Expression of heat shock protein 27 in the periodontium on the tension side during orthodontic tooth movement

doi:10.3969/j.issn.2095-4344.2017.08.009

Abstract

Abstract:

BACKGROUND: A large number of cytokines produce in the periodontium on the tension side during orthodontic tooth movement, participate in periodontal remodeling, and make the tooth move to its normal position, thus achieving alveolar remodeling. Heat shock protein 27 (HSP27) is reported to be involved in the periodontal remodeling.
OBJECTIVE: To investigate the expression of HSP27 in the rat periodontium on the tension side during the orthodontic tooth movement.
METHODS: The rat models of orthodontic tooth movement were constructed using NiTi coil spring with the force value of 50 g. The periodontal samples were collected at 1, 3, 5, 7, 10 and 14 days after exerting force to detect the expression level of HSP27 in the periodontium on the tension side.
RESULTS AND CONCLUSION: Immunofluorescence staining results revealed that the expression level of HSP27 in the periodontal tissues began to increase at the 1st day after exerting force, reached the highest level at the 3rd day, and then fell to the initial level at the 5th day. To conclude, HSP27 is evoked by orthodontic force early, and it may play a role in periodontal remodeling.

中国组织工程研究杂志出版内容重点：组织构建；骨细胞；软骨细胞；细胞培养；成纤维细胞；血管内皮细胞；骨质疏松；组织工程

Key words: Heat-Shock Proteins, Tooth, Orthodontics, Tissue Engineeirng

CLC Number:

R318

Nie Jing1, Li Ze-hui2, Jiang Han2, Pan Xu1, Li Chun-Xia1. Expression of heat shock protein 27 in the periodontium on the tension side during orthodontic tooth movement[J]. Chinese Journal of Tissue Engineering Research, 2017, 21(8): 1197-1201.

Figures/Tables 1

References

[1] Singh K, Agrawal NK, Gupta SK.Decreased expression of heat shock proteins may lead to compromised wound healing in type 2 diabetes mellitus patients.J Diabetes Complications. 2015;29(4):578-588.

[2] Guo JS, Cho CH, Wang JY,et al.Expression and immunolocalization of heat shock proteins in the healing of gastric ulcers in rats.Scand J Gastroenterol.2002; 37(1): 17-22.

[3] Gelmedin V, Delaney A, Jennelle L, et al.Expression profile of heat shock response factors during hookworm larval activation and parasitic development. Mol Biochem Parasitol. 2015;202(1):1-14

[4] Feder ME, Hofmann GE. Heat-shock proteins, molecular chaperones, and the stress response: evolutionary and ecological physiology.Annu Rev Physiol.1999;61:243-282.

[5] Tokunaga M, Baron B, Kitagawa T, et al.Active Hexose-correlated Compound Down-regulates Heat Shock Factor 1, a Transcription Factor for HSP27, in Gemcitabine-resistant Human Pancreatic Cancer Cells. Anticancer Res.2015;35(11):6063-6067

[6] Heikkila JJ. Heat shock protein gene expression and function in amphibian model systems.Comp Biochem Physiol A Mol Integr Physiol.2010;156(1):19-33.

[7] Nafar F, Williams JB, Mearow KM.Astrocytes release HspB1 in response to amyloid-β exposure in vitro.J Alzheimers Dis. 2016;49(1):251-263.

[8] Vidyasagar A, Wilson NA, Djamali A. Heat shock protein 27 (HSP27): biomarker of disease and therapeutic target. Fibrogenesis Tissue Repair. 2012;5(1):7

[9] Arrigo AP, Preville X. Role of Hsp25 related protein. Handbook of experimental pharmacology. 1999;136：101-132.

[10] Martinez-Rossi NM, Jacob TR, Sanches PR, et al.Heat Shock Proteins in Dermatophytes: Current Advances and Perspectives. Curr Genomics.2016;17(2):99-111.

