Influence of etching with erbium, chromium:yttrium-scandium-gallium-garnet laser on microleakage of class V restoration

The aim of this in vitro study was to evaluate some parameters of dental etching when irradiated with an erbium, chromium:yttrium-scandium-gallium-garnet (Er,Cr:YSGG) laser. One-hundred sound human third molars were selected and randomly distributed into ten groups (n = 10). The class V cavities of group 1 (control) were prepared with a bur and etched with 37% phosphoric acid, while groups G2 to G10, were prepared with laser (5 W, 88.46 J/cm(2), 90/70% air/water) and etched with the following powers: G3 and G4, 0.25 W; G5 and G6, 0.5 W; G7 and G8, 0.75 W; G9 and G10, 1 W. Group G2 received no laser etching. Prior to restoration, G2, G4, G6, G8 and G10 received acid etching. After restoration, all samples were submitted to a microleakage test. According to statistical analysis (Kruskal-Wallis and Dunn`s tests), G10 presented the lowest microleakage values (P < 0.05). The other groups showed no differences between them. Etching with Er,Cr:YSGG laser (1 W) followed by phosphoric acid was effective in reducing the microleakage of class V restorations.

Influence of the Additional Er:YAG Laser Conditioning Step on the Microleakage of Class V Restorations

The purpose of this study was to evaluate the influence of an additional Er:YAG laser conditioning step after laser cavity preparations, on the microleakage of class V composite restorations. Forty-eight bovine incisors were randomly divided into four groups: G1(control) cavities prepared with bur, G2- cavities prepared with laser (400 mJ/2 Hz), G3-cavities prepared and subsequently conditioned with Er:YAG laser (60 mJ/2 Hz); G4-idem for G3, but the laser conditioning was carried out without water-spray. All the cavities were restored using Clearfill SE Bond (R) and Z-250 (R) composite resin. The samples were thermal cycled for 700 cycles and then immersed in 50% silver nitrate solution. The sectioned restorations were exposed to a photoflood lamp to reveal silver nitrate penetration. The Kruskal-Walis one-way analyses of variance test and post hoc Wilcoxon pair-wise comparison were used to compare microleakage degrees. At the gingival margin G2 showed a lower microleakage mean than the control bur-prepared cavities (p = 0.0003). At occlusal margins there were no statistically significant differences between the groups (p = 0.28). It may be concluded that Er:YAG laser class V cavity preparations do not need to be followed by an additional laser conditioning step to result in levels of microleakage similar to or lower than those obtained after bur preparations. (C) 2008 Wiley Periodicals, Inc. J Biomed Mater Res Part B: Appl Biomater 87B: 538-543, 2008

Presence of arsenic in different types of MTA and white and gray Portland cement

Objective. The presence of arsenic in various types of mineral trioxide aggregate (MTA) and Portland cements were evaluated to verify if they comply with the ISO-recommended limit for water-based cements of 2 mg arsenic/kg material. Study design. An amount of 5 mL of hydrochloric acid was added to 2 g each of MTA and Portland cement to be analyzed. After 15 minutes, the material was filtered and the volume of supernatant was diluted with reagent-grade water up to 40 mL. Atomic absorption spectrophotometry readings were performed in triplicate. Results. The following mean values were obtained: CPM (Egeo, Buenos Aires, Argentina) 11.06 mg/kg; CPM sealer (Egeo) 10.30 mg/kg; MTA- Obtura (Angelus, Londrina, PR, Brazil) 0.39 mg/kg; Experimental MTA: 10.30 mg/kg; White MTA- Angelus (Angelus) 1.03 mg/kg; Gray MTA- Angelus (Angelus) 5.91 mg/kg; ProRoot-MTA (Dentsply/Tulsa Dental Specialties, Tulsa, OK) 5.25 mg/kg; Gray Portland cement (Votorantim Cimentos, Cubatao, SP, Brazil): 34.27 mg/kg; and White Portland cement (Cimento Rio Branco, Rio de Janeiro, RJ, Brazil) 0.52 mg/kg. Conclusion. All tested materials presented arsenic in their composition. The form of arsenic was not analyzed nor the toxicity of the arsenic found. Only MTA- Obtura, White MTA- Angelus, and White Portland cement presented arsenic levels below the limit set in the ISO 9917-1 standard. (Oral Surg Oral Med Oral Pathol Oral Radiol Endod 2008; 106: 909-913)

On the intersection problem for 1-factorizations and near 1-factorizations of K-v

The number of 1-factors (near 1-factors) that mu 1-factorizations (near 1-factorizations) of the complete graph K-v, v even (v odd), can have in common, is studied. The problem is completely settled for mu = 2 and mu = 3.

