An in-vitro model for tooth eruption utilizing periodontal ligament fibroblasts and collagen lattices

1983 ◽  
Vol 28 (8) ◽  
pp. 715-722 ◽  
Author(s):  
C.G. Bellows ◽  
A.H. Melcher ◽  
J.E. Aubin
Keyword(s):  
Periodontal Ligament ◽  
In Vitro Model ◽  
Tooth Eruption ◽  
Periodontal Ligament Fibroblasts ◽  
Vitro Model ◽  
Collagen Lattices

scholarly journals Glycosaminoglycans accelerate biomimetic collagen mineralization in a tissue-based in vitro model

2020 ◽  
Vol 117 (23) ◽  
pp. 12636-12642 ◽  
Author(s):  
Magdalena Wojtas ◽  
Alexander J. Lausch ◽  
Eli D. Sone
Keyword(s):  
Protein Content ◽  
Periodontal Ligament ◽  
In Vitro Model ◽  
Enzymatic Digestion ◽  
Dental Tissues ◽  
Mineralized Tissues ◽  
Collagen Mineralization ◽  
Vitro Model

Mammalian teeth are attached to the jawbone through an exquisitely controlled mineralization process: unmineralized collagen fibers of the periodontal ligament anchor directly into the outer layer of adjoining mineralized tissues (cementum and bone). The sharp interface between mineralized and nonmineralized collagenous tissues makes this an excellent model to study the mechanisms by which extracellular matrix macromolecules control collagen mineralization. While acidic phosphoproteins, localized in the mineralized tissues, play key roles in control of mineralization, the role of glycosaminoglycans (GAGs) is less clear. As several proteoglycans are found only in the periodontal ligament, it has been hypothesized that these inhibit mineralization of collagen in this tissue. Here we used an in vitro model based on remineralization of mouse dental tissues to determine the role of matrix GAGs in control of mineralization. GAGs were selectively removed from demineralized mouse periodontal sections via enzymatic digestion. Proteomic analysis confirmed that enzymatic GAG removal does not significantly alter protein content. Analysis of remineralized tissue sections by transmission electron microscopy (TEM) shows that GAG removal reduced the rate of remineralization in mineralized tissues compared to the untreated control, while the ligament remained unmineralized. Protein removal with trypsin also reduced the rate of mineralization, but to a lesser extent than GAG removal, despite a much larger effect on protein content. These results indicate that GAGs promote mineralization in mineralized dental tissues rather than inhibiting mineral formation in the ligament, which may have broader implications for understanding control of collagen mineralization in connective tissues.

scholarly journals α11β1 Integrin-Dependent Regulation of Periodontal Ligament Function in the Erupting Mouse Incisor

2007 ◽  
Vol 27 (12) ◽  
pp. 4306-4316 ◽  
Author(s):  
Svetlana N. Popova ◽  
Malgorzata Barczyk ◽  
Carl-Fredrik Tiger ◽  
Wouter Beertsen ◽  
Paola Zigrino ◽  
...  
Keyword(s):  
Periodontal Ligament ◽  
Tooth Movement ◽  
Tooth Eruption ◽  
Collagen I ◽  
Periodontal Ligament Fibroblasts ◽  
Primary Defect ◽  
Embryonic Fibroblasts ◽  
Mouse Incisor

ABSTRACT The fibroblast integrin α11β1 is a key receptor for fibrillar collagens. To study the potential function of α11 in vivo, we generated a null allele of the α11 gene. Integrin α11−/− mice are viable and fertile but display dwarfism with increased mortality, most probably due to severely defective incisors. Mutant incisors are characterized by disorganized periodontal ligaments, whereas molar ligaments appear normal. The primary defect in the incisor ligament leads to halted tooth eruption. α11β1-defective embryonic fibroblasts displayed severe defects in vitro, characterized by (i) greatly reduced cell adhesion and spreading on collagen I, (ii) reduced ability to retract collagen lattices, and (iii) reduced cell proliferation. Analysis of matrix metalloproteinase in vitro and in vivo revealed disturbed MMP13 and MMP14 synthesis in α11−/− cells. We show that α11β1 is the major receptor for collagen I on mouse embryonic fibroblasts and suggest that α11β1 integrin is specifically required on periodontal ligament fibroblasts for cell migration and collagen reorganization to help generate the forces needed for axial tooth movement. Our data show a unique role for α11β1 integrin during tooth eruption.

Effect of 405-nm high-intensity narrow-spectrum light on fibroblast-populated collagen lattices: an in vitro model of wound healing

2011 ◽  
Vol 16 (4) ◽  
pp. 048003 ◽  
Author(s):  
Richard McDonald ◽  
Scott J. MacGregor ◽  
John G. Anderson ◽  
Michelle Maclean ◽  
M. Helen Grant
Keyword(s):  
Wound Healing ◽  
High Intensity ◽  
In Vitro Model ◽  
Narrow Spectrum ◽  
Vitro Model ◽  
Collagen Lattices

An in vitro model for investigation of vitamin A effects on wound healing

2021 ◽  
pp. 1-6
Author(s):  
Hoda Keshmiri Neghab ◽  
Mohammad Hasan Soheilifar ◽  
Gholamreza Esmaeeli Djavid
Keyword(s):  
Wound Healing ◽  
Endothelial Cell ◽  
Vitamin A ◽  
In Vitro Model ◽  
Cellular Proliferation ◽  
Endothelial Cell Migration ◽  
Normal Fibroblast ◽  
Anti Inflammatory ◽  
Vitro Model

Abstract. Wound healing consists of a series of highly orderly overlapping processes characterized by hemostasis, inflammation, proliferation, and remodeling. Prolongation or interruption in each phase can lead to delayed wound healing or a non-healing chronic wound. Vitamin A is a crucial nutrient that is most beneficial for the health of the skin. The present study was undertaken to determine the effect of vitamin A on regeneration, angiogenesis, and inflammation characteristics in an in vitro model system during wound healing. For this purpose, mouse skin normal fibroblast (L929), human umbilical vein endothelial cell (HUVEC), and monocyte/macrophage-like cell line (RAW 264.7) were considered to evaluate proliferation, angiogenesis, and anti-inflammatory responses, respectively. Vitamin A (0.1–5 μM) increased cellular proliferation of L929 and HUVEC (p < 0.05). Similarly, it stimulated angiogenesis by promoting endothelial cell migration up to approximately 4 fold and interestingly tube formation up to 8.5 fold (p < 0.01). Furthermore, vitamin A treatment was shown to decrease the level of nitric oxide production in a dose-dependent effect (p < 0.05), exhibiting the anti-inflammatory property of vitamin A in accelerating wound healing. These results may reveal the therapeutic potential of vitamin A in diabetic wound healing by stimulating regeneration, angiogenesis, and anti-inflammation responses.

Sign in / Sign up

Export Citation Format

Share Document