A Mid-scala Cochlear Implant Electrode Design Achieves a Stable Post-surgical Position in the Cochlea of Patients Over Time-A Prospective Observational Study.

INTRODUCTION: Cochlear implant (CI) electrode design impacts the clinical performance of patients. Stability and the occurrence of electrode array migration, which is the postoperative movement of the electrode array, were investigated using a mid-scalar electrode array and postoperative image analysis. METHODS: A prospective observational study was conducted. A mid-scalar electrode was surgically placed using a mastoidectomy, followed by a posterior tympanotomy and an extended round-window or cochleostomy insertion. A few days after surgery and 3 months later Cone Beam Computed Tomography (CBCT) was performed. The two different CBCT's were fused, and the differences between the electrode positions in three dimensions were calculated (the migration). A migration greater than 0.5 mm was deemed clinically relevant. RESULTS: Fourteen subjects participated. The mid-scalar electrode migrated in one patient (7%). This did not lead to the extrusion of an electrode contact. The mean migration of every individual electrode contact in all patients was 0.36 mm (95% confidence interval 0.22-0.50 mm), which approximates to the estimated measurement error of the CBCT technique. CONCLUSION: A mid-scalar electrode array achieves a stable position in the cochlea in a small but representative group of patients. The methods applied in this work can be used for providing postoperative feedback for surgeons and for benchmarking electrode designs.

A Proposed Method for Accurate 3D Analysis of Cochlear Implant Migration Using Fusion of Cone Beam CT.

INTRODUCTION: The goal of this investigation was to compare fusion of sequential cone beam computerized tomography (CT) volumes to the gold standard (fiducial registration) in order to be able to analyze clinical cochlear implant (CI) migration with high accuracy in three dimensions. MATERIALS AND METHODS: Paired cone beam CT volumes were performed on five human cadaver temporal bones and one human subject. These volumes were fused using 3D Slicer 4 and BRAINSFit software. Using a gold standard fiducial technique, the accuracy, robustness, and performance time of the fusion process were assessed. RESULTS: This proposed fusion protocol achieves a subvoxel median Euclidean distance of 0.05 mm in human cadaver temporal bones and 0.16 mm (mean) when applied to the described in vivo human synthetic data set in over 95% of all fusions. Performance times are <2 min. CONCLUSION: Here, a new and validated method based on existing techniques is described, which could be used to accurately quantify migration of CI electrodes.

Revisiting Place-Pitch Match in CI Recipients Using 3D Imaging Analysis.

OBJECTIVE: To improve the estimation of the perceived pitch in a single-sided deaf cochlear implant (CI) listener by using accurate 3-dimensional (3D) image analysis of the cochlear electrode positions together with the predicted tonotopical function for humans. METHODS: An SSD CI user underwent a Cone-Beam computed tomography (CBCT) scan. Electrode contacts were marked in 3D space in relation to the nearest point on the cochlear lateral wall. Distance to the base of the lateral wall was calculated and plotted against the place-pitch function for humans. An adaptive procedure was used to elicit the perceived pitch of electrically evoked stimulation by matching it with a contralateral acoustic pitch. RESULTS: The electrically evoked pitch percept matched well with the calculated frequency. The median mismatch in octaves was 0.12 for our method in comparison to 0.69 using the conventional Stenvers view. CONCLUSION: A method of improved image analysis is described that can be used to predict the pitch percept on corresponding cochlear electrode positions. This method shows the potential of 3D imaging in CI fitting optimization.

Domain swapping in the human histamine H1 receptor.

G-protein-coupled receptors (GPCRs) represent the largest family of receptors involved in transmembrane signaling. Although these receptors were generally believed to be monomeric entities, accumulating evidence supports the presence of GPCRs in multimeric forms. Here, using immunoprecipitation as well as time-resolved fluorescence resonance energy transfer to assess protein-protein interactions in living cells, we unambiguously demonstrate the occurrence of dimerization of the human histamine H(1) receptor. We also show the presence of domain-swapped H(1) receptor dimers in which there is the reciprocal exchange of transmembrane domain TM domains 6 and 7 between the receptors present in the dimer. Mutation of aspartate(107) in transmembrane (TM) 3 or phenylalanine(432) in TM6 to alanine results in two radioligand-binding-deficient mutant H(1) receptors. Coexpression of H(1)D(107) A and H(1)F(432)A, however, results in a reconstituted radioligand binding site that exhibits a pharmacological profile that corresponds to the wild-type H(1) receptor. Interestingly, the H(1) receptor radioligands [(3)H]mepyramine and [(3)H]-(-)-trans-1-phenyl-3-N,N-dimethylamino-1,2,3,4-tetrahydronaphthalene show differential saturation binding values (B(max)) for wild-type H(1) receptors but not for the radioligand binding site that is formed upon coexpression of H(1) D(107)A and H(1) F(432)A receptors, suggesting the presence of different H(1) receptor populations.