[11] Tokuda H, Kuroyanagi G, Tsujimoto M, et al.Thrombin Receptor-Activating Protein (TRAP)-Activated Akt Is Involved in the Release of Phosphorylated-HSP27 (HSPB1) from Platelets in DM Patients.Int J Mol Sci.2016；14;17(5).

[12] Nitnavare RB, Yeshvekar RK, Sharma KK, et al.Molecular cloning, characterization and expression analysis of a heat shock protein 10 (Hsp10) from Pennisetum glaucum (L.), a C4 cereal plant from the semi-arid tropics.Mol Biol Rep. 2016; 43(8):861-870.

[13] Cybulsky AV, Guillemette J, Papillon J.Ste20-like kinase, SLK, activates the heat shock factor 1 - Hsp70 pathway.Biochim Biophys Acta. 2016 Sep;1863(9):2147-55

[14] Deforest WN,Hentscher-Johnson JK,Liu Y.Human tooth movement by continuous high and low stresses.Angle Orthod. 2014;84(1):102-108.

[15] Kirschneck C, Proff P, Maurer M, et al.Orthodontic forces add to nicotine-induced loss of periodontal bone : An in vivo and in vitro study. J Orofac Orthop.2015;76(3):195-212

[16] Ren Y, Maltha JC, Kuijpers-Jagtman AM.The rat as a model for orthodontic tooth movement--a critical review and a proposed solution.Eur J Orthod.2004;26(5):483-490.

[17] Christian K , Peter P, Jochen F.Differentiated analysis of orthodontic tooth movement in rats with an improved rat model and three-dimensional imaging. Ann Anat. 2013;195(6): 539-553.

[18] Sirisoontorn I,Hotokezaka H, Hashimoto M.Tooth movement and root resorption; The effect of ovariectomy on orthodontic force application in rats.The Angle Orthodontist.2011;81(4): 570-577.

[19] Jäger A, Zhang D, Kawarizadeh A, et al.Soluble cytokine receptor treatment in experimental orthodontic tooth movement in the rat. Eur J Orthod. 2005;27(1):1-11.

[20] Yamaguchi M.RANK/RANKL/OPG during orthodontic tooth movement. Orthod Craniofac Res.2009;12(2):113-119.

[21] Rody WJ Jr, King GJ, et al.Osteoclast recruitment to sites of compression in orthodontic tooth movement. Am J Orthod Dentofacial Orthop.2001；120(5)：477-489.

[22] Ikeda M, Yoshimura Y, Kikuiri T, et al.Release from optimal compressive force suppresses osteoclast differentiation.Mol Med Rep. 2016;14(5):4699-4705.

[23] Bakathir MA, Linjawi AI, Omar SS, et al.Effects of nicotine on bone during orthodontic tooth movement in male rats. Histological and immunohistochemical study.Saudi Med J. 2016;37(10):1127-1135

[24] Tang S, Chen H, Cheng Y, et al.Expression profiles of heat shock protein 27 and αB-crystallin and their effects on heat-stressed rat myocardial cells in vitro and in vivo.Mol Med Rep. 2016;13(2):1633-1638.

[25] Cele FN, Kumalo H, Soliman ME.Mechanism of Inhibition of Hsp90 Dimerization by Gyrase B Inhibitor Coumermycin A1 (C-A1) Revealed by Molecular Dynamics Simulations and Thermodynamic Calculations. Cell Biochem Biophys.2016; 74(3):353-363.

[26] Walsh D, Li Z, Wu Y, Nagata K.Heat shock and the role of the HSPs during neural plate induction in early mammalian CNS and brain development.Cell Mol Life.1997;53(2):198-211.

[27] Doberentz E, Führing S, Madea B.Sudden infant death syndrome: no significant expression of heat-shock proteins (HSP27, HSP70).Forensic Sci Med Pathol. 2016;12(1):33-39.

