Scapular Dyskinesis Is Not an Isolated Risk Factor for Shoulder Injury in Athletes: A Systematic Review and Meta-analysis.

BACKGROUND: Scapular dyskinesis has been considered a risk factor for athletic shoulder injury; however, findings in the prospective literature have demonstrated mixed results. PURPOSE: To determine if scapular dyskinesis increases the risk of shoulder injury in athletes. STUDY DESIGN: Meta-analysis. METHODS: A systematic search was conducted on the MEDLINE, CINAHL Plus, SPORTDiscus, and Embase databases to identify prospective studies examining scapular dyskinesis and shoulder injury risk in athletes. Studies were included if they assessed participants using a dynamic scapular assessment at baseline and monitored for the development of shoulder injury. Data from the studies were subject to meta-analysis using the Mantel-Haenszel method to produce a pooled risk ratio. RESULTS: Seven studies were eligible for inclusion, resulting in 212 shoulder injuries observed across 923 athletes. Scapular dyskinesis was present in 46% of participants, and these athletes had an injury rate of 25%. The presence of scapular dyskinesis displayed a trend to increase the risk of shoulder injury, but this was not statistically significant (risk ratio, 1.07; 95% CI, 0.85-1.34; P = .59). CONCLUSION: Scapular dyskinesis was not significantly associated with the development of shoulder injury in athletes. REGISTRATION: CRD42019133089 (PROSPERO).

Characterization of recombinant dihydrodipicolinate synthase from the bread wheat Triticum aestivum.

MAIN CONCLUSION: Recombinant wheat DHDPS was produced for the first time in milligram quantities and shown to be an enzymatically active tetramer in solution using analytical ultracentrifugation and small angle X-ray scattering. Wheat is an important cereal crop with an extensive role in global food supply. Given our rapidly growing population, strategies to increase the nutritional value and production of bread wheat are of major significance in agricultural science to satisfy our dietary requirements. Lysine is one of the most limiting essential amino acids in wheat, thus, a thorough understanding of lysine biosynthesis is of upmost importance to improve its nutritional value. Dihydrodipicolinate synthase (DHDPS; EC 4.3.3.7) catalyzes the first committed step in the lysine biosynthesis pathway of plants. Here, we report for the first time the expression and purification of recombinant DHDPS from the bread wheat Triticum aestivum (Ta-DHDPS). The optimized protocol yielded 36 mg of > 98% pure recombinant Ta-DHDPS per liter of culture. Enzyme kinetic studies demonstrate that the recombinant Ta-DHDPS has a KM (pyruvate) of 0.45 mM, KM (l-aspartate-4-semialdehyde) of 0.07 mM, kcat of 56 s-1, and is inhibited by lysine (IC 50 LYS of 0.033 mM), which agree well with previous studies using labor-intensive purification from wheat suspension cultures. We subsequently employed circular dichroism spectroscopy, analytical ultracentrifugation and small angle X-ray scattering to show that the recombinant enzyme is folded with 60% α/ß structure and exists as a 7.5 S tetrameric species with a Rg of 33 Å and Dmax of 118 Å. This study is the first to report the biophysical properties of the recombinant Ta-DHDPS in aqueous solution and offers an excellent platform for future studies aimed at improving nutritional value and primary production of bread wheat.

Quaternary Structure Analyses of an Essential Oligomeric Enzyme.

Here, we review recent studies aimed at defining the importance of quaternary structure to a model oligomeric enzyme, dihydrodipicolinate synthase. This will illustrate the complementary and synergistic outcomes of coupling the techniques of analytical ultracentrifugation with enzyme kinetics, in vitro mutagenesis, macromolecular crystallography, small angle X-ray scattering, and molecular dynamics simulations, to demonstrate the role of subunit self-association in facilitating protein dynamics and enzyme function. This multitechnique approach has yielded new insights into the molecular evolution of protein quaternary structure.