A direct comparison between extracted tooth and filter-membrane biofilm models of endodontic irrigation using Enterococcus faecalis.

Endodontic restorations often fail due to inadequate disinfection of the root canal even though the antimicrobial irrigants used have been shown to be capable of killing the bacterium frequently implicated in this complication, Enterococcus faecalis (Ef). Extracted human teeth were root-prepared and filled with a liquid culture of Ef. Following incubation, the root canals were irrigated with 1% sodium hypochlorite (NaOCl), electrochemically activated water or saline control.

Oro-facial injuries and mouthguard use in elite female field hockey players.

The objectives of this study were to assess the prevalence of oro-facial injuries, frequency of mouthguard use and players' attitudes towards the use of mouthguards among elite English female field hockey players. All 140 players of the English Hockey Association female Premiere League were asked to complete a questionnaire. Main outcome measures were prevalence of oro-facial injuries, frequency of wearing of mouthguards and attitudes to mouthguard wearing.

Quinacrine blocks PrP (106-126)-formed channels.

We investigated the action of the acridine derivative, quinacrine (QC), which has been shown to act as a noncompetitive channel inhibitor. The main effects of QC are voltage- and concentration-dependent changes in the kinetics of the prion protein fragment (PrP[106-126])-formed cation channels. The current-voltage relationships show that the maximal current (I) was not affected whereas the physiologically important mean current (I') was reduced as a result of changes in channel kinetics.

Cu2+-induced modification of the kinetics of A beta(1-42) channels.

We found that the amyloid beta peptide A beta(1-42) is capable of interacting with membrane and forming heterogeneous ion channels in the absence of any added Cu2+ or biological redox agents that have been reported to mediate A beta(1-42) toxicity. The A beta(1-42)-formed cation channel was inhibited by Cu2+ in cis solution ([Cu2+]cis) in a voltage- and concentration-dependent manner between 0 and 250 microM. The [Cu2+]cis-induced channel inhibition is fully reversible at low concentrations between 50 and 100 microM [Cu2+]cis and partially reversible at 250 microM [Cu2+]cis.

Channels formed with a mutant prion protein PrP(82-146) homologous to a 7-kDa fragment in diseased brain of GSS patients.

A major prion protein (PrP) mutant that forms amyloid fibrils in the diseased brain of patients with Gerstmann-Sträussler-Scheinker syndrome (GSS) is a fragment of 7 kDa spanning from residues 81-82 to 144-153 of PrP. Analysis of ionic membrane currents, recorded with a lipid bilayer technique, revealed that the wild-type fragment PrP(82-146) WT and the partially scrambled PrP(82-146) (127-146) SC are capable of forming heterogeneous ion channels that are similar to those channels formed with PrP(106-126). In contrast, PrP(82-146) peptides in which the region from residue 106 to 126 had been scrambled (SC) showed a reduction in interaction with lipid membranes and did not form channels.

Heterogeneous amyloid-formed ion channels as a common cytotoxic mechanism: implications for therapeutic strategies against amyloidosis.

The amyloidoses consist of human and animal chronic, progressive, and sometimes fatal diseases that are characterized by the deposition of insoluble proteinaceous amyloid fibrils in various tissues. Despite the biochemical diversity of amyloids, they share certain properties. The amphipathic and the charged nature of many amyloid-forming peptides point to their intrinsic ability to form diverse beta-sheet-based aggregates and channel types in negatively charged membranes.