Effect of repeated torque/mechanical loading cycles on two different abutment types in implants with internal tapered connections: an in vitro study

Internal tapered connections were developed to improve biomechanical properties and to reduce mechanical problems found in other implant connection systems. The purpose of this study was to evaluate the effects of mechanical loading and repeated insertion/removal cycles on the torque loss of abutments with internal tapered connections. Sixty-eight conical implants and 68 abutments of two types were used. They were divided into four groups: groups 1 and 3 received solid abutments, and groups 2 and 4 received two-piece abutments. In groups 1 and 2, abutments were simply installed and uninstalled; torque-in and torque-out values were measured. In groups 3 and 4, abutments were installed, mechanically loaded and uninstalled; torque-in and torque-out values were measured. Under mechanical loading, two-piece abutments were frictionally locked into the implant; thus, data of group 4 were catalogued under two subgroups (4a: torque-out value necessary to loosen the fixation screw; 4b: torque-out value necessary to remove the abutment from the implant). Ten insertion/removal cycles were performed for every implant/abutment assembly. Data were analyzed with a mixed linear model (P <= 0.05). Torque loss was higher in groups 4a and 2 (over 30% loss), followed by group 1 (10.5% loss), group 3 (5.4% loss) and group 4b (39% torque gain). All the results were significantly different. As the number of insertion/removal cycles increased, removal torques tended to be lower. It was concluded that mechanical loading increased removal torque of loaded abutments in comparison with unloaded abutments, and removal torque values tended to decrease as the number of insertion/removal cycles increased. To cite this article:Ricciardi Coppede A, de Mattos MdaGC, Rodrigues RCS, Ribeiro RF. Effect of repeated torque/mechanical loading cycles on two different abutment types in implants with internal tapered connections: an in vitro study.Clin. Oral Impl. Res. 20, 2009; 624-632.doi: 10.1111/j.1600-0501.2008.01690.x.

Regulation of Multidrug Resistance-Associated Protein 2 by Calcium Signaling in Mouse Liver

Mu hiding resistance associated protein 2 (Mrp2) is a canalicular transporter responsible for organic anion secretion into bile. Mrp2 activity is regulated by insertion into the plasma membrane; however, the factors that control this are not understood. Calcium (Ca(2+)) signaling regulates exocytosis of vesicles in most cell types, and the type II inositol 1,4,5-triphosphate receptor (InsP(3)R2) regulates Ca(2+) release in the canalicular region of hepatocytes. However, the role of InsP(3)R2 and of Ca(2+) signals in canalicular insertion and function of Mrp2 is not known. The aim of this study was to determine the role of InsP(3)R2-mediated Ca(2+) signals in targeting Mrp2 to the canalicular membrane. Livers, isolated hepatocytes, and hepatocytes in collagen sandwich culture from wild-type (WT) and InsP(3)R2 knockout (KO) mice were used for western blots, confocal immunofluorescence, and time-lapse imaging of Ca(2+) signals and of secretion of a fluorescent organic anion. Plasma membrane insertion of green fluorescent protein (GFP)-Mrp2 expressed in HepG2 cells was monitored by total internal reflection microscopy. InsP(3)R2 was concentrated in the canalicular region of WT mice but absent in InsP(3)R2 KO livers, whereas expression and localization of InsP(3)R1 was preserved, and InsP(3)R3 was absent from both WT and KO livers. Ca(2+) signals induced by either adenosine triphosphate (ATP) or vasopressin were impaired in hepatocytes lacking InsP(3)R2. Canalicular secretion of the organic anion 5-chloromethylfluorescein diacetate (CMFDA) was reduced in KO hepatocytes, as well as in WT hepatocytes treated with 1,2-bis(o-aminophenoxy)ethane-N,N,N`,N`-tetra-acetic acid (BAPTA). Moreover, the choleretic effect of tauroursodeoxycholic acid (TUDCA) was impaired in InsP(3)R2 KO mice. Finally, ATP increased GFP-Mrp2 fluorescence in the plasma membrane of HepG2 cells, and this also was reduced by BAPTA. Conclusion: InsP(3)R2-mediated Ca(2+) signals enhance organic anion secretion into bile by targeting Mrp2 to the canalicular membrane. (HEPATOLOGY 2010;52:327-337)

Exercise Training Reduces Insulin Resistance and Upregulates the mTOR/p70S6k Pathway in Cardiac Muscle of Diet-Induced Obesity Rats

Obesity and insulin resistance are rapidly expanding public health problems. These disturbances are related to many diseases, including heart pathology. Acting through the Akt/mTOR pathway, insulin has numerous and important physiological functions, such as the induction of growth and survival of many cell types and cardiac hypertrophy. However, obesity and insulin resistance can alter mTOR/p70S6k. Exercise training is known to induce this pathway, but never in the heart of diet-induced obesity subjects. To evaluate the effect of exercise training on mTOR/p70S6k in the heart of obese Wistar rats, we analyzed the effects of 12 weeks of swimming on obese rats, induced by a high-fat diet. Exercise training reduced epididymal fat, fasting serum insulin and plasma glucose disappearance. Western blot analyses showed that exercise training increased the ability of insulin to phosphorylate intracellular molecules such as Akt (2.3-fold) and Foxo1 (1.7-fold). Moreover, reduced activities and expressions of proteins, induced by the high-fat diet in rats, such as phospho-JNK (1.9-fold), NF-kB (1.6-fold) and PTP-1B (1.5-fold), were observed. Finally, exercise training increased the activities of the transduction pathways of insulin-dependent protein synthesis, as shown by increases in Raptor phosphorylation (1.7-fold), p70S6k phosphorylation (1.9-fold), and 4E-BP1 phosphorylation (1.4-fold) and a reduction in atrogin-1 expression (2.1-fold). Results demonstrate a pivotal regulatory role of exercise training on the Akt/ mTOR pathway, in turn, promoting protein synthesis and antagonizing protein degradation. J. Cell. Physiol. 226: 666-674, 2011. (C) 2010 Wiley-Liss, Inc.