Role of HSP70 protein in human periodontal ligament cell function and physiology

Wolf, Michael and Marciniak, Jana and Lossdorfer, Stefan and Kirschneck, Christian and Brauner, Isabel and Goetz, Werner and Jaeger, Andreas (2019) Role of HSP70 protein in human periodontal ligament cell function and physiology. ANNALS OF ANATOMY-ANATOMISCHER ANZEIGER, 221. pp. 76-83. ISSN 0940-9602, 1618-0402

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Abstract

Objective: Heat pre-treatment of mechanically loaded human periodontal ligament cells (hPDL) dampens the inflammatory cellular response, as evidenced by a reduced expression of pro-inflammatory cytokines, inhibition of monocyte adhesion and osteoclastic differentiation. These findings imply heat shock proteins (HSP) as cell protective molecules acting in the PDL that are up-regulated upon ischemia caused by mechanical loading. HSP70 and its inhibition by VER155008 as the active agent in several pharmaceuticals are established targets and strategies, respectively, in the treatment of neoproliferative diseases. However, the effect of both players on periodontal remodeling in unknown. Therefore, we analyzed the role of HSP70 and its frequently used inhibitor VER155008 in the regulation of physiological hPDL cell functions and immune cell interaction. Materials and Methods: Fifth passage hPDL cells were cultured in the presence of 25 mu m HSP70 inactivating agent VER155008. At harvest, HSP70 expression, cell proliferation, and parameters of cell interaction, colony formation and wound healing were analyzed by means of real-time PCR, immunohistochemistry, Western blot, biochemical MTS assay, microscopy, and functional assays for monocyte adhesion and differentiation. Results: Basal HSP70 expression and hPDL cell morphology were not affected by HSP70 inhibitor VER155008. In contrast, cell proliferation, tissue defect healing, and colony formation were reduced significantly following HSP70 inhibition, whereas apoptosis and necrosis, monocyte adhesion and osteoclastic differentiation were markedly increased. Conclusions: The present data indicate a regulatory role for HSP70 protein in hPDL cell biology. (C) 2018 Published by Elsevier GmbH.

Item Type: Article
Uncontrolled Keywords: HEAT-SHOCK PROTEINS; SMALL-MOLECULE INHIBITOR; ANTICANCER ACTIVITY; GENE-EXPRESSION; IN-VITRO; HEAT-SHOCK-PROTEIN-70; INDUCTION; APOPTOSIS; CYTOKINES; PROLIFERATION; Heat shock proteins; Human PDL cells; Inhibitor VER155008; Proliferation; Wound healing
Subjects: 600 Technology > 610 Medical sciences Medicine
Divisions: Medicine > Lehrstuhl für Kieferorthopädie
Depositing User: Dr. Gernot Deinzer
Date Deposited: 22 Apr 2020 05:57
Last Modified: 22 Apr 2020 05:57
URI: https://pred.uni-regensburg.de/id/eprint/27858

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