Regulation and properties of KCNQ1 (K(v)LQT1) and impact of the cystic fibrosis transmembrane conductance regulator

The K+ channel KCNQ1 (K(V)LQT1) is a voltage-gated K+ channel, coexpressed with regulatory subunits such as KCNE1 (IsK, mink) or KCNE3, depending on the tissue examined. Here, we investigate regulation and properties of human and rat KCNQ1 and the impact of regulators such as KCNE1 and KCNE3. Because the cystic fibrosis transmembrane conductance regulator (CFTR) has also been suggested to regulate KCNQ1 channels we studied the effects of CFTR on KCNQ1 in Xenopus oocytes, Expression of both human and rat KCNQ1 induced time dependent K+ currents that were sensitive to Ba2+ and 293B. Coexpression with KCNE1 delayed voltage activation, while coexpression with KCNE3 accelerated current activation. KCNQ1 currents were activated by an increase in intracellular cAMP, independent of coexpression with KCNE1 or KCNE3. cAMP dependent activation was abolished in N-terminal truncated hKCNQ1 but was still detectable after deletion of a single PKA phosphorylation motif. In the presence but not in the absence of KCNE1 or KCNE3, K+ currents were activated by the Ca2+ ionophore ionomycin. Coexpression of CFTR with either human or rat KCNQ1 had no impact on regulation of KCNQ1 K+ currents by cAMP but slightly shifted the concentration response curve for 293B. Thus, KCNQ1 expressed in Xenopus oocytes is regulated by cAMP and Ca2+ but is not affected by CFTR.

Cloning and function of the rat colonic epithelial K+ channel K(V)LQT1

K(V)LQT1 (K(V)LQ1) is a voltage-gated K+ channel essential for repolarization of the heart action potential that is defective in cardiac arrhythmia. The channel is inhibited by the chromanol 293B, a compound that blocks cAMP-dependent electrolyte secretion in rat and human colon, therefore suggesting expression of a similar type of K+ channel in the colonic epithelium. We now report cloning and expression of K(V)LQT1 from rat colon. Overlapping clones identified by cDNA-library screening were combined to a full length cDNA that shares high sequence homology to K(V)LQT1 cloned from other species. RT-PCR analysis of rat colonic musoca demonstrated expression of K(V)LQT1 in crypt cells and surface epithelium. Expression of rK(V)LQT1 in Xenopus oocytes induced a typical delayed activated K+ current. that was further activated by increase of intracellular cAMP but not Ca2+ and that was blocked by the chromanol 293B. The same compound blocked a basolateral cAMP-activated K+ conductance in the colonic mucosal epithelium and inhibited whole cell K+ currents in patch-clamp experiments on isolated colonic crypts. We conclude that K(V)QT1 is forming an important component of the basolateral cAMP-activated K+ conductance in the colonic epithelium and plays a crucial role in diseases like secretory diarrhea and cystic fibrosis.

Expression and function of colonic epithelial K(v)LQT1 K+ channels

1. K(V)LQT1 (KCNQ1) is a voltage-gated K+ channel essential for repolarization of the heart action potential Defects in ion channels have been demonstrated in cardiac arrhythmia. This channel is inhibited potently by the chromanol 293B, The same compound has been shown to block cAMP-dependent electrolyte secretion in rat and human colon, Therefore, it was suggested that a K+ channel similar to K(V)LQT1 is expressed in the colonic epithelium. 2, In the present paper, expression of K(V)LQT1 and its function in colonic epithelial cells is described. Reverse transcription-polymerase chain reaction analysis of rat colonic mucosa demonstrated expression of K(V)LQT1 in both crypt cells and surface epithelium. When expressed in Xenopus oocytes, K(V)LQT1 induced a typical delayed activated K+ current. 3, As demonstrated, the channel activity could be further activated by increases in intracellular cAMP. These and other data support the concept that K(V)LQT1 is forming a component of the basolateral cAMP-activated Kf conductance in the colonic epithelium.