[28] Gong X, Ahner A, Roldan A, et al.Non-native Conformers of Cystic Fibrosis Transmembrane Conductance Regulator NBD1 Are Recognized by Hsp27 and Conjugated to SUMO-2 for Degradation.J Biol Chem. 2016;291(4):2004-2017.

[29] Tokunaga M, Baron B, Kitagawa T, et al. Active Hexose-correlated Compound Down-regulates Heat Shock Factor 1, a Transcription Factor for HSP27, in Gemcitabine-resistant Human Pancreatic Cancer Cells.Anticancer Res. 2015;35(11):6063-6067.

[30] Voll EA, Ogden IM, Pavese JM.Heat shock protein 27 regulates human prostate cancer cell motility and metastatic progression.Oncotarget.2014;5 (9): 2648–2663.

[31] Kato K,Adachi S,Matsushima-Nishiwaki R.Regulation by heat shock protein 27 of osteocalcin synthesis in osteoblasts. Endocrinology. 2011;152(5):1872-1882.

[32] Arrigo AP,Ducasse C.Expression of the anti- apoptotic protein Hsp27 during both the keratinocyte differentiation and dedifferentiation of HaCat cells:expression linked to changes in intracellular protein organization.Exp Gerontol. 2002;37: 1247-1255.

[33] Tsujimoto M, Kuroyanagi G, Matsushima-Nishiwaki R, et al.Factor Xa Inhibitor Suppresses the Release of Phosphorylated HSP27 from Collagen-Stimulated Human Platelets: Inhibition of HSP27 Phosphorylation via p44/p42 MAP Kinase.PLoS One. 2016 Feb 11;11(2)

[34] Park AM, Kanai K, Itoh T, et al. Heat Shock Protein 27 Plays a Pivotal Role in Myofibroblast Differentiation and in the Development of Bleomycin-Induced Pulmonary Fibrosis. PLoS One. 2016 Feb 9;11(2)

[35] Shochet GE, Komemi O, Sadeh-Mestechkin D, et al.Heat shock protein-27 (HSP27) regulates STAT3 and eIF4G levels in first trimester human placenta.J Mol Histol. 2016;47(6): 555-563

[36] Kato K, Tokuda H, Adachi S. Role of heat shock protein 27 in transforming growth factor-β-stimulated vascular endothelial growth factor release in osteoblasts.Int J Mol Med.2011; 27(3):423-428.

[37] Maki T, Keisuke N, Rina M. Immunohistochemical Changes of Heat Shock Protein 27 Expression in the Mouse Periodontal Tissues Exposed to Orthodontic Mechanical Stress.Journal of Hard Tissue Biology.2012;21(1):43-50.

[38] Muraoka R, Nakano K, Kurihara S, et al. Immunohistochemical expression of heat shock proteins in the mouse periodontal tissues due to orthodontic mechanical stress .Eur J Med Res.2010;15(11):475-482.

[39] Satoh JI.Differential expression of heat shock protein 27 in human neuronsand glial cellsin culture.J Neurosci Res.1995; 41(6):805- 818.

[40] Sookoian S, Castaño GO, Scian R, et al.Heat Shock Protein 27 is down-regulated in Ballooned Hepatocytes of Patients with Nonalcoholic Steatohepatitis (NASH).Sci Rep. 2016;6:22528

[41] Sreekanth GP, Chuncharunee A, Sirimontaporn A, et al. SB203580 Modulates p38 MAPK Signaling and Dengue Virus-Induced Liver Injury by Reducing MAPKAPK2, HSP27, and ATF2 Phosphorylation.LoS One. 2016;11(2):e0149486

[42] Booth L, Shuch B, Albers T, et al.Multi-kinase inhibitors can associate with heat shock proteins through their NH2-termini by which they suppress chaperone function.Oncotarget. 2016;7(11):12975-12996

[43] Kliková K, Pilchova I, Stefanikova A, et al.The Role of Heat Shock Proteins in Leukemia.Klin Onkol.2016;29(1):29-38