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Journal articles on the topic 'Periodontal ligament Anatomy'

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Published: 4 June 2021
Last updated: 5 February 2022

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1

Becker, J., D. Schuppan, J. P. Rabanus, R. Rauch, U. Niechoy, and H. R. Gelderblom. "Immunoelectron microscopic localization of collagens type I, V, VI and of procollagen type III in human periodontal ligament and cementum." Journal of Histochemistry & Cytochemistry 39, no. 1 (January 1991): 103–10. http://dx.doi.org/10.1177/39.1.1983870.

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We examined the ultrastructural localization of collagens Type I, V, VI and of procollagen Type III in decalcified and prefixed specimens of the periodontal ligament and cementum, by immunoelectron microscopy using ultra-thin cryostat sections. Immunostaining for collagen Type I was pronounced on the major cross-striated fibrils entering cementum and in cementum proper, whereas staining for procollagen Type III was almost exclusively observed on the major fibrils in the periodontal ligament situated more remote from cementum. Reactivity for collagen Type V was limited to aggregated, unbanded filamentous material of about 12 nm diameter that was found mainly in larger spaces between bundles of cross-striated collagen fibrils and occasionally on single microfibrils that apparently originated from the ends of the major collagen fibrils, which may support the concept of this collagen as a component of core fibrils. Collagen Type VI was present as microfilaments appearing to interconnect single cross-striated fibrils. In the densely packed fibril bundles of the periodontal ligament, no collagen type VI was detected. Neither Type V or Type VI collagen was observed in cementum.
2

Häkkinen, L., O. Oksala, T. Salo, F. Rahemtulla, and H. Larjava. "Immunohistochemical localization of proteoglycans in human periodontium." Journal of Histochemistry & Cytochemistry 41, no. 11 (November 1993): 1689–99. http://dx.doi.org/10.1177/41.11.8409375.

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Proteoglycans (PGs) are extracellular and cell surface-associated macromolecules that regulate cell adhesion, cell growth, matrix formation, and bind growth factors. In this work we studied the distribution of core proteins of four PGs (decorin, biglycan, a large molecular weight PG, and CD44) in human gingiva and periodontal ligament by immunohistochemical staining of frozen tissue sections with specific antibodies. Decorin, a major PG of this tissue, was localized on collagen fiber bundles in the gingival and periodontal connective tissues. Staining for decorin was most intense at the subepithelial region. Biglycan was a minor PG component of the human periodontium, showing some accumulation in connective tissue under the oral epithelium. At the immunohistochemical level, biglycan appeared to form fine filament-like structures on extracellular matrix fibers. Localization of large molecular weight PG differed from that of decorin and biglycan. It was concentrated in deep connective tissue areas of the gingiva and in the periodontal ligament, and was only weakly present at the subepithelial region. CD44 was mainly concentrated in cell-cell contact areas of basal and spinous layers of oral epithelium. In the connective tissue of gingiva and periodontal ligament, CD44 was localized on fibroblast cell surfaces. Connective tissue area under the junctional epithelium contained relatively small amounts of PGs. The results indicate that different parts of human periodontium contain a typical variety of PGs, suggesting a specific function for each PG species in the location at which they accumulate.
3

de Jong, T., A. D. Bakker, V. Everts, and T. H. Smit. "The intricate anatomy of the periodontal ligament and its development: Lessons for periodontal regeneration." Journal of Periodontal Research 52, no. 6 (June 21, 2017): 965–74. http://dx.doi.org/10.1111/jre.12477.

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4

Sawada, Takashi, Yuu Sugawara, Tomohiro Asai, Natsuko Aida, Takaaki Yanagisawa, Kazumasa Ohta, and Sadayuki Inoue. "Immunohistochemical Characterization of Elastic System Fibers in Rat Molar Periodontal Ligament." Journal of Histochemistry & Cytochemistry 54, no. 10 (June 16, 2006): 1095–103. http://dx.doi.org/10.1369/jhc.5a6905.2006.

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5

Abuduwali, Nuersailike, Stefan Lossdörfer, Jochen Winter, Michael Wolf, Werner Götz, and Andreas Jäger. "Autofluorescent characteristics of human periodontal ligament cells in vitro." Annals of Anatomy - Anatomischer Anzeiger 195, no. 5 (October 2013): 449–54. http://dx.doi.org/10.1016/j.aanat.2013.03.007.

