These results suggest that during the Er,Cr:YSGG laser irradiation, water spray directed at the ablation sites increases the ablation depths and water plays an important role as an initiator of the ablation of dental hard tissues.

The results of this study suggest that Er:YAG laser irradition with and without water mist appears to be more effective for caries prevention.

The results of this study suggest that addition of a fine water mist directed at the ablation sites does not greatly decrease the ablation, and does not cause any carbonization and melting in the surrounding dental hard tissues.

Articles you may be interested inIn situ spectroscopic ellipsometry study of the hydrogenation process of switchable mirrors based on magnesium-nickel alloy thin films J. Appl. Phys. 107, 043517 (2010); 10.1063/1.3294655Mg segregation in Mg-rich Mg-Ni switchable mirror studied by Rutherford backscattering, elastic recoil detection analysis, and nuclear reaction analysis Microstructure of Mg-Ni thin film prepared by direct current magnetron sputtering and its properties as a negative electrode

The MMPs (matrix metalloproteinases) MMP-9 and -2 each possess a unique CBD (collagen-binding domain) containing three fibronectin type II-like modules. The present experiments investigated whether the contributions to ligand interactions and enzymatic activities by the CBD of MMP-9 (CBD-9) corresponded to those of CBD in MMP-2 (CBD-2). The interactions of recombinant CBD-9 with a series of collagen types and extracellular matrix molecules were characterized by protein-protein binding assays. CBD-9 bound native and denatured type I, II, III, IV and V collagen, as well as Matrigel and laminin, with apparent K(d) values of (0.1-6.8)x10(-7) M, which were similar to the K(d) values for CBD-2 [(0.2-3.7)x10(-7) M]. However, CBD-9 bound neither native nor denatured type VI collagen. We also generated two modified MMPs, MMP-9(E402A) and MMP-2(E404A), by site-specific mutations in the active sites to obtain enzymes with intact ligand binding, but abrogated catalytic properties. In subsequent competitive binding assays, CBD-9 and MMP-9(E402A) inhibited the interactions of MMP-2(E404A) and, conversely, CBD-2 and MMP-2(E404A) competed with MMP-9(E402A) binding to native and denatured type I collagens, pointing to shared binding sites. Importantly, the capacity of CBD-9 to disrupt the MMP-9 and MMP-2 binding of collagen translated to inhibition of the gelatinolytic activity of the enzymes. Collectively, these results emphasize the essential contribution of CBD-9 to MMP-9 substrate binding and gelatinolysis, and demonstrate that the CBDs of MMP-9 and MMP-2 bind the same or closely positioned sites on type I collagen.