Visualization and clinical relevance of the endolymphatic duct and sac in Ménière's disease.

Background: Ménière's disease (MD) is a chronic inner ear disorder with a multifactorial etiology. Decreased visualization of the endolymphatic duct (ED) and sac (ES) is thought to be associated with MD, although controversy exists about whether this finding is specific to MD. Recent literature has revealed that two distinct ES pathologies, developmental hypoplasia and epithelial degeneration, can be distinguished in MD using the angular trajectory of the vestibular aqueduct (ATVA) or ED-ES system as a radiographic surrogate marker.

Quality of life after intratympanic steroid injection for Ménière's disease.

Objective: This study explores how treatment with intratympanic steroid injection affects quality of life, as well as several subjective complaints in patients with Ménière's disease.

Methods: Patients filled in the Ménière's Disease Outcome Questionnaire (MDOQ) and answered questions about subjective complaints. Scores before and after treatment were compared using paired tests.

Hydropic Ear Disease: Correlation Between Audiovestibular Symptoms, Endolymphatic Hydrops and Blood-Labyrinth Barrier Impairment.

To investigate the correlation between clinical features and MRI-confirmed endolymphatic hydrops (EH) and blood-labyrinth barrier (BLB) impairment. Retrospective cross-sectional study. Vertigo referral center (Haga Teaching Hospital, The Hague, the Netherlands).

Septorhinoplasty and Septoplasty: Outcomes of a Large Cohort Using Autologous Versus Homologous Cartilage, 1999-2019.

This study describes the complication rate and use of autologous and/or homologous cartilage in a large 20-year cohort of septo(rhino)plasty surgeries in a Dutch hospital, in relation to postoperative complications of septo(rhino)plasty surgery described in previous studies. A retrospective medical chart review was conducted. 2606 patients, mean age 34.

The ubiquitin-associated (UBA) domain of SCCRO/DCUN1D1 protein serves as a feedback regulator of biochemical and oncogenic activity.

Amplification of squamous cell carcinoma-related oncogene (SCCRO) activates its function as an oncogene in a wide range of human cancers. The oncogenic activity of SCCRO requires its potentiating neddylation domain, which regulates its E3 activity for neddylation. The contribution of the N-terminal ubiquitin-associated (UBA) domain to SCCRO function remains to be defined.

SCCRO3 (DCUN1D3) antagonizes the neddylation and oncogenic activity of SCCRO (DCUN1D1).

The activity of cullin-RING type ubiquitination E3 ligases is regulated by neddylation, a process analogous to ubiquitination that culminates in covalent attachment of the ubiquitin-like protein Nedd8 to cullins. As a component of the E3 for neddylation, SCCRO/DCUN1D1 plays a key regulatory role in neddylation and, consequently, cullin-RING ligase activity. The essential contribution of SCCRO to neddylation is to promote nuclear translocation of the cullin-ROC1 complex.

Oncogenic function of SCCRO5/DCUN1D5 requires its Neddylation E3 activity and nuclear localization.

Purpose: To determine mechanisms by which SCCRO5 (aka DCUN1D5) promotes oncogenesis.

Experimental Design: SCCRO5 mRNA and protein expression were assessed in 203 randomly selected primary cancer tissue samples, matched histologically normal tissues, and cell lines by use of real-time PCR and Western blot analysis. SCCRO5 overexpression was correlated with survival.

REM-associated nasal obstruction: a study with acoustic rhinometry during sleep.

Objective: Obstructive sleep apnea events are more common in REM sleep, although there is no relationship between sleep phase and pharyngeal airway status. We studied the patency of the nasal airway during REM and non-REM sleep with the use of acoustic rhinometry.

Methods: Serial acoustic rhinometric assessment of nasal cross-sectional area was performed in 10 subjects, before sleep and during REM and non-REM sleep.

SCCRO (DCUN1D1) is an essential component of the E3 complex for neddylation.

Covalent modification of cullins by the ubiquitin-like protein NEDD8 (neddylation) regulates protein ubiquitination by promoting the assembly of cullin-RING ligase E3 complexes. Like ubiquitination, neddylation results from an enzymatic cascade involving the sequential activity of a dedicated E1 (APPBP1/Uba3), E2 (Ubc12), and an ill-defined E3. We show that SCCRO (also known as DCUN1D1) binds to the components of the neddylation pathway (Cullin-ROC1, Ubc12, and CAND1) and augments but is not required for cullin neddylation in reactions using purified recombinant proteins.