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6

McCulloch, C. A. G. "Progenitor cell populations in the periodontal ligament of mice." Anatomical Record 211, no. 3 (March 1985): 258–62. http://dx.doi.org/10.1002/ar.1092110305.

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7

Cho, Moon-Il, and Philias R. Garant. "3H-mannose utilization by fibroblasts of the periodontal ligament." Anatomical Record 218, no. 1 (May 1987): 5–13. http://dx.doi.org/10.1002/ar.1092180103.

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8

Oehmke, Matthias J., Christopher R. C. Schramm, Erich Knolle, Nathalie Frickey, Thomas Bernhart, and Hans-Joachim Oehmke. "Age-dependent changes of the periodontal ligament in rats." Microscopy Research and Technique 63, no. 4 (2004): 198–202. http://dx.doi.org/10.1002/jemt.20027.

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9

Nagai, Nobuhiro, Ayumi Hirakawa, Nao Otani, and Masanobu Munekata. "Development of Tissue-Engineered Human Periodontal Ligament Constructs with Intrinsic Angiogenic Potential." Cells Tissues Organs 190, no. 6 (2009): 303–12. http://dx.doi.org/10.1159/000213247.

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10

Hirashima, Shingo, Tomonoshin Kanazawa, Keisuke Ohta, and Kei-ichiro Nakamura. "Three-dimensional ultrastructural imaging and quantitative analysis of the periodontal ligament." Anatomical Science International 95, no. 1 (September 10, 2019): 1–11. http://dx.doi.org/10.1007/s12565-019-00502-5.

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11

Roberts, W. Eugene, and Emily R. Morey. "Proliferation and differentiation sequence of osteoblast histogenesis under physiological conditions in rat periodontal ligament." American Journal of Anatomy 174, no. 2 (October 1985): 105–18. http://dx.doi.org/10.1002/aja.1001740202.

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12

Tung, P. S., C. Domenicucci, S. Wasi, and J. Sodek. "Specific immunohistochemical localization of osteonectin and collagen types I and III in fetal and adult porcine dental tissues." Journal of Histochemistry & Cytochemistry 33, no. 6 (June 1985): 531–40. http://dx.doi.org/10.1177/33.6.3889139.

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Affinity-purified antibodies have been used in combination with the peroxidase-antiperoxidase technique to study the distribution of osteonectin and collagen types I and III in porcine dental tissues. Tissue sections (2 mm thick), including unerupted (fetal) or erupted (adult) teeth, were fixed in periodate-lysine-paraformaldehyde, demineralized in 12% w/v ethylenediaminetetraacetic acid, and after embedding, 6 micron sections were prepared for immunolocalization. Strong staining for osteonectin was observed in dentine of unerupted teeth and in the associated alveolar bone. Light to moderate staining was observed in the dental pulp, stratum intermedium, stellate reticulum, and the reticular elements in the endosteal spaces. In erupted teeth, osteonectin staining in dentine was concentrated around dentinal tubules and the associated alveolar bone stained with variable intensity. Cementum was poorly stained. However, the periodontal ligament and reticular material in the endosteal spaces showed moderate to strong staining. Weaker staining was apparent in the pulp and lamina propria of the gingiva. In comparison, type I collagen showed a similar distribution to osteonectin in both fetal and adult tissues, whereas type III collagen was generally restricted to the periodontal ligament, reticular elements of the endosteal spaces, and Sharpey's fibers in bone and cementum. Both odontoblast and ameloblast layers in fetal tissues stained for osteonectin and type III collagen.
13

Michaeli, Y., M. Weinreb, A. Barad, and S. Steigman. "Three-dimensional presentation of the fibroblast progenitor compartment in the periodontal ligament of the rat incisor." American Journal of Anatomy 180, no. 3 (November 1987): 243–48. http://dx.doi.org/10.1002/aja.1001800305.

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14

Lekic, P. C., D. Rajshankar, H. Chen, H. Tenenbaum, and C. A. G. MCculloch. "Transplantation of labeled periodontal ligament cells promotes regeneration of alveolar bone." Anatomical Record 262, no. 2 (2001): 193–202. http://dx.doi.org/10.1002/1097-0185(20010201)262:2<193::aid-ar1028>3.0.co;2-7.

