A Two-year Outcome of Various Techniques of Discectomy On Complications: A Multicentric Retrospective Study

Objective Various techniques of performing lumbar discectomy are prevalent, each having its rationale and claimed benefits. The authors ventured to assess the total complication rate of lumbar discectomy as well as the complication rates of individual complications, namely CSF leaks, superficial wound infections, deep wound infections, recurrence rates, re-operation rates, and wrong level surgery. Methods This was a retrospective study of patients operated using open discectomy (OD), microdiscectomy (MD), microendoscopic discectomy (MED), interlaminar endoscopic lumbar discectomy (IELD), transforaminal endoscopic lumbar discectomy (TELD), and Destandau techniques (DT) with a minimum follow-up of 2 years. The inclusion criteria were age>15 years, failed conservative treatment for 4-6 weeks, and the involvement of a single lumbar level. Results There is no statistically significant association between surgical technique and complications. The total complication rate was 12.89% in 946 operated cases. The most common complication was recurrence (5.81%), followed by re-operation (3.69%), CSF leak (1.90%), wrong level surgery (0.63%), superficial infection (0.52%) and deep infection (0.31%). There were minor differences in the incidence of complications between techniques. Conclusion This is the first study to compare the complication rates of all the prevalent discectomy techniques across the globe in 946 patients. Although there were minor differences in incidences of complications between individual techniques, there was no statistical significance. The various rates of individual complications provide a reference value for future studies related to complications following discectomy

Bilateral infraorbital nerve blocks decrease postoperative pain but do not reduce time to discharge following outpatient nasal surgery

While infraorbital nerve blocks have demonstrated analgesic benefits for pediatric nasal and facial plastic surgery, no studies to date have explored the effect of this regional anesthetic technique on adult postoperative recovery. We designed this study to test the hypothesis that infraorbital nerve blocks combined with a standardized general anesthetic decrease the duration of recovery following outpatient nasal surgery. At a tertiary care university hospital, healthy adult subjects scheduled for outpatient nasal surgery were randomly assigned to receive bilateral infraorbital injections with either 0.5% bupivacaine (Group IOB) or normal saline (Group NS) using an intraoral technique immediately following induction of general anesthesia. All subjects underwent a standardized general anesthetic regimen and were transported to the recovery room following tracheal extubation. The primary outcome was the duration of recovery (minutes) from recovery room admission until actual discharge to home. Secondary outcomes included average and worst pain scores, nausea and vomiting, and supplemental opioid requirements. Forty patients were enrolled. A statistically significant difference in mean [SD] recovery room duration was not observed between Groups IOB and NS (131 [61] min vs 133 [58] min, respectively; P = 0.77). Subjects in Group IOB did experience a reduction in average pain on a 0–100 mm scale (mean [95% confidence interval]) compared to Group NS (−11 [−21 to 0], P = 0.047), but no other comparison of secondary outcomes was statistically significant. When added to a standardized general anesthetic, bilateral IOB do not decrease actual time to discharge following outpatient nasal surgery despite a beneficial effect on postoperative pain

Roles of residues in the interface of transient protein-protein complexes before complexation

Transient protein-protein interactions play crucial roles in all facets of cellular physiology. Here, using an analysis on known 3-D structures of transient protein-protein complexes, their corresponding uncomplexed forms and energy calculations we seek to understand the roles of protein-protein interfacial residues in the unbound forms. We show that there are conformationally near invariant and evolutionarily conserved interfacial residues which are rigid and they account for ∼65% of the core interface. Interestingly, some of these residues contribute significantly to the stabilization of the interface structure in the uncomplexed form. Such residues have strong energetic basis to perform dual roles of stabilizing the structure of the uncomplexed form as well as the complex once formed while they maintain their rigid nature throughout. This feature is evolutionarily well conserved at both the structural and sequence levels. We believe this analysis has general bearing in the prediction of interfaces and understanding molecular recognition

Progressive dry-core-wet-rim hydration trend in a nested-ring topology of protein binding interfaces

<p>Abstract</p> <p>Background</p> <p>Water is an integral part of protein complexes. It shapes protein binding sites by filling cavities and it bridges local contacts by hydrogen bonds. However, water molecules are usually not included in protein interface models in the past, and few distribution profiles of water molecules in protein binding interfaces are known.</p> <p>Results</p> <p>In this work, we use a tripartite protein-water-protein interface model and a nested-ring atom re-organization method to detect hydration trends and patterns from an interface data set which involves immobilized interfacial water molecules. This data set consists of 206 obligate interfaces, 160 non-obligate interfaces, and 522 crystal packing contacts. The two types of biological interfaces are found to be drier than the crystal packing interfaces in our data, agreeable to a hydration pattern reported earlier although the previous definition of immobilized water is pure distance-based. The biological interfaces in our data set are also found to be subject to stronger water exclusion in their formation. To study the overall hydration trend in protein binding interfaces, atoms at the same burial level in each tripartite protein-water-protein interface are organized into a ring. The rings of an interface are then ordered with the core atoms placed at the middle of the structure to form a nested-ring topology. We find that water molecules on the rings of an interface are generally configured in a dry-core-wet-rim pattern with a progressive level-wise solvation towards to the rim of the interface. This solvation trend becomes even sharper when counterexamples are separated.</p> <p>Conclusions</p> <p>Immobilized water molecules are regularly organized in protein binding interfaces and they should be carefully considered in the studies of protein hydration mechanisms.</p

An overview of the utilisation of microalgae biomass derived from nutrient recycling of wet market wastewater and slaughterhouse wastewater

Microalgae have high nutritional values for aquatic organisms compared to fish meal, because microalgae cells are rich in proteins, lipids, and carbohydrates. However, the high cost for the commercial production of microalgae biomass using fresh water or artificial media limits its use as fish feed. Few studies have investigated the potential of wet market wastewater and slaughterhouse wastewater for the production of microalgae biomass. Hence, this study aims to highlight the potential of these types of wastewater as an alternative superior medium for microalgae biomass as they contain high levels of nutrients required for microalgae growth. This paper focuses on the benefits of microalgae biomass produced during the phycore-mediation of wet market wastewater and slaughterhouse wastewater as fish feed. The extraction techniques for lipids and proteins as well as the studies conducted on the use of microalgae biomass as fish feed were reviewed. The results showed that microalgae biomass can be used as fish feed due to feed utilisation efficiency, physiological activity, increased resistance for several diseases, improved stress response, and improved protein retention

Effect of Fibrin Glue on the Biomechanical Properties of Human Descemet's Membrane

10.1371/journal.pone.0037456PLoS ONE75