Clinical comparison of the effectiveness of novel sonic instruments and curettes for periodontal debridement after 2 months.

AIM: The aim of this study was to evaluate in vivo the effectiveness of scaling and root planing of new oscillating instruments (Periosonic) using a sonic handpiece compared to hand curettes with a split mouth design after 2 months. METHODS: 11 patients with adult periodontitis participated in this study. Plaque index (PII) (O'Leary), bleeding on probing (BOP), probing pocket depth (PPD), recession (REC) and clinical attachment level (CAL) were recorded at baseline and 2 months after treatment. After oral hygiene instruction, 2 randomly assigned quadrants per patient were scaled and root planed with curettes (control side) and the remaining 2 quadrants with the Periosonic instruments 1 and 2 (test side). The student t-test for paired data was used to test the significance of difference between test and control sides. RESULTS: There was no statistical difference (p>0.05) between the 2 sides for the improvement of the clinical parameters excepted for the group with initial PPD of 4-6 mm (test: 1.3+/-0.4 mm PPD reduction, control: 1.6+/-0.4 mm). For PPD > or =7 mm, the test side had better clinical improvement in attachment levels (2.2+/-0.9 mm), less recession (-0.4+/-0.5 mm) with lower PPD reduction (2.4+/-0.6 mm) than the control side (AL: 1.6+/-1.8 mm; REC: -1.3+/-0.7 mm, PPD reduction: 3.0+/-1.4 mm). CONCLUSION: This clinical study demonstrated that Periosonic(R) instruments are clinically at least as effective as curettes in PPD reduction when initial PPD is < or =6 mm and show better clinical attachment level improvement with less recession for initial PPD of > or =7 mm.

Tooth substance loss resulting from mechanical, sonic and ultrasonic root instrumentation assessed by liquid scintillation.

AIMS: This study investigated the loss of tooth substance (microg) by means of liquid scintillation in combination with profilometric and SEM analyses in order to evaluate the roughness and morphological changes of the root surface before and after instrumentation. METHOD: 40 polished and irradiated bovine root surfaces were scaled in vitro while covered with 50 ml distilled water using a sonic prototype (Periosonic 1/2), a magnetostrictive ultrasonic (Cavitron with Slimline inserts) scaler and a hand curette. Pressures were applied for the Periosonic, Cavitron and hand curette at 500, 500 and 30 g respectively, for 30-s intervals, up to 120 s. Loss of apatite (microg) was determined from the decays/min (32P) of the water samples using the radiochemical method of liquid scintillation. Replicas were made of the specimens for SEM and profilometric analyses. RESULTS: The least substance loss was noted significantly (p<0.01) at all time intervals after Slimline, followed by the fine sonic prototype Periosonic 2, then the Periosonic 1 and finally the hand curette. In contrast, profilometric and SEM analyses revealed the smoothest root surfaces after the hand curette, whereas Cavitron produced a less smooth surface. CONCLUSION: It can be concluded that this method can reveal very precisely small quantities of substance lost and, in combination with SEM analysis and microroughness measurements, be of considerable value in evaluating the aggressiveness and efficacy of periodontal instruments.

A comparative in vitro study of a magnetostrictive and a piezoelectric ultrasonic scaling instrument.