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15

Wolf, Michael, Jana Marciniak, Stefan Lossdörfer, Christian Kirschneck, Isabel Brauner, Werner Götz, and Andreas Jäger. "Role of HSP70 protein in human periodontal ligament cell function and physiology." Annals of Anatomy - Anatomischer Anzeiger 221 (January 2019): 76–83. http://dx.doi.org/10.1016/j.aanat.2018.09.006.

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16

Komatsu, K., Y. Yamazaki, S. Yamaguchi, and M. Chiba. "Comparison of biomechanical properties of the incisor periodontal ligament among different species." Anatomical Record 250, no. 4 (April 1998): 408–17. http://dx.doi.org/10.1002/(sici)1097-0185(199804)250:4<408::aid-ar3>3.0.co;2-t.

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17

Takano-Yamamoto, T., T. Takemura, Y. Kitamura, and S. Nomura. "Site-specific expression of mRNAs for osteonectin, osteocalcin, and osteopontin revealed by in situ hybridization in rat periodontal ligament during physiological tooth movement." Journal of Histochemistry & Cytochemistry 42, no. 7 (July 1994): 885–96. http://dx.doi.org/10.1177/42.7.8014472.

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We investigated the gene expression for non-collagenous proteins in periodontal ligament (PDL) by in situ hybridization histochemistry with a non-radioisotopic probe with cRNAs for osteocalcin (Osc), osteonectin (Osn), and osteopontin (Opn) in rat maxillary dento-alveolar unit containing molars and intact PDL. A highly intense positive signal for Osn and Osc mRNAs was expressed at all distal surfaces of the interradicular septum of buccal roots of the upper second molar in 7-week-old Sprague-Dawley male rats. Cells showing positive signals for Osn and Osc mRNAs were osteoblasts and osteoprogenitor cells. The distribution of Opn mRNA-positive signal was demonstrable at the mesial surface of the interradicular septum of buccal roots, where physiological bone resorption was specifically restricted during physiological tooth movement. Opn mRNA was expressed in cells on the bone resorption surface, including osteoclasts, and osteocytes. A moderately intense positive signal for Osn mRNA was distributed in fibroblasts throughout the ligament. Odontoblasts and pre-mature odontoblasts exhibited a strong signal for Osn and Osc mRNA. Cementoblasts and cementocytes were positive for Osn, Osc, and Opn mRNAs. These findings suggest physiological roles of Osc, Osn, and Opn in bone remodeling, PDL remodeling, dentinogenesis, and cementogenesis.
18

Sloan, P., D. H. Carter, C. M. Kielty, and C. A. Shuttleworth. "An immunohistochemical study examining the role of collagen type VI in the rodent periodontal ligament." Histochemical Journal 25, no. 7 (July 1993): 523–30. http://dx.doi.org/10.1007/bf00159289.

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19

Sioustis, Ioana-Andreea, Mihai Axinte, Marius Prelipceanu, Alexandra Martu, Diana-Cristala Kappenberg-Nitescu, Silvia Teslaru, Ionut Luchian, Sorina Mihaela Solomon, Nicanor Cimpoesu, and Silvia Martu. "Finite Element Analysis of Mandibular Anterior Teeth with Healthy, but Reduced Periodontium." Applied Sciences 11, no. 9 (April 23, 2021): 3824. http://dx.doi.org/10.3390/app11093824.

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Finite element analysis studies have been of interest in the field of orthodontics and this is due to the ability to study the stress in the bone, periodontal ligament (PDL), teeth and the displacement in the bone by using this method. Our study aimed to present a method that determines the effect of applying orthodontic forces in bodily direction on a healthy and reduced periodontium and to demonstrate the utility of finite element analysis. Using the cone-beam computed tomography (CBCT) of a patient with a healthy and reduced periodontium, we modeled the geometric construction of the contour of the elements necessary for the study. Afterwards, we applied a force of 1 N and a force of 0.8 N in order to achieve bodily movement and to analyze the stress in the bone, in the periodontal ligament and the absolute displacement. The analysis of the applied forces showed that a minimal ligament thickness is correlated with the highest value of the maximum stress in the PDL and a decreased displacement. This confirms the results obtained in previous clinical practice, confirming the validity of the simulation. During orthodontic tooth movement, the morphology of the teeth and of the periodontium should be taken into account. The effect of orthodontic forces on a particular anatomy could be studied using FEA, a method that provides real data. This is necessary for proper treatment planning and its particularization depends on the patient’s particular situation.
20

Lekic, Predrag, Jaro Sodek, and Christopher A. G. McCulloch. "Osteopontin and bone sialoprotein expression in regenerating rat periodontal ligament and alveolar bone." Anatomical Record 244, no. 1 (January 1996): 50–58. http://dx.doi.org/10.1002/(sici)1097-0185(199601)244:1<50::aid-ar5>3.0.co;2-j.

