Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 2013 May;84(5):694-703.
doi: 10.1902/jop.2012.120078. Epub 2012 Jul 6.

Tumor necrosis factor-α and Porphyromonas gingivalis lipopolysaccharides decrease periostin in human periodontal ligament fibroblasts

Miguel Padial-Molina  1 , Sarah L Volk, Juan C Rodriguez, Julie T Marchesan, Pablo Galindo-Moreno, Hector F Rios
Affiliations
Free article

Tumor necrosis factor-α and Porphyromonas gingivalis lipopolysaccharides decrease periostin in human periodontal ligament fibroblasts

Miguel Padial-Molina et al. J Periodontol. 2013 May.
Free article

Abstract

Background: Periostin is a matricellular protein essential for tissue integrity and maturation and is believed to have a key function as a modulator of periodontal ligament (PDL) homeostasis. The aim of this study is to evaluate whether periodontal disease-associated pathogen-related virulence factors (endotoxins/lipopolysaccharides [LPS]) and proinflammatory cytokines alter the expression of periostin in PDL cells.

Methods: Human PDL cultures were exposed to inflammatory mediators (tumor necrosis factor-α [TNF-α]), bacterial virulence factors (Porphyromonas gingivalis LPS) or a combination in a biomechanically challenged environment. Culture conditions were applied for 24 hours, 4 days, and 7 days. Periostin and TGF-β inducible gene clone H3 (βIGH3) mRNA expression from cell lysates were analyzed. Periostin and βIGH3 proteins were also detected and semiquantified in both cell lysates and cell culture supernatants by Western blot. In addition, periostin localization by immunofluorescence was performed. Analysis of variance and Fisher tests were used to define the statistical differences among groups (P <0.05).

Results: In a mechanically challenged environment, periostin protein was more efficiently incorporated into the matrix compared to the non-loaded controls (higher levels of periostin in the supernatant in the non-loaded group). Interestingly, chronic exposure to proinflammatory cytokines and/or microbial virulence factors significantly decreased periostin protein levels in the loaded cultures. There was greater variability on βIGH3 levels, and no particular pattern was clearly evident.

Conclusions: Inflammatory mediators (TNF-α) and bacterial virulence factors (P. gingivalis LPS) decrease periostin expression in human PDL fibroblasts. These results support a potential mechanism by which periostin alterations could act as a contributing factor during periodontal disease progression.

PubMed Disclaimer

Publication types