Acknowledgement
This study was supported by the National Research Foundation of Korea through the Ministry of Education (2022R1I1A1A01070644) and by the Ministry of Science and ICT (2022R1F1A1069624).
References
- Schwarz DS, Blower MD. The endoplasmic reticulum: structure, function and response to cellular signaling. Cell Mol Life Sci 2016;73:79-94. https://doi.org/10.1007/s00018-015-2052-6
- Almanza A, Carlesso A, Chintha C, Creedican S, Doultsinos D, Leuzzi B, et al. Endoplasmic reticulum stress signalling - from basic mechanisms to clinical applications. FEBS J 2019;286:241-78. https://doi.org/10.1111/febs.14608
- Hetz C, Zhang K, Kaufman RJ. Mechanisms, regulation and functions of the unfolded protein response. Nat Rev Mol Cell Biol 2020;21:421-38. https://doi.org/10.1038/s41580-020-0250-z
- Marciniak SJ. Endoplasmic reticulum stress: a key player in human disease. FEBS J 2019;286:228-31. https://doi.org/10.1111/febs.14740
- Kropski JA, Blackwell TS. Endoplasmic reticulum stress in the pathogenesis of fibrotic disease. J Clin Invest 2018;128:64-73. https://doi.org/10.1172/JCI93560
- Arksey H, O'Malley L. Scoping studies: towards a methodological framework. Int J Soc Res Methodol 2005;8:19-32. https://doi.org/10.1080/1364557032000119616
- Kim DS, Kim JH, Lee GH, Kim HT, Lim JM, Chae SW, et al. p38 Mitogen-activated protein kinase is involved in endoplasmic reticulum stress-induced cell death and autophagy in human gingival fibroblasts. Biol Pharm Bull 2010;33:545-9. https://doi.org/10.1248/bpb.33.545
- Kim DS, Li B, Rhew KY, Oh HW, Lim HD, Lee W, et al. The regulatory mechanism of 4-phenylbutyric acid against ER stress-induced autophagy in human gingival fibroblasts. Arch Pharm Res 2012;35:1269-78. https://doi.org/10.1007/s12272-012-0718-2
- Domon H, Takahashi N, Honda T, Nakajima T, Tabeta K, Abiko Y, et al. Up-regulation of the endoplasmic reticulum stress-response in periodontal disease. Clin Chim Acta 2009;401:134-40. https://doi.org/10.1016/j.cca.2008.12.007
- Yamada H, Nakajima T, Domon H, Honda T, Yamazaki K. Endoplasmic reticulum stress response and bone loss in experimental periodontitis in mice. J Periodontal Res 2015;50:500-8. https://doi.org/10.1111/jre.12232
- Hayashi C, Fukuda T, Kawakami K, Toyoda M, Nakao Y, Watanabe Y, et al. miR-1260b inhibits periodontal bone loss by targeting ATF6β mediated regulation of ER stress. Front Cell Dev Biol 2022;10:1061216. https://doi.org/10.3389/fcell.2022.1061216
- Ranga Rao S, Subbarayan R, Ajitkumar S, Murugan Girija D. 4PBA strongly attenuates endoplasmic reticulum stress, fibrosis, and mitochondrial apoptosis markers in cyclosporine treated human gingival fibroblasts. J Cell Physiol 2018;233:60-6. https://doi.org/10.1002/jcp.25836
- Rao SR, Ajitkumar S, Subbarayan R, Girija DM. Cyclosporine-A induces endoplasmic reticulum stress in human gingival fibroblasts - an in vitro study. J Oral Biol Craniofac Res 2018;8:165-7. https://doi.org/10.1016/j.jobcr.2016.11.002
- Katsiougiannis S, Tenta R, Skopouli FN. Endoplasmic reticulum stress causes autophagy and apoptosis leading to cellular redistribution of the autoantigens Ro/Sjogren's syndrome-related antigen A (SSA) and La/SSB in salivary gland epithelial cells. Clin Exp Immunol 2015;181:244-52. https://doi.org/10.1111/cei.12638