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21

Lekic, P., I. Rubbino, F. Krasnoshtein, S. Cheifetz, C. A. G. McCulloch, and H. Tenenbaum. "Bisphosphonate modulates proliferation and differentiation of rat periodontal ligament cells during wound healing." Anatomical Record 247, no. 3 (March 1997): 329–40. http://dx.doi.org/10.1002/(sici)1097-0185(199703)247:3<329::aid-ar4>3.0.co;2-p.

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22

Zhang, X., D. Schuppan, J. Becker, P. Reichart, and H. R. Gelderblom. "Distribution of undulin, tenascin, and fibronectin in the human periodontal ligament and cementum: comparative immunoelectron microscopy with ultra-thin cryosections." Journal of Histochemistry & Cytochemistry 41, no. 2 (February 1993): 245–51. http://dx.doi.org/10.1177/41.2.7678270.

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We studied the ultrastructural localization of three distantly related glycoproteins of the extracellular matrix, undulin, tenascin and fibronectin, in decalcified sections of human periodontal ligament (PL) and cementum. Undulin was associated with tightly packed major collagen fibrils and not with microfibrils, indicating that this protein may be involved in the supramolecular and functional organization of collagen fibrils into flexible bundles. Tenascin was found on globular masses between less densely packed collagen fibrils, thus displaying a pattern quite distinct from that of undulin. Fibronectin was noted in bulky material between the cross-striated fibrils, often surrounding individual fibrils like garlands, and in the microfibrillar meshwork extending from cross-striated fibrils. The three glycoproteins displayed a distinct and unique pattern of distribution in PL that can be correlated with their molecular structure and potential functions.
23

McCulloch, C. A. G., E. Nemeth, B. Lowenberg, and A. H. Melcher. "Paravascular cells in endosteal spaces of alveolar bone contribute to periodontal ligament cell populations." Anatomical Record 219, no. 3 (November 1987): 233–42. http://dx.doi.org/10.1002/ar.1092190304.

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24

Michaeli, Yael, Shulamit Steigman, Amir Barad, and Miron Weinreb. "Three-dimensional presentation of cell migration in the periodontal ligament of the rat incisor." Anatomical Record 221, no. 2 (June 1988): 584–90. http://dx.doi.org/10.1002/ar.1092210204.

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25

Johnson, Roger B. "Comparative35S-sulfate and3H-proline metabolism within the interdental septal bone and adjacent periodontal ligament." Anatomical Record Part A: Discoveries in Molecular, Cellular, and Evolutionary Biology 288A, no. 7 (2006): 817–26. http://dx.doi.org/10.1002/ar.a.20343.

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26

Lekic, P., and C. A. G. McCulloch. "Periodontal ligament cell populations: The central role of fibroblasts in creating a unique tissue." Anatomical Record 245, no. 2 (June 1996): 327–41. http://dx.doi.org/10.1002/(sici)1097-0185(199606)245:2<327::aid-ar15>3.0.co;2-r.

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27

Menéndez-Diaz, I., J. D. Muriel, O. García-Suárez, A. Obaya, S. Cal, J. Cobo, J. A. Vega, and T. Cobo. "Periostin, dentin matrix protein 1 and P2rx7 ion channel in human teeth and periodontal ligament." Annals of Anatomy - Anatomischer Anzeiger 216 (March 2018): 103–11. http://dx.doi.org/10.1016/j.aanat.2017.12.004.

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28

Kato, J., S. Wakisaka, and K. Kurisu. "Immunohistochemical Changes in the Distribution of Nerve Fibers in the Periodontal Ligament during an Experimental Tooth Movement of the Rat Molar." Cells Tissues Organs 157, no. 1 (1996): 53–62. http://dx.doi.org/10.1159/000147866.

