Association between maximum mouth opening and area of bony fusion in simulated temporomandibular joint bony ankylosis.

The aim of this study was to investigate the quantitative association between active/passive maximum mouth opening (AMMO/PMMO) and the severity of simulated temporomandibular joint (TMJ) bony ankylosis. Twenty-eight male sheep were divided randomly and equally into surgical and control groups. Surgical group animals underwent bilateral TMJ osteotomy during which left lateral pterygoid muscle function was blocked. Control animals did not undergo surgery. Body weight, AMMO/PMMO, and TMJ morphological features were evaluated preoperatively and at 12 and 24 weeks post-surgery. In the surgical group, only the right TMJ complexes with maintained lateral pterygoid muscle function developed TMJ bony ankylosis. The AMMO/PMMO and end-feel distance in the surgical group were significantly lower than those in the control group (P < 0.001, both) at 12 and 24 weeks post-surgery. Moreover, AMMO (r = -0.940 and -0.952, P < 0.001, both) and PMMO (r = -0.944 and -0.953, P < 0.001, both) were negatively correlated with the area (mm2) of bony fusion post-surgery. These findings may be useful for the clinical treatment of early mandibular condyle fracture, with the use of occlusal pads/open-mouth plates to relax the lateral pterygoid muscle and block its function. When bony ankylosis developed in the TMJ, the greater the area of bony fusion, the more limited were AMMO/PMMO.

Localization of MMP-2, MMP-9, TIMP-1, and TIMP-2 in human coronal dentine.

OBJECTIVES: Matrix metalloproteinases (MMPs) and their inhibitors (TIMPs) play important roles in dentine formation, caries progression and hybrid layer degradation. This study tested the hypothesis that the distribution and concentrations of MMP-2, MMP-9, TIMP-1 and TIMP-2 are different at different depths of human coronal dentine, including odontoblasts. METHODS: Protein localization was performed using immunohistochemistry. Co-localization of the MMPs and their inhibitors was conducted using immunofluorescence double labelling. Protein concentrations were measured by ELISA and gelatinolytic potential was assessed with gelatine zymography. RESULTS: MMP-2 was the main gelatinase in dentine and was concentrated in the odontoblasts, deep dentine and the dentinoenamel junction. TIMP-2 was co-localized with MMP-2 mainly in the odontoblasts but its concentration was low. Both MMP-9 and TIMP-1 showed a decreasing distribution from the deep to the superficial dentine layers; however, the concentration of TIMP-1 was much higher than that of MMP-9. The gelatinolytic potential of dentine protein extracts decreased gradually from deep to superficial dentine. CONCLUSIONS: The concentrations and distribution patterns of MMP-2, MMP-9, TIMP-1 and TIMP-2, and the gelatinolytic potential of dentine matrix are variable along different dentine depths. Thus, differential collagen degradation potentials may be expected depending upon the depth in which dentine is exposed.