- Kaira K, Toyoda M, Shimizu A, Shino M, Sakakura K, Takayasu Y, et al. Expression of ER stress markers (GRP78/BiP and PERK) in adenoid cystic carcinoma. Acta Otolaryngol 2016;136:1-7. https://doi.org/10.3109/00016489.2015.1083120
- Giampietri C, Petrungaro S, Conti S, Facchiano A, Filippini A, Ziparo E. Cancer microenvironment and endoplasmic reticulum stress response. Mediators Inflamm 2015;2015:417281. https://doi.org/10.1155/2015/417281
- Yakin M, Seo B, Rich A. Tunicamycin-induced endoplasmic reticulum stress up-regulates tumour-promoting cytokines in oral squamous cell carcinoma. Cytokine 2019;120:130-43. https://doi.org/10.1016/j.cyto.2019.04.013
- Seo B, Coates DE, Lewis J, Seymour GJ, Rich AM. Unfolded protein response is involved in the metabolic and apoptotic regulation of oral squamous cell carcinoma. Pathology 2022;54:874-81. https://doi.org/10.1016/j.pathol.2022.04.003
- Ohata Y, Tsuchiya M, Hirai H, Yamaguchi S, Akashi T, Sakamoto K, et al. Leukemia inhibitory factor produced by fibroblasts within tumor stroma participates in invasion of oral squamous cell carcinoma. PLoS One 2018;13:e0191865. https://doi.org/10.1371/journal.pone.0191865
- Ping Q, Yan R, Cheng X, Wang W, Zhong Y, Hou Z, et al. Cancer-associated fibroblasts: overview, progress, challenges, and directions. Cancer Gene Ther 2021;28:984-99. https://doi.org/10.1038/s41417-021-00318-4
- Bu L, Baba H, Yoshida N, Miyake K, Yasuda T, Uchihara T, et al. Biological heterogeneity and versatility of cancer-associated fibroblasts in the tumor microenvironment. Oncogene 2019;38:4887-901. https://doi.org/10.1038/s41388-019-0765-y
- Sahai E, Astsaturov I, Cukierman E, DeNardo DG, Egeblad M, Evans RM, et al. A framework for advancing our understanding of cancer-associated fibroblasts. Nat Rev Cancer 2020;20:174-86. https://doi.org/10.1038/s41568-019-0238-1
- Yang D, Liu J, Qian H, Zhuang Q. Cancer-associated fibroblasts: from basic science to anticancer therapy. Exp Mol Med 2023;55:1322-32. https://doi.org/10.1038/s12276-023-01013-0
- Joshi R, Tawfik A, Edeh N, McCloud V, Looney S, Lewis J, et al. Dentin sialophosphoprotein (DSPP) gene-silencing inhibits key tumorigenic activities in human oral cancer cell line, OSC2. PLoS One 2010;5:e13974. https://doi.org/10.1371/journal.pone.0013974
- Gkouveris I, Nikitakis NG, Aseervatham J, Ogbureke KUE. The tumorigenic role of DSPP and its potential regulation of the unfolded protein response and ER stress in oral cancer cells. Int J Oncol 2018;53:1743-51. https://doi.org/10.3892/ijo.2018.4484
- Nikoloudaki G, Creber K, Hamilton DW. Wound healing and fibrosis: a contrasting role for periostin in skin and the oral mucosa. Am J Physiol Cell Physiol 2020;318:C1065-77. https://doi.org/10.1152/ajpcell.00035.2020
- Squier CA, Kremer MJ. Biology of oral mucosa and esophagus. J Natl Cancer Inst Monogr 2001;2001:7-15. https://doi.org/10.1093/oxfordjournals.jncimonographs.a003443
- Groeger SE, Meyle J. Epithelial barrier and oral bacterial infection. Periodontol 2000 2015;69:46-67. https://doi.org/10.1111/prd.12094
- Groeger S, Meyle J. Oral mucosal epithelial cells. Front Immunol 2019;10:208. https://doi.org/10.3389/fimmu.2019.00208