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29

Takagi, Minoru, Toshitada Kazama, Kazuyuki Shimada, Yasunobu Hosokawa, and Hideki Hishikawa. "Differential distribution and ultrastructural staining of oxytalan and elastic fibers in the periodontal ligament ofAlligator mississippiensis." Anatomical Record 225, no. 4 (December 1989): 279–87. http://dx.doi.org/10.1002/ar.1092250404.

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30

Lin, Wen-Lang, Christopher A. G. McCulloch, and Moon-Il Cho. "Differentiation of periodontal ligament fibroblasts into osteoblasts during socket healing after tooth extraction in the rat." Anatomical Record 240, no. 4 (December 1994): 492–506. http://dx.doi.org/10.1002/ar.1092400407.

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31

Honma, Shiho, Kunitaka Taki, Shi Lei, Hitoshi Niwa, and Satoshi Wakisaka. "Immunohistochemical Localization of SNARE Proteins in Dental Pulp and Periodontal Ligament of the Rat Incisor." Anatomical Record: Advances in Integrative Anatomy and Evolutionary Biology 293, no. 6 (February 23, 2010): 1070–80. http://dx.doi.org/10.1002/ar.21106.

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32

Kuroiwa, M., T. Tachikawa, N. Izumiyama, K. Takubo, S. Yoshiki, and S. Higashi. "Ultrastructure of the Rat Periodontal Ligament as Observed with Quick-Freeze, Deep-Etch and Replica Methods: Arrangement of Collagen and Related Structures." Cells Tissues Organs 157, no. 4 (1996): 291–302. http://dx.doi.org/10.1159/000147891.

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33

Maeda, Takeyasu, Koichi Kannari, Osamu Sato, Shigeo Kobayashi, Toshihiko Iwanaga, and Tsuneo Fujita. "Cholinesterase activity in terminal Schwann cells associated with Ruffini endings in the periodontal ligament of rat incisors." Anatomical Record 228, no. 3 (November 1990): 339–44. http://dx.doi.org/10.1002/ar.1092280313.

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34

Cheng, Mosha, and Qing Zhou. "Targeting EZH2 Ameliorates the LPS-Inhibited PDLSC Osteogenesis via Wnt/β-Catenin Pathway." Cells Tissues Organs 209, no. 4-6 (2020): 227–35. http://dx.doi.org/10.1159/000511702.

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As a histone methyltransferase, enhancer of zeste homolog 2 (EZH2), suppresses osteoblast maturation and is involved in inflammation. However, the role of EZH2 in human periodontal ligament stem cells (PDLSCs) under inflammation still needs to be further investigated. This study aimed to identify the underlying mechanisms and explore the function of EZH2 in PDLSC osteogenesis under inflammation. PDLSCs were treated with sh-EZH2, DZNep or DKK1 under inflammation. The alkaline phosphatase (ALP) activity, alizarin red staining, and osteogenesis-related protein levels were analyzed. Lipopolysaccharide (LPS)-induced inflammation restrained osteogenic differentiation. Under inflammation, the upregulation of EZH2 suppressed the expression of osteogenic markers, including osteocalcin, runt-related transcription factor 2, and bone morphogenetic protein-2, the activity of ALP, and the accumulation of mineralization through the Wnt/β-catenin pathway. EZH2 knockdown inhibited the levels of proinflammatory cytokines such as interleukin-6 and tumor necrosis factor-α. These results suggested that LPS-induced overexpression of EZH2 suppressed PDLSC osteogenesis under inflammatory conditions through the Wnt/β-catenin pathway. These findings give new insights into the physiological differentiation and pathological inflammation of PDLSC osteogenesis, and provide an underlying therapeutic target for periodontitis.
35

Kato, J., K. Tanne, H. Ichikawa, S. Matsuo, S. Wakisaka, M. Akai, K. Kurisu, and M. Sakuda. "Distribution of Calcitonin Gene-Related Peptide and Substance P-lmmunoreactive Nerve Fibers and Their Correlation in the Periodontal Ligament of the Mouse Incisor." Cells Tissues Organs 145, no. 2 (1992): 101–5. http://dx.doi.org/10.1159/000147349.

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36

Bosshardt, Dieter D., Marzio Bergomi, Giovanna Vaglio, and Anselm Wiskott. "Regional structural characteristics of bovine periodontal ligament samples and their suitability for biomechanical tests." Journal of Anatomy 212, no. 3 (March 2008): 319–29. http://dx.doi.org/10.1111/j.1469-7580.2008.00856.x.

