Comparison of the efficacy of a neutral wrist splint and wrist splint with lumbrical unit for the treatment of patients with carpal tunnel syndrome

Purpose: The purpose of this study was to compare the effect of a neutral wrist splint or a wrist splint with an additional metacarpophalangeal (MCP) unit on pain, function, grip and pinch strength in patients with mild-to-moderate carpal tunnel syndrome (CTS). Methods: Twenty four patients received conservative treatment using either the neutral wrist splint or wrist splint with the MCP unit for a period of 6 weeks. Primary outcome measures were pain, function, grip and pinch strength. Data was collected immediately before and after using the two types of splints at baseline (0 weeks) and 6 weeks. Statistical analysis was performed using the paired t-test and independent T-test. Results: Compared to baseline, both the neutral wrist splint and the wrist splint with an MCP unit significantly decreased pain, increased function and pinch and grip strength. Comparisons of the two types of splints for grip (P =0.675) and pinch strength (P =0.650) revealed that there were no significant differences between the two after 6 weeks of wear. However, there were significant differences in pain levels (P =0.022) and the DASH score (P =0.027) between the two types of splints from baseline to 6 weeks. Conclusion: The wrist splint with an MCP unit was more effective than the neutral wrist splint in pain reduction and improvement of function

Proton transfer in the oxidative half-reaction of pentaerythritol tetranitrate reductase

The roles of His181, His184 and Tyr186 in PETN reductase have been examined by mutagenesis, spectroscopic and stopped-flow kinetics, and by determination of crystallographic structures for the Y186F PETN reductase and reduced wild-type enzyme—progesterone complex. Residues His181 and His184 are important in the binding of coenzyme, steroids, nitroaromatic ligands and the substrate 2-cyclohexen-1-one. The H181A and H184A enzymes retain activity in reductive and oxidative half-reactions, and thus do not play an essential role in catalysis. Ligand binding and catalysis is not substantially impaired in Y186F PETN reductase, which contrasts with data for the equivalent mutation (Y196F) in Old Yellow Enzyme. The structure of Y186F PETN reductase is identical to wild-type enzyme, with the obvious exception of the mutation. We show in PETN reductase that Tyr186 is not a key proton donor in the reduction of α/β unsaturated carbonyl compounds. The structure of two electron-reduced PETN reductase bound to the inhibitor progesterone mimics the catalytic enzyme-steroid substrate complex and is similar to the structure of the oxidized enzyme-inhibitor complex. The reactive C1-C2 unsaturated bond of the steroid is inappropriately orientated with the flavin N5 atom for hydride transfer. With steroid substrates, the productive conformation is achieved by orientating the steroid through flipping by 180°, consistent with known geometries for hydride transfer in flavoenzymes. Our data highlight mechanistic differences between Old Yellow Enzyme and PETN reductase and indicate that catalysis requires a metastable enzyme-steroid complex and not the most stable complex observed in crystallographic studies