Background
For the first time the expression of the ion transport protein sodium/potassium-ATPase and its isoforms was analyzed in the human cochlea using light- and confocal microscopy as well as super-resolution structured illumination microscopy. It may increase our understanding of its role in the propagation and processing of action potentials in the human auditory nerve and how electric nerve responses are elicited from auditory prostheses. Material and
Conclusion
The human auditory nerve displays distinct morphologic features represented in its molecular expression. It was found that electric signals generated via hair cells may not go uninterrupted across the spiral ganglion, but are locally processed. This may be related to particular filtering properties in the human acoustic pathway.
Material and methods
Archival human cochlear sections were obtained from trans-cochlear surgeries. Antibodies against the Na/K-ATPase β1 isoform together with α1 and α3 were used for immunohistochemistry. An algorithm was applied to assess the expression in various domains.
Methods
Archival human cochlear sections were obtained from trans-cochlear surgeries. Antibodies against the Na/K-ATPase β1 isoform together with α1 and α3 were used for immunohistochemistry. An algorithm was applied to assess the expression in various domains.
Results
Na/K ATPase β1 subunit was expressed, mostly combined with the α1 isoform. Neurons expressed the β1 subunit combined with α3, while satellite glial cells expressed the α1 isoform without recognized association with β1. Types I and II spiral ganglion neurons and efferent fibers expressed the Na/K-ATPase α3 subunit. Inner hair cells, nerve fibers underneath, and efferent and afferent fibers in the organ of Corti also expressed α1. The highest activity of Na/K-ATPase β1 was at the inner hair cell/nerve junction and spiral prominence.