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37

Staszyk, Carsten, and Hagen Gasse. "A simple fluorescence labeling method to visualize the three-dimensional arrangement of collagen fibers in the equine periodontal ligament." Annals of Anatomy - Anatomischer Anzeiger 186, no. 2 (April 2004): 149–52. http://dx.doi.org/10.1016/s0940-9602(04)80030-x.

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38

Masset, Alexandra, Carsten Staszyk, and Hagen Gasse. "The blood vessel system in the periodontal ligament of the equine cheek teeth – Part I: The spatial arrangement in layers." Annals of Anatomy - Anatomischer Anzeiger 188, no. 6 (November 2006): 529–33. http://dx.doi.org/10.1016/j.aanat.2006.06.010.

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39

Sato, Osamu, Takeyasu Maeda, Toshihiko Iwanaga, and Shigeo Kobayashi. "Innervation of the Incisors and Periodontal Ligament in Several Rodents: an Immunohistochemical Study of Neurofílament Protein and Glia-Specifîc S-100 Protein." Cells Tissues Organs 134, no. 2 (1989): 94–99. http://dx.doi.org/10.1159/000146671.

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40

Loescher, A. R., and G. R. Holland. "Distribution and morphological characteristics of axons in the periodontal ligament of cat canine teeth and the changes observed after reinnervation." Anatomical Record 230, no. 1 (May 1991): 57–72. http://dx.doi.org/10.1002/ar.1092300107.

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41

Cho, Moon-Il, and Philias R. Garant. "Radioautographic study of [3H]mannose utilization during cementoblast differentiation, formation of acellular cementuum, and development of periodontal ligament principal fibers." Anatomical Record 223, no. 2 (February 1989): 209–22. http://dx.doi.org/10.1002/ar.1092230214.

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42

Cho, Moon-Il, and Philias R. Garant. "Expression and role of epidermal growth factor receptors during differentiation of cementoblasts, osteoblasts, and periodontal ligament fibroblasts in the rat." Anatomical Record 245, no. 2 (June 1996): 342–60. http://dx.doi.org/10.1002/(sici)1097-0185(199606)245:2<342::aid-ar16>3.0.co;2-p.

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43

Nešković, Jelena, Milica Jovanović-Medojević, and Slavoljub Živković. "Clinical and radiological analysis of the causes for endodontic treatment failure." Stomatoloski glasnik Srbije 64, no. 2 (June 1, 2017): 63–73. http://dx.doi.org/10.1515/sdj-2017-0006.

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Summary Introduction Development of inflammatory lesions or their persistence after primary treatment is considered endodontic failure. The reason for failure can be complex anatomy of the canal system and numerous iatrogenic factors. The objective of this study was to analyze, clinically and radiographically, the causes of primary endodontic treatment failure and assess possibilities for retreatment of teeth with failed endodontic treatment. Method The study included 79 teeth (36 multirooted and 43 singlerooted tooth) indicated for repeated endodontic treatment. Based on the radiographic assessment of the status of periapical structures, teeth were divided into two groups. The first group included teeth without periapical lesions, i.e. the healthy periodontal tissues (PAI score of 1 and 2) in which retreatment was required for prosthodontic reason due to the poor quality of obturation (28 teeth), and the second group included teeth with visible signs of periapical tissue damage (PAI scores 3, 4 and 5) (51 teeth). In both groups, quality of obturation, coronal sealing and the presence or absence of clinical symptoms was analyzed. Results The most common radiographic finding of definitive obturation was short filling (65.8% of cases); “forgotten” canals (25.3%); non-homogeneous obturation with correct length (5.1%) and fractured instrument (3.8%). There was significant difference between healthy periodontal ligament and adequate restoration (P < 0.001). In 95% of patients with symptoms, changes in the periapical tissue were observed. Also, there was significant difference in the presence of symptoms after primary treatments, between the teeth with healthy apical periodontal tissue and teeth with periapical lesions (P = 0.019). Conclusion The outcome of the root canal treatment is significantly affected by the quality (density) of obturation and the presence and quality of coronal restoration. In patients with symptoms there were changes in the periapical tissue.
44

Nemeth, Endre, Christopher A. G. McCulloch, and Antony H. MeLcher. "Coordinated regulation of endothelial and fibroblast cell proliferation and matrix synthesis in periodontal ligament adjacent to appositional and resorptive bone surfaces." Anatomical Record 223, no. 4 (April 1989): 368–75. http://dx.doi.org/10.1002/ar.1092230404.

