamotsu Kiyoshima, Mayumi Shimizu, Kaneki Eisuke, Yasuharu Takenoshita, Metastatic adenocarcinoma of the mandibular condyle from uterine cervix Report of a case, Oral Science International, 10.1016/S1348-8643(13)00028-1, 11, 1, 40-44, 2014.01, Metastasis to the mandibular condyle is rare, and such lesions should be identified by both clinical and pathological examinations. We experienced a case of adenocarcinoma occurring in the right mandibular condyle. A 65-year-old female with uterine cervical cancer showed condylar dysfunction. Imaging examinations revealed a tumor with bone destruction and a rapidly progressive course, while pathological examinations suggested metastasis originating from another site. Based on the clinical and pathological findings, the patient was diagnosed with condylar metastasis derived from the uterine cervix, in addition to a recurrence of uterine cervical cancer.. |
| 20. |
Tada, Yukiyo, Tada, Yukiyo, Kokabu, Shoichiro, Sugiyama, Goro, Nakatomi, Chihiro, Jimi, Eijiro, Jimi, Eijiro, Watanabe, Seiji, Aoki, Kazuhiro, Sugamori, Yasutaka, Ohya, Keiichi, Fukushima, Hidefumi, Osawa, Kenji, Okamoto, Masato, Fujikawa, Tomoyuki, Itai, Akiko, Matsuo, Kou, The novel IκB kinase β inhibitor IMD-0560 prevents bone invasion by oral squamous cell carcinoma, Oncotarget, 10.18632/oncotarget.2640, 5, 23, 12317-12330, 2014.01. |
| 21. |
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, Advances in Biological Regulation, 10.1016/j.jbior.2013.07.001, 53, 3, 331-340, 2013.01, PRIP, phospholipase C (PLC)-related but catalytically inactive protein is a protein with a domain organization similar to PLC-δ1. We have reported that PRIP interacts with the catalytic subunits of protein phosphatase 1 and 2A (PP1c and PP2Ac), depending on the phosphorylation of PRIP. We also found that Akt was precipitated along with PRIP by anti-PRIP antibody from neuronal cells. In this article, we summarize our current reach regarding the interaction of PRIP with Akt and protein phosphatases, in relation to the cellular phospho-regulations. PP1 and PP2A are major members of the protein serine/threonine phosphatase families. We have identified PP1 and PP2A as interacting partners of PRIP. We first investigated the interaction of PRIP with two phosphatases, using purified recombinant proteins. PRIP immobilized on beads pulled-down the catalytic subunits of both PP1 and PP2A, indicating that the interactions were in a direct manner, and the binding of PP1 and PP2A to PRIP were mutually exclusive. Site-directed mutagenesis experiments revealed that the binding sites for PP1 and PP2A on PRIP were not identical, but in close proximity. Phosphorylation of PRIP by protein kinase A (PKA) resulted in the reduced binding of PP1, but not PP2A. Rather, the dissociation of PP1 from PRIP by phosphorylation accompanied the increased binding of PP2A in invitro experiments. This binding regulation of PP1 and PP2A to PRIP by PKA-dependent phosphorylation was also observed in living cells treated with forskolin or isoproterenol. These results suggested that PRIP directly interacts with the catalytic subunits of two distinct phosphatases in a mutually exclusive manner and the interactions are regulated by phosphorylation, thus functioning as a scaffold to regulate the activities and subcellular localizations of both PP1 and PP2A in phospho-dependent cellular signaling.. |
| 22. |
Goro Sugiyama, Hiroshi Takeuchi, Koki Nagano, Jing Gao, Yukiko Ohyama, Yoshihide Mori, Masato Hirata, Regulated interaction of protein phosphatase 1 and protein phosphatase 2A with phospholipase C-related but catalytically inactive protein, Biochemistry, 10.1021/bi2018128, 51, 16, 3394-3403, 2012.04, Protein phosphatase 1 (PP1) and protein phosphatase 2A (PP2A) are major members of the protein serine/threonine phosphatase families. We have identified PP1 and PP2A as interacting partners of PRIP (phospholipase C-related but catalytically inactive protein), a protein isolated in our laboratory. We first investigated the interaction of PRIP with two phosphatases, using purified recombinant proteins. PRIP immobilized on beads pulled down the catalytic subunits of both PP1 and PP2A, indicating that the interactions were in a direct manner, and the binding of PP1 and the binding of PP2A to PRIP were mutually exclusive. Site-directed mutagenesis experiments revealed that the binding sites for PP1 and PP2A on PRIP were not identical, but similar. Phosphorylation of PRIP by protein kinase A (PKA) resulted in the weakened binding of PP1, but not PP2A. Rather, the dissociation of PP1 from PRIP by phosphorylation accompanied the strengthened binding of PP2A in in vitro experiments. This regulation of binding of PP1 and PP2A to PRIP by PKA-dependent phosphorylation was also observed in living cells treated with forskolin or isoproterenol. These results suggested that PRIP directly interacts with the catalytic subunits of two distinct phosphatases in a mutually exclusive manner and the interactions are regulated by phosphorylation, thus functioning as a scaffold to regulate the activities and subcellular localizations of both PP1 and PP2A in phospho-dependent cellular signaling.. |
| 23. |
Takeuchi Hiroshi, Zhang Zhao, Gao Jing, Sugiyama Goro, Takeuchi Takako, Hirata Masato, Second basic pockets contribute to the localization of PX domains by binding to phosphatidic acid, Advances in Biological Regulation, 10.1016/j.advenzreg.2011.09.006, 52, 1, 183-194, 2012.01. |