- Kabakov L, Nemcovsky CE, Plasmanik-Chor M, Meir H, Bar DZ, Weinberg E. Fibroblasts from the oral masticatory and lining mucosa have different gene expression profiles and proliferation rates. J Clin Periodontol 2021;48:1393-401. https://doi.org/10.1111/jcpe.13532
- Kashima TG, Nishiyama T, Shimazu K, Shimazaki M, Kii I, Grigoriadis AE, et al. Periostin, a novel marker of intramembranous ossification, is expressed in fibrous dysplasia and in c-Fos-overexpressing bone lesions. Hum Pathol 2009;40:226-37. https://doi.org/10.1016/j.humpath.2008.07.008
- Chau E, Daley T, Darling MR, Hamilton D. The expression and immunohistochemical localization of periostin in odontogenic tumors of mixed epithelial/mesenchymal origin. Oral Surg Oral Med Oral Pathol Oral Radiol 2013;116:214-20. https://doi.org/10.1016/j.oooo.2013.05.008
- Siriwardena BS, Kudo Y, Ogawa I, Kitagawa M, Kitajima S, Hatano H, et al. Periostin is frequently overexpressed and enhances invasion and angiogenesis in oral cancer. Br J Cancer 2006;95:1396-403. https://doi.org/10.1038/sj.bjc.6603431
- Wiseman RL, Mesgarzadeh JS, Hendershot LM. Reshaping endoplasmic reticulum quality control through the unfolded protein response. Mol Cell 2022;82:1477-91. https://doi.org/10.1016/j.molcel.2022.03.025
- So JS. Roles of endoplasmic reticulum stress in immune responses. Mol Cells 2018;41:705-16. https://doi.org/10.14348/molcells.2018.0241
- Park K, Lee SE, Shin KO, Uchida Y. Insights into the role of endoplasmic reticulum stress in skin function and associated diseases. FEBS J 2019;286:413-25. https://doi.org/10.1111/febs.14739
- Heindryckx F, Binet F, Ponticos M, Rombouts K, Lau J, Kreuger J, et al. Endoplasmic reticulum stress enhances fibrosis through IRE1α-mediated degradation of miR-150 and XBP-1 splicing. EMBO Mol Med 2016;8:729-44. https://doi.org/10.15252/emmm.201505925
- Kranz P, Neumann F, Wolf A, Classen F, Pompsch M, Ocklenburg T, et al. PDI is an essential redox-sensitive activator of PERK during the unfolded protein response (UPR). Cell Death Dis 2017;8:e2986. https://doi.org/10.1038/cddis.2017.369
- Eletto D, Eletto D, Dersh D, Gidalevitz T, Argon Y. Protein disulfide isomerase A6 controls the decay of IRE1α signaling via disulfide-dependent association. Mol Cell 2014;53:562-76. https://doi.org/10.1016/j.molcel.2014.01.004
- Higa A, Taouji S, Lhomond S, Jensen D, Fernandez-Zapico ME, Simpson JC, et al. Endoplasmic reticulum stress-activated transcription factor ATF6α requires the disulfide isomerase PDIA5 to modulate chemoresistance. Mol Cell Biol 2014;34:1839-49. https://doi.org/10.1128/MCB.01484-13
- Oeckinghaus A, Ghosh S. The NF-kappaB family of transcription factors and its regulation. Cold Spring Harb Perspect Biol 2009;1:a000034. https://doi.org/10.1101/cshperspect.a000034
- Schroder M. Endoplasmic reticulum stress responses. Cell Mol Life Sci 2008;65:862-94. https://doi.org/10.1007/s00018-007-7383-5
- Kelley N, Jeltema D, Duan Y, He Y. The NLRP3 inflammasome: an overview of mechanisms of activation and regulation. Int J Mol Sci 2019;20:3328. https://doi.org/10.3390/ijms20133328
- Papaliagkas V, Anogianaki A, Anogianakis G, Ilonidis G. The proteins and the mechanisms of apoptosis: a mini-review of the fundamentals. Hippokratia 2007;11:108-13.