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45

Jheon, Andrew, Jun Chen, William Teo, Bernhard Ganss, Jaro Sodek, and Sela Cheifetz. "Temporal and Spatial Expression of a Novel Zinc Finger Transcription Factor, AJ18, in Developing Murine Skeletal Tissues." Journal of Histochemistry & Cytochemistry 50, no. 7 (July 2002): 973–82. http://dx.doi.org/10.1177/002215540205000711.

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Abstract:
Bone morphogenetic proteins (BMPs) are characterized by their ability to induce osteoblastic differentiation. However, the mechanism of osteo-induction by BMPs has yet to be determined. Using differential display we previously identified AJ18, a zinc finger transcription factor, as an immediate-early response gene to BMP-7. AJ18 was shown to bind to the osteoblast-specific element2 (OSE2) and to modulate transactivation by Runx2, a master gene in osteoblastic differentiation. Here we describe the temporal and spatial expression of AJ18 in developing mouse tissues. AJ18 mRNA expression was observed in most tissues, except liver, and was generally highest early in embryonic development, decreasing markedly after parturition. Consistent with immunohistochemical analysis, AJ18 mRNA expression was highest in the brain, kidney, and bone of 17 dpc (days post coitum) embryos. In endochondral bones of embryonic and 4-week-old mice, immunostaining for AJ18 was strong in the nuclei of proliferating and pre-hypertrophic chondrocytes, and osteoblasts, whereas there was low or no staining in hypertrophic chondrocytes. In teeth of embryonic and 4-week-old mice, nuclear staining was observed in precursor and mature ameloblasts, odontoblasts, and cementoblasts, respectively. In addition, in 4-week-old mice staining of AJ18 was observed within alveolar bone cells and periodontal ligament cells. In general, the spatial expression of AJ18 in skeletal and non-skeletal tissues of mouse embryos showed striking similarity to the expression of BMP-7 mRNA. Therefore, the expression of AJ18 is consistent with its perceived role as a transcriptional factor that regulates developmental processes downstream of BMP-7.
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Jäger, A., N. Heim, F. J. Kramer, M. Setiawan, M. Peitz, and A. Konermann. "A novel serum-free medium for the isolation, expansion and maintenance of stemness and tissue-specific markers of primary human periodontal ligament cells." Annals of Anatomy - Anatomischer Anzeiger 231 (September 2020): 151517. http://dx.doi.org/10.1016/j.aanat.2020.151517.

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Maeda, Takeyasu, Osamu Sato, Shigeo Kobayashi, Toshihiko Iwanaga, and Tsuneo Fujita. "The ultrastructure of ruffini endings in the periodontal ligament of rat incisors with special reference to the terminal schwann cells (K-cells)." Anatomical Record 223, no. 1 (January 1989): 95–103. http://dx.doi.org/10.1002/ar.1092230114.

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Tadokoro, Osamu, Vaska Radunovic, and Katsuhiro Inoue. "Epithelial Cell Rests of Malassez and OX6-Immunopositive Cells in the Periodontal Ligament of Rat Molars: A Light and Transmission Electron Microscope Study." Anatomical Record: Advances in Integrative Anatomy and Evolutionary Biology 291, no. 3 (2008): 242–53. http://dx.doi.org/10.1002/ar.20648.

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Masset, Alexandra, Carsten Staszyk, and Hagen Gasse. "The blood vessel system in the periodontal ligament of the equine cheek teeth – Part II: The micro-architecture and its functional implications in a constantly remodelling system." Annals of Anatomy - Anatomischer Anzeiger 188, no. 6 (November 2006): 535–39. http://dx.doi.org/10.1016/j.aanat.2006.06.007.

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50

Cho, Moon-Il, Wen-Lang Lin, and Philias R. Garant. "Occurrence of epidormal growth factor-binding sites during differentiation of cementoblasts and periodontal ligament fibroblasts of the young rat: A light and electron microscopic radioautographic study." Anatomical Record 231, no. 1 (September 1991): 14–24. http://dx.doi.org/10.1002/ar.1092310104.

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