BACKGROUND: The effects of magnetostrictive ultrasonic instruments and piezoelectric ultrasonic instruments on tooth surfaces seem to differ with regards to root debridement. AIM: The purpose of this study was to compare a magnetostrictive ultrasonic scaling instrument with a piezoelectric ultrasonic scaling instrument and a hand curette regarding time taken, calculus removal, tooth surface roughness (Ra), and SEM examination before and after instrumentation. METHODS: 30 extracted human teeth with subgingival calculus were assigned to one of three treatment groups (n=10). The working force was standardised for both ultrasonic instruments at 200 g and for the curette at 500 g. RESULTS: The results revealed that the time needed for instrumentation was 126.1+/-38.2 s for the curette, significantly more than for the piezoelectric ultrasonic instrument (74.1+/-27.6 s; p<0.05) and 104.9+/-25.4 s for the magnetostrictive ultrasonic instrument. Remaining calculus was similar for all three groups. The end Ra values were significantly worse for the piezoelectric instrument (2.02+/-0.41; p<0.05) compared to 1.42+/-0.48 for the curette and 1.36+/-0.41 for the magnetostrictive instrument. The SEM examination revealed the smoothest surfaces but, subjectively, the most tooth substance loss after the curette, followed by the magnetostrictive instrument, with the least substance loss, and then the piezoelectric instrument, with medium substance loss. CONCLUSION: The piezoelectric ultrasonic scaler was more efficient than the magnetostrictive ultrasonic scaler in removing calculus but left the instrumented tooth surface rougher.

Late endosomal membranes rich in lysobisphosphatidic acid regulate cholesterol transport.

The fate of free cholesterol released after endocytosis of low-density lipoproteins remains obscure. Here we report that late endosomes have a pivotal role in intracellular cholesterol transport. We find that in the genetic disease Niemann-Pick type C (NPC), and in drug-treated cells that mimic NPC, cholesterol accumulates in late endosomes and sorting of the lysosomal enzyme receptor is impaired. Our results show that the characteristic network of lysobisphosphatidic acid-rich membranes contained within multivesicular late endosomes regulates cholesterol transport, presumably by acting as a collection and distribution device. The results also suggest that similar endosomal defects accompany the anti-phospholipid syndrome and NPC.

Targeting of SCG10 to the area of the Golgi complex is mediated by its NH2-terminal region.

SCG10 is a neuronal growth-associated protein that is concentrated in the growth cones of developing neurons. SCG10 shows a high degree of sequence homology to the ubiquitous phosphoprotein stathmin, which has been recently identified as a factor that destabilizes microtubules by increasing their catastrophe rate. Whereas stathmin is a soluble cytosolic protein, SCG10 is membrane-associated, indicating that the protein acts in a distinct subcellular compartment. Identifying the precise intracellular distribution of SCG10 as well as the mechanisms responsible for its specific targeting will contribute to elucidating its function. The main structural feature distinguishing the two proteins is that SCG10 contains an NH2-terminal extension of 34 amino acids. In this study, we have examined the intracellular distribution of SCG10 in PC12 cells and in transfected COS-7 cells and the role of the NH2-terminal domain in membrane-binding and intracellular targeting. SCG10 was found to be localized to the Golgi complex region. We show that the NH2-terminal region (residues 1-34) was necessary for membrane targeting and Golgi localization. Fusion proteins consisting of the NH2-terminal 34 amino acids of SCG10 and the related protein stathmin or the unrelated protein, beta-galactosidase, accumulated in the Golgi, demonstrating that this sequence was sufficient for Golgi localization. Biosynthetic labeling of transfected COS-7 cells with [3H]palmitic acid revealed that two cysteine residues contained within the NH2-terminal domain were sites of palmitoylation.

Structure of phaseolin at 2.2 A resolution. Implications for a common vicilin/legumin structure and the genetic engineering of seed storage proteins.

The refinement to 2.2 A resolution of the three-dimensional structure of the seed storage protein phaseolin from the French bean (Phaseolus vulgaris) via an alternative crystal form is described. The refined structure reveals details of the molecule hitherto unobserved and in particular we identify the structural role of conserved residues within the broader 7 S (vicilin) family of seed storage proteins. On this basis we are able to postulate a canonical model for the structure of the 7 S proteins. This model in turn provides a means for interpreting the structure of the 11 S (legumin) family of seed storage proteins, for which no X-ray diffraction data are available. The 11 S proteins are shown to bear a much closer relationship to the 7 S proteins than was previously recognized. The canonical model of the 7 S protein structure also provides a basis for proposing engineered mutations of these proteins with the goal of enhancing nutritional and functional properties.