Publications by authors named "Danwei Xiang"

Background: Extracellular matrix (ECM) protein malfunction or defect may lead to temporomandibular joint osteoarthritis (TMJ OA). Dentin sialophophoprotein (DSPP) is a mandibular condylar cartilage ECM protein, and its deletion impacted cell proliferation and other extracellular matrix alterations of postnatal condylar cartilage. However, it remains unclear if long-term loss of function of DSPP leads to TMJ OA.

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The calcifying epithelial odontogenic tumor (CEOT) is a rare benign odontogenic tumor, which usually presents with distension of affected tissues. Radiologically, the lesions are often associated with an unerupted tooth and may have spot calcification shadows. The authors report a case of a CEOT in a 48-year-old male involving the right mandibular jaw bone and mentum soft tissues.

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Objectives: We aimed to observe the posttranslational role of dentin sialophosphoprotein (DSPP) on postnatal development of mandibular condyle in mice.

Methods: To explore the function of full-length DSPP, four groups of mice were employed: (1) wild type (WT) mice; (2)Dspp knockout (Dspp KO) mice; (3) mice expressing the normal DSPP transgene in the Dspp KO background (Dspp KO/normal Tg); (4) mice expressing the uncleavable full-length DSPP in the Dspp KO background (Dspp KO/D452A Tg). Firstly, Plain X-ray Radiography and Micro-computed Tomography were used to observe the condylar morphology changes of Dspp KO/D452A Tg mice in comparison with the other three groups.

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Rationale: Cutaneous perforators of peroneal vessels are divided into proximal and distal perforators on the basis of perforator distributions and musculocutaneous or septocutaneous properties. The traditional fibular osteocutaneous free flap is raised over the distal two-thirds of the fibula with a skin paddle based on distal perforators, which is affixed to the posterior crural septum. However, the skin pedicle may not be available due to anatomic variations or intraoperative injuries.

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Dentin dysplasia (DD) and dentinogenesis imperfecta (DGI) patients have abnormal structure, morphology, and function of dentin. DD-II, DGI-II, and DGI-III are caused by heterozygous mutations in the dentin sialophosphoprotein () gene in humans. Evidences have shown that loss of function of DSPP in knockout mice leads to phenotypes similar to DGI-III, and that the abnormal dentinogenesis is associated with decreased levels of DSPP, indicating that DSPP haploinsufficiency may play a role in dentinogenesis.

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Dentin sialophosphoprotein (DSPP), which expresses and synthesizes in odontoblasts of dental pulp, is a critical protein for normal teeth mineralization. Originally, DSPP was identified as a dentin-specific protein. In 2010, DSPP was also found in femoral head cartilage, and it is still unclear what roles DSPP play in femoral head cartilage formation, growth, and maintenance.

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