Biomaterial Properties of Titanium in Dentistry

Background Among various dental materials and their successful restorative uses, titanium provides an excellent example of integrating science and technology involving multiple disciplines of dentistry including biomaterials, prosthodontics and surgical sciences. Titanium and its alloys have emerged as a material of choice for dental implants fulfilling all requirements biologically, chemically and mechanically. Several excellent reviews have discussed the properties of titanium and its surface characteristics that render it biocompatible. However, in most patients, titanium implants are used alongside several other metals. Presence of different metals in the same oral environment can alter the properties of titanium. Other influencing factors include intra-oral pH, salivary content, and effect of fluorides. Highlight This review discusses the effect of the above-mentioned conditions on the properties of titanium and its alloys. An extensive literature search encompassing the properties of titanium in an altered oral environment and its interaction with other restorative materials is presented. Specific conditions that could cause titanium to corrode, specifically due to interaction with other dental materials used in oral rehabilitation, as well as methods that can be employed for passivation of titanium are discussed. Conclusion This review presents an overview of the properties of titanium that are vital for its use in implant dentistry. From a restorative perspective, interaction between implant restoration metals, intra-oral fluorides and pH may cause titanium to corrode. Therefore, in order to avoid the resulting deleterious effects, an understanding of these interactions is important for long-term prognosis of implant restorations

Genome-wide reconstitution of chromatin transactions reveals that RSC preferentially disrupts H2AZ-containing nucleosomes

Chromatin transactions are typically studied in vivo, or in vitro using artificial chromatin lacking the epigenetic complexity of the natural material. Attempting to bridge the gap between these approaches, we established a system for isolating the yeast genome as a library of mononucleosomes harboring the natural epigenetic signature, suitable for biochemical manipulation. Combined with deep sequencing, this library was used to investigate the stability of individual nucleosomes and, as proof of principle, the nucleosome preference of the chromatin remodeling complex, RSC. This approach uncovered a distinct preference of RSC for nucleosomes derived from regions with a high density of histone variant H2AZ, and this preference is indeed markedly diminished using nucleosomes from cells lacking H2AZ. The preference for H2AZ remodeling/nucleosome ejection can also be reconstituted with recombinant nucleosome arrays. Together, our data indicate that, despite being separated from their genomic context, individual nucleosomes can retain their original identity as promoter- or transcription start site (TSS)-nucleosomes. Besides shedding new light on substrate preference of the chromatin remodeler RSC, the simple experimental system outlined here should be generally applicable to the study of chromatin transactions

Functional Interactions between KCNE1 C-Terminus and the KCNQ1 Channel

The KCNE1 gene product (minK protein) associates with the cardiac KvLQT1 potassium channel (encoded by KCNQ1) to create the cardiac slowly activating delayed rectifier, IKs. Mutations throughout both genes are linked to the hereditary cardiac arrhythmias in the Long QT Syndrome (LQTS). KCNE1 exerts its specific regulation of KCNQ1 activation via interactions between membrane-spanning segments of the two proteins. Less detailed attention has been focused on the role of the KCNE1 C-terminus in regulating channel behavior. We analyzed the effects of an LQT5 point mutation (D76N) and the truncation of the entire C-terminus (Δ70) on channel regulation, assembly and interaction. Both mutations significantly shifted voltage dependence of activation in the depolarizing direction and decreased IKs current density. They also accelerated rates of channel deactivation but notably, did not affect activation kinetics. Truncation of the C-terminus reduced the apparent affinity of KCNE1 for KCNQ1, resulting in impaired channel formation and presentation of KCNQ1/KCNE1 complexes to the surface. Complete saturation of KCNQ1 channels with KCNE1-Δ70 could be achieved by relative over-expression of the KCNE subunit. Rate-dependent facilitation of K+ conductance, a key property of IKs that enables action potential shortening at higher heart rates, was defective for both KCNE1 C-terminal mutations, and may contribute to the clinical phenotype of arrhythmias triggered by heart rate elevations during exercise in LQTS mutations. These results support several roles for KCNE1 C-terminus interaction with KCNQ1: regulation of channel assembly, open-state destabilization, and kinetics of channel deactivation

The Solar-Driven Coal/Fe3O4 Redox System

The solar-driven endothermic reaction of coal and magnetite was studied for mixing solar and fossil energies. The overall reaction can be represented by CHx + Fe3O4 = CO + 3FeO + 1/2xH2 where x depends on the coal(x= 0.2 in our study). Laboratory experimental studies with an equimolar mixture of anthracite coal and Fe3O4 powder using an infrared furnace showed rapid gas evolution above about 1200°C and 1bar, producing FeO(s) and a gas mixture containing a CO/CO2 molar ratio of 4.5. Solar-driven experiments were conducted using a high-flux solar furnace. Samples were directly exposed for short time intervals to a solar flux irradiation of 300 W/cm2. The carbon content decreased rapidly after only 1 second exposure, suggesting efficient heat transfer and chemical conversion by direct absorption of concentrated solar energy at the reaction site. The proposed solar thermochemical process offers the possibility of performing simultaneously the gasification of coal and reduction of iron oxide, and for producing a fuel with an upgraded calorific value