- Kim H, Tu HC, Ren D, Takeuchi O, Jeffers JR, Zambetti GP, et al. Stepwise activation of BAX and BAK by tBID, BIM, and PUMA initiates mitochondrial apoptosis. Mol Cell 2009;36:487-99. https://doi.org/10.1016/j.molcel.2009.09.030
- Garrido C, Galluzzi L, Brunet M, Puig PE, Didelot C, Kroemer G. Mechanisms of cytochrome c release from mitochondria. Cell Death Differ 2006;13:1423-33. https://doi.org/10.1038/sj.cdd.4401950
- Elmore S. Apoptosis: a review of programmed cell death. Toxicol Pathol 2007;35:495-516. https://doi.org/10.1080/01926230701320337
- Wegner KW, Saleh D, Degterev A. Complex pathologic roles of RIPK1 and RIPK3: moving beyond necroptosis. Trends Pharmacol Sci 2017;38:202-25. https://doi.org/10.1016/j.tips.2016.12.005
- Seo J, Nam YW, Kim S, Oh DB, Song J. Necroptosis molecular mechanisms: recent findings regarding novel necroptosis regulators. Exp Mol Med 2021;53:1007-17. https://doi.org/10.1038/s12276-021-00634-7
- Saveljeva S, Mc Laughlin SL, Vandenabeele P, Samali A, Bertrand MJ. Endoplasmic reticulum stress induces ligand-independent TNFR1-mediated necroptosis in L929 cells. Cell Death Dis 2015;6:e1587. https://doi.org/10.1038/cddis.2014.548
- Bernales S, McDonald KL, Walter P. Autophagy counterbalances endoplasmic reticulum expansion during the unfolded protein response. PLoS Biol 2006;4:e423. https://doi.org/10.1371/journal.pbio.0040423
- Sano R, Reed JC. ER stress-induced cell death mechanisms. Biochim Biophys Acta 2013;1833:3460-70. https://doi.org/10.1016/j.bbamcr.2013.06.028
- Binet F, Sapieha P. ER Stress and angiogenesis. Cell Metab 2015;22:560-75. https://doi.org/10.1016/j.cmet.2015.07.010
- Ghosh R, Lipson KL, Sargent KE, Mercurio AM, Hunt JS, Ron D, et al. Transcriptional regulation of VEGF-A by the unfolded protein response pathway. PLoS One 2010;5:e9575. https://doi.org/10.1371/journal.pone.0009575
- Gargalovic PS, Imura M, Zhang B, Gharavi NM, Clark MJ, Pagnon J, et al. Identification of inflammatory gene modules based on variations of human endothelial cell responses to oxidized lipids. Proc Natl Acad Sci U S A 2006;103:12741-6. https://doi.org/10.1073/pnas.0605457103
- Li A, Dubey S, Varney ML, Dave BJ, Singh RK. IL-8 directly enhanced endothelial cell survival, proliferation, and matrix metalloproteinases production and regulated angiogenesis. J Immunol 2003;170:3369-76. https://doi.org/10.4049/jimmunol.170.6.3369
- Pereira ER, Liao N, Neale GA, Hendershot LM. Transcriptional and post-transcriptional regulation of proangiogenic factors by the unfolded protein response. PLoS One 2010;5:e12521. https://doi.org/10.1371/journal.pone.0012521
- Ribatti D, Tamma R, Annese T. Epithelial-mesenchymal transition in cancer: a historical overview. Transl Oncol 2020;13:100773. https://doi.org/10.1016/j.tranon.2020.100773
- Feng YX, Sokol ES, Del Vecchio CA, Sanduja S, Claessen JH, Proia TA, et al. Epithelial-to-mesenchymal transition activates PERK-eIF2α and sensitizes cells to endoplasmic reticulum stress. Cancer Discov 2014;4:702-15. https://doi.org/10.1158/2159-8290.CD-13-0945
- Moon SY, Kim HS, Nho KW, Jang YJ, Lee SK. Endoplasmic reticulum stress induces epithelial-mesenchymal transition through autophagy via activation of c-Src kinase. Nephron Exp Nephrol 2014;126:127-40. https://doi.org/10.1159/000362457
- Chang YJ, Chen WY, Huang CY, Liu HH, Wei PL. Glucose-regulated protein 78 (GRP78) regulates colon cancer metastasis through EMT biomarkers and the NRF-2/HO-1 pathway. Tumour Biol 2015;36:1859-69. https://doi.org/10.1007/s13277-014-2788-x