Severity of tongue base collapse in various body positions in patients with obstructive sleep apnea: A trajectory analysis.

BACKGROUND: Drug-induced sleep endoscopy (DISE) is used for evaluating upper airway anatomy and determining airway obstruction patterns. It is typically performed with the patient in the supine position. Airway collapse severity is influenced by body position and level of consciousness; the resultant dynamic changes may vary across patients. In this study, we evaluated the severity of upper airway collapse through awake endoscopy and DISE and identified factors affecting the pattern of airway collapse severity. METHODS: This study included 66 patients with obstructive sleep apnea. The patients underwent type 1 polysomnography, tongue strength assessment, awake endoscopy in the sitting and supine positions, and DISE. Group-based trajectory modeling was performed to identify patients with different collapse severity patterns in different body positions and at different levels of consciousness. RESULTS: Patient with similar severity trajectory were assigned to the same group. Two different severity trajectories (group 1 and group 2) were identified at the tongue base level. Tongue depression strength varied significantly between groups 1 and 2 (47.00 vs. 35.00 kPa; P = .047). During awake endoscopy, collapse severity was significantly higher in group 2 than in group 1. Group 1 had lower rapid eye movement/nonrapid eye movement apnea-hypopnea index ratios and higher tongue depression strength than did group 2. CONCLUSION: In patients with obstructive sleep apnea, tongue strength may vary depending on body position. Our results should be interpreted with caution because of the limited sample size. Future studies should investigate the effect of oropharyngeal rehabilitation on tongue strength and collapse severity.

Oropharyngeal Rehabilitation for Patients With Moderate to Severe Obstructive Sleep Apnea After Transoral Robotic Surgery.

OBJECTIVE: To determine whether combined transoral robotic surgery and postoperative oropharyngeal rehabilitation are effective for reducing the severity of obstructive sleep apnea. STUDY DESIGN: A quasi-experimental study enrolled participants without blinding between May 2019 and April 2021. SETTING: Single-center study at National Cheng Kung University Hospital. METHODS: Patients with moderate to severe obstructive sleep apnea who were otherwise healthy were recruited from the ear, nose, and throat department at National Cheng Kung University Hospital. The group undergoing transoral robotic surgery with oropharyngeal rehabilitation (n = 18) received a 12-week intervention consisting of home-based rehabilitation exercises following surgery; the transoral robotic surgery group (n = 17) received surgery only; and the control group (n = 15) received conservative treatment, such as continuous positive airway pressure therapy or other oral appliance therapy. Polysomnography data and tongue muscle performance were measured before and after the interventions. RESULTS: The group that underwent transoral robotic surgery with oropharyngeal rehabilitation exhibited significantly improved tongue protrusion strength as compared with the transoral robotic surgery-only group, as well as significantly improved apnea-hypopnea index in the supine position vs the control group. CONCLUSION: In this study, we demonstrated the synergistic effects of transoral robotic surgery and postoperative oropharyngeal rehabilitation for adult patients with obstructive sleep apnea. Objective records should be used to monitor home-based rehabilitation exercises and examine the lasting synergistic effects.

Genetic requirements and meiotic function of phosphorylation of the yeast axial element protein Red1.

The synaptonemal complex (SC) is a meiosis-specific tripartite structure that forms between two homologous chromosomes; it consists of a central region and two parallel lateral elements. Lateral elements also are called axial elements prior to synapsis. In Saccharomyces cerevisiae, Red1, Hop1, and Mek1 are structural components of axial/lateral elements. The red1/mek1/hop1 mutants all exhibit reduced levels of interhomolog recombination and produce no viable spores. Red1 is a phosphoprotein. Several earlier reports proposed that phosphorylated Red1 plays important roles in meiosis, including in signaling meiotic DNA damage or in preventing exit from the pachytene chromosomes. We report here that the phosphorylation of Red1 is carried out in CDC28-dependent and CDC28-independent manners. In contrast to previous results, we found Red1 phosphorylation to be independent of meiotic DNA recombination, the Mec1/Tel1 DNA damage checkpoint kinases, and the Mek1 kinase. To functionally validate the phosphorylation of Red1, we mapped the phosphorylation sites on this protein. A red1(14A) mutant showing no detectable Red1 phosphorylation did not exhibit decreased sporulation efficiency, defects in viable spore production, or defects in meiotic DNA damage checkpoints. Thus, our results suggest that the phosphorylation of Red1 is not essential for its functions in meiosis.

Yeast axial-element protein, Red1, binds SUMO chains to promote meiotic interhomologue recombination and chromosome synapsis.

The synaptonemal complex (SC) is a tripartite protein structure consisting of two parallel axial elements (AEs) and a central region. During meiosis, the SC connects paired homologous chromosomes, promoting interhomologue (IH) recombination. Here, we report that, like the CE component Zip1, Saccharomyces cerevisiae axial-element structural protein, Red1, can bind small ubiquitin-like modifier (SUMO) polymeric chains. The Red1-SUMO chain interaction is dispensable for the initiation of meiotic DNA recombination, but it is essential for Tel1- and Mec1-dependent Hop1 phosphorylation, which ensures IH recombination by preventing the inter-sister chromatid DNA repair pathway. Our results also indicate that Red1 and Zip1 may directly sandwich the SUMO chains to mediate SC assembly. We suggest that Red1 and SUMO chains function together to couple homologous recombination and Mec1-Tel1 kinase activation with chromosome synapsis during yeast meiosis.

Kinetic and structural properties of triosephosphate isomerase from Helicobacter pylori.

Triosephosphate isomerase (TIM) catalyzes the interconversion between dihydroxyacetone phosphate and D-glyceraldehyde-3-phosphate in the glycolysis-gluconeogenesis metabolism pathway. The Helicobacter pylori TIM gene (HpTIM) was cloned, and HpTIM was expressed and purified. The enzymatic activity of HpTIM for the substrate GAP was determined (K(m) = 3.46 +/- 0.23 mM and k(cat) = 8.8 x 10(4) min(-1)). The crystal structure of HpTIM was determined by molecular replacement at 2.3 A resolution. The overall structure of HpTIM was (beta/alpha)beta(beta/alpha)(6), which resembles the common TIM barrel fold, (beta/alpha)(8); however, a helix is missing after the second beta-strand. The conformation of loop 6 and binding of phosphate ion suggest that the determined structure of HpTIM was in the "closed" state. A highly conserved Arg-Asp salt bridge in the "DX(D/N)G" motif of most TIMs is absent in HpTIM because the sequence of this motif is "(211)SVDG(214)." To determine the significance of this salt bridge to HpTIM, four mutants, including K183S, K183A, D213Q, and D213A, were constructed and characterized. The results suggest that this conserved salt bridge is not essential for the enzymatic activity of HpTIM; however, it might contribute to the conformational stability of HpTIM.