A Role for α11β1 Integrin in the Human Periodontal Ligament

Barczyk, Malgorzata; Olsen, L-H Borge; Franca, P da; Loos, Bruno G.; Mustafa, Kamal; Gullberg, Donald; Bolstad, Anne Isine

doi:10.1177/0022034509339291

Cited by 38 publications

(35 citation statements)

References 32 publications

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“…The collagen‐binding integrin α1β1 regulates MMP‐9 (Pozzi et al, 2000), α2β1 has been reported to regulate MMP‐1 and MMP‐13 (Langholz et al, 1995; Riikonen et al, 1995; Ravanti et al, 1999) and, in mouse embryonic fibroblasts (MEFs) α11β1 appears to regulate MMP‐13 activity (Popova et al, 2007a). In a previous study (Barczyk et al, 2009), we demonstrated robust α11 integrin expression in human healthy and periodontitis affected molar PDL tissue, as well as on fibroblasts established from human PDL tissue. Silencing of ITGA11 mRNA with siRNA resulted in reduced ability of PDL fibroblasts to reorganize collagen lattices.…”

mentioning

confidence: 49%

α11β1 integrin‐mediated MMP‐13‐dependent collagen lattice contraction by fibroblasts: Evidence for integrin‐coordinated collagen proteolysis

Barczyk

Lü

Popova

et al. 2013

Journal Cellular Physiology

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We have previously determined that integrin α11β1 is required on mouse periodontal ligament (PDL) fibroblasts to generate the force needed for incisor eruption. As part of the phenotype of α11(-/-) mice, the incisor PDL (iPDL) is thickened, due to disturbed matrix remodeling. To determine the molecular mechanism behind the disturbed matrix dynamics in the PDL we crossed α11(-/-) mice with the Immortomouse and isolated immortalized iPDL cells. Microarray analysis of iPDL cells cultured inside a 3D collagen gel demonstrated downregulated expression of a number of genes in α11-deficient iPDL cells, including matrix metalloproteinase-13 (MMP-13) and cathepsin K. α11(-/-) iPDL cells in vitro displayed disturbed interactions with collagen I during contraction of attached and floating collagen lattices and furthermore displayed reduced MMP-13 protein expression levels. The MMP-13 specific inhibitor WAY 170523 and the Cathepsin K Inhibitor II both blocked part of the α11 integrin-mediated collagen remodeling. In summary, our data demonstrate that in iPDL fibroblasts the mechanical strain generated by α11β1 integrin regulates molecules involved in collagen matrix dynamics. The positive regulation of α11β1-dependent matrix remodeling, involving MMP-13 and cathepsin K, might also occur in other types of fibroblasts and be an important regulatory mechanism for coordinated extracellular and intracellular collagen turnover in tissue homeostasis.

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mentioning

confidence: 49%

α11β1 integrin‐mediated MMP‐13‐dependent collagen lattice contraction by fibroblasts: Evidence for integrin‐coordinated collagen proteolysis

Barczyk

Lü

Popova

et al. 2013

Journal Cellular Physiology

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“…Therefore, we predicted that GroEL may induce the PDL cells migration mediating by the expression of integrins α1 and α2. Additionally, previous evidences showed integrins α10β1 and integrins α11β1 regulate human PDL cells activation [62], [63]. Whether P. gingivalis GroEL affects the expression of integrins α10β1 and α11β1 remain to be elucidated.…”

Section: Discussionmentioning

confidence: 94%

Porphyromonas gingivalis GroEL Induces Osteoclastogenesis of Periodontal Ligament Cells and Enhances Alveolar Bone Resorption in Rats

Lin

Hsiao²,

Huang

et al. 2014

PLoS ONE

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Porphyromonas gingivalis is a major periodontal pathogen that contains a variety of virulence factors. The antibody titer to P. gingivalis GroEL, a homologue of HSP60, is significantly higher in periodontitis patients than in healthy control subjects, suggesting that P. gingivalis GroEL is a potential stimulator of periodontal disease. However, the specific role of GroEL in periodontal disease remains unclear. Here, we investigated the effect of P. gingivalis GroEL on human periodontal ligament (PDL) cells in vitro, as well as its effect on alveolar bone resorption in rats in vivo. First, we found that stimulation of PDL cells with recombinant GroEL increased the secretion of the bone resorption-associated cytokines interleukin (IL)-6 and IL-8, potentially via NF-κB activation. Furthermore, GroEL could effectively stimulate PDL cell migration, possibly through activation of integrin α1 and α2 mRNA expression as well as cytoskeletal reorganization. Additionally, GroEL may be involved in osteoclastogenesis via receptor activator of nuclear factor κ-B ligand (RANKL) activation and alkaline phosphatase (ALP) mRNA inhibition in PDL cells. Finally, we inoculated GroEL into rat gingiva, and the results of microcomputed tomography (micro-CT) and histomorphometric assays indicated that the administration of GroEL significantly increased inflammation and bone loss. In conclusion, P. gingivalis GroEL may act as a potent virulence factor, contributing to osteoclastogenesis of PDL cells and resulting in periodontal disease with alveolar bone resorption.

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“…A previous study 75 showed that α 11 β 1 is the major receptor for collagen I on mouse embryonic fibroblasts and suggested that α 11 β 1 integrin is particularly essential in PDL fibroblasts for cell migration and collagen reorganization to help generate the forces needed for axial tooth movement. Specifically, α 11 β 1 is a major collagen receptor on cultured HPDL cells, which implies that it is also functionally important in HPDLs in vivo 76 . Moreover, the expression of the αvβ6 integrin was downregulated in human periodontal disease and also contributed to the development of cardiovascular diseases by increasing the total systemic inflammatory burden 67 .…”

Section: Discussionmentioning

confidence: 99%

Antioxidants Counteract Nicotine and Promote Migration via RacGTP in Oral Fibroblast Cells

Miguel

Opperman

Allen

et al. 2010

Journal of Periodontology

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Treatment with AO combinations clearly counteracted the effects of nicotine by restoring and increasing cell-migration rates. We found the combination of PFR was the most effective in HGFs, whereas, RFT was the most effective combination in HPDL fibroblast. These results clearly demonstrate that PF, RFT, and PFR counteract the negative effects of nicotine on cultured oral fibroblasts via the RacGTP signal-transduction pathway.

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A Role for α11β1 Integrin in the Human Periodontal Ligament

Cited by 38 publications

References 32 publications

α11β1 integrin‐mediated MMP‐13‐dependent collagen lattice contraction by fibroblasts: Evidence for integrin‐coordinated collagen proteolysis

α11β1 integrin‐mediated MMP‐13‐dependent collagen lattice contraction by fibroblasts: Evidence for integrin‐coordinated collagen proteolysis

Porphyromonas gingivalis GroEL Induces Osteoclastogenesis of Periodontal Ligament Cells and Enhances Alveolar Bone Resorption in Rats

Antioxidants Counteract Nicotine and Promote Migration via RacGTP in Oral Fibroblast Cells

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