ABSTRACT
AIM: Various chemical solutions have been recommended for denture disinfection; however, the immersion effect on the properties of denture base resin may also have effect on strength of the resin material. The purpose of this in vitro study was to compare and evaluate the flexural strength of heat-cure acrylic denture base resin by combination method of denture cleansing and plant extract immersion. MATERIALS AND METHODS: In this study, ninety specimens of heat-cure acrylic denture base resin material were fabricated with dimensions of 65 mm × 10 mm × 3.3 mm. The specimens were divided into three groups, namely, Group I-III of thirty specimens each and were immersed in distilled water, denture cleanser, and thyme essential oil, respectively. The flexural strength of specimen was evaluated. RESULTS: Natural plant extract showed better flexural strength than immersed in denture cleanser and control group but statistically was not significant. CONCLUSION: The study concluded that plant extract, namely, thyme essential oil, showed better flexural strength than combination method and can be used as denture cleanser.
ABSTRACT
Scaffold proteins organize pre- and postsynaptic compartments and align pre- and postsynaptic events. Cask is a multi-domain scaffold protein essential for brain synaptic functions. Caskin1 is a recently discovered, brain-specific Cask-interacting multi-domain protein of unknown function. In the present study, we determined the localization of these scaffold proteins in the bovine retina. The retina contains tonically active ribbon synapses and conventional synapses. We found Cask highly enriched in virtually all retinal synapses. Cask was localized in close vicinity to the active zone protein RIM1/2 in ribbon and conventional synapses. Caskin1 is also enriched in retinal synapses but is present only in a subset of Cask-positive synapses. These findings suggest that Cask plays an important role in all retinal synapses. In contrast, Caskin1 appears to execute more specialized functions in distinct sets of retinal synapses, possibly for neuronal pathway formation and stabilization of distinct synaptic contacts.
